9CF0

Parasitella parasitica Fanzor (PpFz) State 1

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0003729	molecular_function	mRNA binding
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005758	cellular_component	mitochondrial intermembrane space
C	0006457	biological_process	protein folding
C	0006974	biological_process	DNA damage response
C	0009267	biological_process	cellular response to starvation
C	0015031	biological_process	protein transport
C	0016018	molecular_function	cyclosporin A binding
C	0016853	molecular_function	isomerase activity
C	0030437	biological_process	ascospore formation
C	0034967	cellular_component	Set3 complex
C	0045835	biological_process	negative regulation of meiotic nuclear division
C	0045836	biological_process	positive regulation of meiotic nuclear division
P	0005515	molecular_function	protein binding
P	0006974	biological_process	DNA damage response
P	0008643	biological_process	carbohydrate transport
P	0015144	molecular_function	carbohydrate transmembrane transporter activity
P	0015768	biological_process	maltose transport
P	0016020	cellular_component	membrane
P	0030288	cellular_component	outer membrane-bounded periplasmic space
P	0034219	biological_process	carbohydrate transmembrane transport
P	0034289	biological_process	detection of maltose stimulus
P	0042597	cellular_component	periplasmic space
P	0042956	biological_process	maltodextrin transmembrane transport
P	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
P	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
P	0055085	biological_process	transmembrane transport
P	0060326	biological_process	cell chemotaxis
P	1901982	molecular_function	maltose binding
P	1990060	cellular_component	maltose transport complex

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YagSpFHRVIpdFMlQGG

Chain	Residue	Details
C	TYR46-GLY63

---

site_id	PS01037
Number of Residues	18
Details	SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN

Chain	Residue	Details
P	PRO-284-ASN-267

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	156
Details	Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"2687115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	7
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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