ID A0A3Q3AWY7_KRYMA Unreviewed; 844 AA.
AC A0A3Q3AWY7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000021035.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000021035.1}
RP IDENTIFICATION.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR AlphaFoldDB; A0A3Q3AWY7; -.
DR STRING; 37003.ENSKMAP00000021035; -.
DR Ensembl; ENSKMAT00000021312.1; ENSKMAP00000021035.1; ENSKMAG00000015646.1.
DR GeneTree; ENSGT00530000064170; -.
DR OMA; PEPNCAI; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 116..155
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 93558 MW; 5706BC03E925A72F CRC64;
MPPPARNSSR RRKRNPDNEE RATGERLPAE VTAPTRMKLR VRRGDGAAAS GGGGPVEETT
ERSREGSRSS SRRKNSNKTS ASATAAAASS SSPPTTSASS VRAVMAAEEA SPDSKCPICL
DRFNNLAYLD HCLHRFCFPC IQEWSHNKAE CPLCKQPFAS ILHSVRAEDD FKEYTLQPPP
TNNSVAATVA MVAAMASAAR SDHHMRLMLR RHRVAEGRET TTRRRRRERG ARGRGSEERA
GGVWELYLDH PPLSFPPLSR HLSVSNVVAE DSEEAEELPA ERGGADSAER GALLNELTGL
RGAAASLASN NRALRRLMTR LAARQRLQRE GGTMQRLRDG QMLDFRRMLY RCGIRVRGIA
GVSGNTGQQR DITAESFHQS HSHLNRLRPW LRRELRVMYG SNSSLVDIVQ NIIMARLALH
GLENTLNLEE DLRPFLQART EHFLHELVSF ARSPLNMDSY DLQAVYEPPP AAAMELDGFS
SSSEGSSVIA ISEEEEVEER GGRSEGTVIN DLNDIIQTGS SLSLSGWDDE TPGPSYSTAE
PSCSLVPPLS LSPTPQEPAN ERGGDRPREE AEEECLIVGY KKPIAERTPE LVQLSSDTEE
EEGEKKKKEE EPAEKTPPLP SPTPSSSYLP IIPPSTSGAF RAEQEAGQKD EEVGGWRSRS
WSGSSGRSRK SVCSLNLAAP ERRRRDDTQR GRRRKKKNKK RGREEGQRRS GVFSNPNRSI
YPPMMRRRSP PLFDSSADSS LEFHCAQVSP ISSPSCSSPS SPLCLSPPQT PPTPSRSPAE
HAHHAEKPGG KRKYKSRHLN SSTKDPSWRQ SGGRPRERRK ERRRRREKTR KEDQQENGGL
GEEG
//
