ID M4ANL7_XIPMA Unreviewed; 890 AA.
AC M4ANL7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000016062.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000016062.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000016062.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR RefSeq; XP_005796324.1; XM_005796267.2.
DR AlphaFoldDB; M4ANL7; -.
DR STRING; 8083.ENSXMAP00000016062; -.
DR Ensembl; ENSXMAT00000016086.2; ENSXMAP00000016062.1; ENSXMAG00000015992.2.
DR GeneID; 102222753; -.
DR KEGG; xma:102222753; -.
DR CTD; 11060; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000154635; -.
DR HOGENOM; CLU_002173_0_1_1; -.
DR InParanoid; M4ANL7; -.
DR OMA; EIDMADW; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF396; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP2; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..120
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 319..352
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 349..382
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 424..456
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 463..496
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 556..890
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 159..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 858
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 890 AA; 100706 MW; 1ABFFBCFC9F751E3 CRC64;
MAAASVTRPG SAQTPEKSQL ILKVVSAKPQ SPKLPNRHPR LSSFVEVTAD GLTSETKKTG
KRTGHLELQW NEDLTLNVTP QSHLDLKLWS CHTLRKELLG SATIDLLDTL RTHDGKMENV
QLSLVLQTEN KGSVVAGGEL NVCLDGMVVD LGSLPNGSTA ADKVLQPDRP NLRRTQSEGT
PTSAGPNSRS NRHSVGGPQG DSPGGSRERT VHNGELTEEQ NRDTSNHRQP SKSNGSPSHT
ADKAELTSNG LDGSRGVVGR QSPPPPSSPS GRSPAANSSG SSPSPGQDAV GPAVPAEPSP
NAPSSAEQAN SNTTESTTDS LPAGWEQRVL PHGRVYYVDH NTKTTTWERP LPAGWEKRVD
QGGRFYYVDH NTRTTTWQRP TAESVRNYQQ WQSQRSQLQG AMHQFSQRFL YQPSGAPVEN
DPLGSLPPGW EKRQDNGRVY FVNHNTRTTQ WDDPRTQGMI KEHPLPPGWE MKYTAEGVRY
FVDHNSRTTT FKDPRPGFES GSRQGGSPGA YDRSFRWKYH QFRFLCHSNA LPSHVKISVS
RQTLFEDSFQ QIMNVKPYDL RRRLYIIMRG EEGLDYGGIA REWFFLLSHE VLNPMYCLFE
YAGKNNYCLQ INPASSINPD HLTYFRFIGR FIAMALYHGK FIDTGFTLPF YKRMLDKKPT
LKDLESIDPE FYNSIMWVKE NNLEECGVEL YFAQDMEILG KVSSHPLKEG GEDELVTEEN
KEEYISLLTD WRFTRGVEEQ TKAFLDGFNE VVPLEWLRYF DEKELELMLC GMQEIDLADW
QKNAIYRHYT KNSKQIHWFW QVVKEMDSEK RIRLLQFVTG TCRLPVGGFT ELIGSNGPQK
FCIDRVGKET WLPRSHTCFN RLDLPPYRSL EQLREKLLFA IEETEGFGQE
//
