5WCF

Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0003682	molecular_function	chromatin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0008168	molecular_function	methyltransferase activity
A	0008469	molecular_function	histone arginine N-methyltransferase activity
A	0010821	biological_process	regulation of mitochondrion organization
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0018216	biological_process	peptidyl-arginine methylation
A	0032259	biological_process	methylation
A	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
A	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
A	0036211	biological_process	protein modification process
A	0042054	molecular_function	histone methyltransferase activity
A	0042393	molecular_function	histone binding
A	0044020	molecular_function	histone H4R3 methyltransferase activity
A	0045652	biological_process	regulation of megakaryocyte differentiation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0070611	molecular_function	histone H3R2 methyltransferase activity
A	0070612	molecular_function	histone H2AR3 methyltransferase activity
A	0090398	biological_process	cellular senescence
A	0140938	molecular_function	histone H3 methyltransferase activity
A	1901796	biological_process	regulation of signal transduction by p53 class mediator
A	2000059	biological_process	negative regulation of ubiquitin-dependent protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue SAH A 401

Chain	Residue
A	HIS57
A	ALA113
A	SER114
A	PRO139
A	VAL140
A	GLU141
A	GLU155
A	MET166
A	SER169
A	HOH503
A	HOH505
A	MET60
A	HOH513
A	ARG66
A	TRP78
A	GLY90
A	ALA91
A	GLY92
A	LEU96
A	GLU112

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site_id	AC2
Number of Residues	16
Details	binding site for residue A0S A 402

Chain	Residue
A	TRP156
A	GLY158
A	TYR159
A	GLY160
A	LEU161
A	LEU162
A	HIS163
A	GLU164
A	SER165
A	ALA189
A	ILE236
A	LEU256
A	PHE292
A	LEU343
A	VAL355
A	MET373

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site_id	AC3
Number of Residues	8
Details	binding site for residue 144 A 403

Chain	Residue
A	VAL56
A	MET60
A	GLU155
A	MET157
A	HIS163
A	HIS317
A	TRP318
A	HOH536

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	GLU155
A	GLU164

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS57

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	GLU141
A	GLY90
A	GLU112
A	ARG66

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR21

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000269|PubMed:23866860

Chain	Residue	Details
A	ARG35
A	ARG37
A	ARG29

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