eF-site ID 6nra-ABCDEFGHIJKLMNOP PDB Code 6nra Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Title hTRiC-hPFD Class1 (No PFD) Classification CHAPERONE Compound T-complex protein 1 subunit alpha Source (TCPQ_HUMAN) Sequence A:  TGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDV TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTS VVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYI NENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMV VDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLIS GYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQV VITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGI DDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLA NLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTS ASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGG GAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTL AVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSN GKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIK L B:  ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSS GRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK AAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHH KDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLD EGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSR VRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQL IYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTF DHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVL RGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEM LMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAG YDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITE SFQVKRQVLLSAAEAAEVILRVDNIIKAA C:  RESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMG GIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGT TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMIS TLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNI ALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVL RGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTD IEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKG ISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRP EELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTIL LRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASE MAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNC GASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGI WEPLAVKLQTYKTAVETAVLLLRIDDIVS D:  DRDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGK GDVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDG TTSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGI EILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSP MSVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVE GLVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIV VSDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSIL RDALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPV AHIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKT VTIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGG GAPEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTL AENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILE ELVVQPLLVSVSALTLATETVRSILKID E:  KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDK DGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVA IEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQ MAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKL IKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKH KLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQW GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR FSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVT IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSE NSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQ HVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE F:  EVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDG TTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKAL QFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTEA VVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLV LDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK SAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVV INQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGV ALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRS VTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGA GAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVL AQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAE VGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAG G:  TDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDG RGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGD GTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLA VNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLISQQK AFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVA GVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKDN AEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSK LPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQT SVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCTF ILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAI EMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDN AGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFV WEPAMVRINALTAASEAACLIVSVDETIKNPR H:  MLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMN KMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQ EQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYE IACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQY GNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGIS SSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITET KGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVT GGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATAL PRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAIS TIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGG ATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALA ENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDML EAGILDTYLGKYWAIKLATNAAVTVLRVDQ I:  MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVG LDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELAD LQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISG YRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKI IGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKA HGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFS LQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILA TGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIA KASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDE LILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVK RVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAE FARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPER KNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEA AITILRIDDLIKLH J:  ADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSS GRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEV GDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATK AAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHH KDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLD EGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSR VRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQL IYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTF DHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVL RGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEM LMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAG YDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITE SFQVKRQVLLSAAEAAEVILRVDNIIKA K:  NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLD PMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVG DGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDD MISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLA CNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDS CVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGES QTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVIT EKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIV SRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKAC TILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGG ASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLI QNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKE LGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSG L:  RDKPAQIRFSNISAAKAVADAIRTSLGPKGMDKMIQDGKG DVTITNDGATILKQMQVLHPAARMLVELSKAQDIEAGDGT TSVVIIAGSLLDSCTKLLQKGIHPTIISESFQKALEKGIE ILTDMSRPVELSDRETLLNSATTSLNSKVVSQYSSLLSPM SVNAVMKVIDPATATSVDLRDIKIVKKLGGTIDDCELVEG LVLTQKVSNSGITRVEKAKIGLIQFCLSAPKTDMDNQIVV SDYAQMDRVLREERAYILNLVKQIKKTGCNVLLIQKSILR DALSDLALHFLNKMKIMVIKDIEREDIEFICKTIGTKPVA HIDQFTADMLGSAELAEEVNLNGSGKLLKITGCASPGKTV TIVVRGSNKLVIEEAERSIHDALCVIRCLVKKRALIAGGG APEIELALRLTEYSRTLSGMESYCVRAFADAMEVIPSTLA ENAGLNPISTVTELRNRHAQGEKTAGINVRKGGISNILEE LVVQPLLVSVSALTLATETVRSILKIDDVVNTR M:  KSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDK DGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGD GTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVA IEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQ MAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKL IKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKH KLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQW GFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPR FSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVT IFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGA AEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSE NSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQ HVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE N:  AEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSG AGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGD GTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKA LQFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTE AVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGL VLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFY KSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFV VINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGG VALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPR SVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPG AGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKV LAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAA EVGVWDNYCVKKQLLHSCTVIATNILLVDEIMR O:  GTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVD GRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVG DGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQL AVNKIKEIAVTVKKADKVEQRKLLEKCAMTALSSKLISQQ KAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLV AGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEKD NAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLS KLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQ TSVNALSADVLGRCQVFEETQIGGERYNFFTGCPKAKTCT FILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGA IEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCD NAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAF VWEPAMVRINALTAASEAACLIVSVDETIKNPRS P:  AKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVIN HLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVG DGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRK AHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQYGNEVF LAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGISSSSVL HGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVL IKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVA DMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTP PVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLR GSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIE LAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGV KANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGIL DTYLGKYWAIKLATNAAVTVLRVDQIIMA Description Functional site 1) chain H residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 2) chain H residue 254 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 3) chain H residue 260 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 4) chain P residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 5) chain P residue 254 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 6) chain P residue 260 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 7) chain C residue 430 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 8) chain H residue 459 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 9) chain K residue 430 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 10) chain P residue 459 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 11) chain C residue 248 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 12) chain C residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 13) chain K residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 14) chain K residue 248 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 15) chain K residue 249 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 16) chain C residue 381 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI9 17) chain K residue 381 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI9 18) chain H residue 282-293 type prosite sequence AIADTGANVVVT description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT source prosite : PS00141 19) chain B residue 95-120 type prosite sequence VGDGTTSVTVLAAELLREAESLIAKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK source prosite : PS00107 20) chain D residue 49-61 type prosite sequence RTSLGPKGMDKMI description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 21) chain B residue 40-52 type prosite sequence KSTLGPKGMDKIL description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 22) chain E residue 49-61 type prosite sequence RTSLGPNGLDKMM description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 23) chain G residue 37-49 type prosite sequence RTTLGPRGMDKLI description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 24) chain H residue 44-56 type prosite sequence RTAYGPNGMNKMV description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 25) chain C residue 38-50 type prosite sequence RTCLGPKSMMKML description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 26) chain A residue 33-45 type prosite sequence KSSLGPVGLDKML description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 27) chain F residue 35-47 type prosite sequence RTNLGPKGTMKML description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 28) chain D residue 70-86 type prosite sequence ITNDGATILKQMQVLHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 29) chain F residue 56-72 type prosite sequence LTKDGNVLLHEMQIQHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 30) chain C residue 59-75 type prosite sequence MTNDGNAILREIQVQHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 31) chain E residue 70-86 type prosite sequence VTNDGATILSMMDVDHQ description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 32) chain G residue 58-74 type prosite sequence ISNDGATILKLLDVVHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 33) chain A residue 54-70 type prosite sequence ITNDGATILKLLEVEHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 34) chain H residue 65-81 type prosite sequence VTNDAATILRELEVQHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 35) chain B residue 63-79 type prosite sequence VTNDGATILKNIGVDNP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 36) chain E residue 98-106 type prosite sequence QDDEIGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 37) chain C residue 87-95 type prosite sequence QDEEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 38) chain F residue 84-92 type prosite sequence QDDITGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 39) chain D residue 98-106 type prosite sequence QDIEAGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 40) chain A residue 82-90 type prosite sequence QDKEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 41) chain H residue 93-101 type prosite sequence QEQEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 42) chain G residue 86-94 type prosite sequence QDAEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 43) chain B residue 91-99 type prosite sequence QDDEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 44) chain H residue 23 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 45) chain P residue 23 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 46) chain O residue 67 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 47) chain O residue 320 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 48) chain N residue 199 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 49) chain N residue 365 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 50) chain N residue 377 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 51) chain N residue 388 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 52) chain H residue 30 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 53) chain P residue 30 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 54) chain M residue 346 type MOD_RES sequence S description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 55) chain M residue 539 type MOD_RES sequence S description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 56) chain L residue 288 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 57) chain L residue 302 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 58) chain L residue 319 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 59) chain L residue 326 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 60) chain P residue 269 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 61) chain P residue 317 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 62) chain M residue 214 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 63) chain M residue 265 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 64) chain M residue 275 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 65) chain M residue 279 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 66) chain M residue 392 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 67) chain H residue 162 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 68) chain H residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 69) chain H residue 269 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 70) chain H residue 317 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 71) chain P residue 162 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 72) chain P residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 73) chain H residue 318 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 74) chain H residue 400 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 75) chain H residue 466 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 76) chain P residue 318 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 77) chain P residue 400 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 78) chain P residue 466 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 79) chain H residue 505 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 80) chain P residue 505 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5 81) chain J residue 248 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5

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