ANM7_TRYB2
ID ANM7_TRYB2 Reviewed; 390 AA.
AC Q582G4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE Short=TbPRMT7;
DE EC=2.1.1.-;
GN Name=PRMT7; ORFNames=Tb927.7.5490;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19254949; DOI=10.1074/jbc.m807279200;
RA Fisk J.C., Sayegh J., Zurita-Lopez C., Menon S., Presnyak V., Clarke S.G.,
RA Read L.K.;
RT "A type III protein arginine methyltransferase from the protozoan parasite
RT Trypanosoma brucei.";
RL J. Biol. Chem. 284:11590-11600(2009).
CC -!- FUNCTION: Arginine methyltransferase that specifically catalyzes the
CC formation of omega-N monomethylarginine (MMA). Has activity toward
CC multiple substrates in vitro. Able to mediate the arginine methylation
CC of histones and myelin basic protein (MBP) in vitro; the relevance of
CC such results is however unclear in vivo. {ECO:0000269|PubMed:19254949}.
CC -!- SUBUNIT: Present in large multiprotein complexes.
CC {ECO:0000269|PubMed:19254949}.
CC -!- INTERACTION:
CC Q582G4; Q582G4: PRMT7; NbExp=2; IntAct=EBI-16101095, EBI-16101095;
CC Q582G4; P62805: H4C9; Xeno; NbExp=4; IntAct=EBI-16101095, EBI-302023;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19254949}.
CC -!- DEVELOPMENTAL STAGE: Expressed during both bloodstream (BF) and
CC procyclic insect (PF) life cycle stages. {ECO:0000269|PubMed:19254949}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- CAUTION: Compared to PRMT7 orthologs in other metazoans, it is shorter
CC and lacks the C-terminal part. {ECO:0000305}.
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DR EMBL; AC091553; AAX78867.1; -; Genomic_DNA.
DR RefSeq; XP_846172.1; XM_841079.1.
DR PDB; 4M36; X-ray; 2.04 A; A=36-378.
DR PDB; 4M37; X-ray; 1.70 A; A=36-378.
DR PDB; 4M38; X-ray; 2.20 A; A/B=36-378.
DR PDBsum; 4M36; -.
DR PDBsum; 4M37; -.
DR PDBsum; 4M38; -.
DR AlphaFoldDB; Q582G4; -.
DR SMR; Q582G4; -.
DR DIP; DIP-60814N; -.
DR IntAct; Q582G4; 2.
DR STRING; 5691.AAZ12613; -.
DR PaxDb; Q582G4; -.
DR GeneID; 3658759; -.
DR KEGG; tbr:Tb927.7.5490; -.
DR VEuPathDB; TriTrypDB:Tb927.7.5490; -.
DR eggNOG; KOG1501; Eukaryota.
DR InParanoid; Q582G4; -.
DR OMA; FARDMQW; -.
DR BRENDA; 2.1.1.321; 6520.
DR Proteomes; UP000008524; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; TAS:UniProtKB.
DR GO; GO:0016273; F:arginine N-methyltransferase activity; IDA:GeneDB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISO:GeneDB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; IDA:GeneDB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:UniProtKB.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; ISO:GeneDB.
DR Gene3D; 3.40.50.150; -; 1.
DR IDEAL; IID50227; -.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..390
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373923"
FT DOMAIN 55..372
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:4M37"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4M37"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4M37"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4M37"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4M37"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:4M36"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:4M37"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4M37"
SQ SEQUENCE 390 AA; 44026 MW; 32C2C7EEF1EB45B1 CRC64;
MPPKQHRHQK KDKNDNALQN TIGFVPPGAT LASVSGYRPP DAFVNRIDRN IPVPARLRHT
PVSLIEAVND FHYAMMNDEE RNNFYYEVLK KHVTPETGVL EIGAGSGLLS LMAAKLGAKW
VVAVEGSEEL AKLARENIRA NNMEHQVKVL HMMSTELKSK HLPEPPDVLL SEIFGTMMLG
ESALDYVVDV RNRLLKPTTK IIPQFGTQYA VPIECDALHR ISSVSGWRDL DLKHMMTLQD
TVSIVFAKHY GIRMNSVNFR RLSDPIELFR VDFSSSNRND IPRRKHFDVV AKESGTAHAM
LFYWKVTDDE FVMSTDPEDT VNNFPRDMQW GQALQLLDAS NGPLPTPVVF TEGKNYNFEC
NFSGDRVILH MQLCPESGNG EMTECEGKTT
