ID A0A0V1CMI4_TRIBR Unreviewed; 924 AA.
AC A0A0V1CMI4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Protein arginine N-methyltransferase 1.5 {ECO:0000313|EMBL:KRY50429.1};
GN Name=PMRT15 {ECO:0000313|EMBL:KRY50429.1};
GN ORFNames=T03_643 {ECO:0000313|EMBL:KRY50429.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50429.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY50429.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50429.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY50429.1}.
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DR EMBL; JYDI01000150; KRY50429.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CMI4; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00814; ADX; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023014};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|EMBL:KRY50429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01015,
KW ECO:0000313|EMBL:KRY50429.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..539
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 543..709
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT DOMAIN 828..903
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF00111"
SQ SEQUENCE 924 AA; 105391 MW; 06A2418F44B4F03D CRC64;
MKYSTKTEDV YSLPGYLLQL ENKNIDFAVI AVENPRALHS TESTTKDNCP LLSIPDIIMK
TRNWSRLVVG EFPPVKYEPH EEDEIQCFIK ARTMQLEYAN YLGLSAMIVS FTQESLAPLA
HVLNHFFLGT SLLKNEFCRS CEADIAVVPR FGLFTLGTIA SGQGPGFTCR LALIVVSEIQ
AVHVGNASVG HCHRRERFLR FEGRCVGDSH SQYGTRRHRV GCILSLVRFV ACIRSKPVIW
CRLPLTWNRI DETADDAWHL YYQLRTACGN DARLEVALEI GADLCDNMQI LDRWTGXXXX
XXGLENRSAT SPGGDLPTVS EFHRQLLSIL FARTSRAILE FDSEQLDTIP VNEYSFCVRN
LYKNQRVLPM EKNSSVMRSY RDYLQLPLQP LFEDLSAATY EVFETDSVKY MQYEMAIKEA
ISDKISGNDV PFFNVIVCGA GRGPLVTAVL KALEHFAIPA FQLIAVEKNI NAVSTLDHLN
KTKWNRKVHI VHSDVRKFKP PAKADIIVSE MLGSFGDNEL SPECLYEAMK FLKPDGVCIP
QFYQSYLSPV HAPKLHYNAA QYRKQVEYND ALECGYVVYP ATAFVIDYPK PLFPFTHKVG
CNTKPKQKNF YKVLKFRSEI DCELSGFLGY FYCILYKDHA LSILPSNHTP NMRSWFSMFF
PLVTPVMVKA GAEIEIHFWR NTGHGKVWYE WWLAKPTVLP VQNPNGRSWS FAFKAYAFQL
IWFYFLHKFT ADVSQYYGNE LYFDKVLYFK NAVPQVKAGF RVVQNATAEF PVDRFKILFS
KFKNSTLEHQ FAESRKKAVR ILLHFIICYS IFSIAVTFLT SHGDQFKAYG KIGDTLLDMV
FNENIPLDGF GICEGTCSCS TCHVILKREQ YDYLPSPRED ELDMLDLAYG LTDTSRLACQ
IVLTEQLDGM EVVVPGLPDA TQFH
//
