ID A0A498MF43_LABRO Unreviewed; 2052 AA.
AC A0A498MF43;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=ROHU_037091 {ECO:0000313|EMBL:RXN15637.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN15637.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN15637.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN15637.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN15637.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins.
CC {ECO:0000256|RuleBase:RU369009}.
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|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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:RXN15637.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QBIY01012838; RXN15637.1; -; Genomic_DNA.
DR STRING; 84645.A0A498MF43; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Ligase {ECO:0000313|EMBL:RXN15637.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MF43};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 797..873
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1655..2052
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2019
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2052 AA; 225841 MW; 366CE376B9A8E9C9 CRC64;
MWKRAQIVML RLQPEQVNQK ANSPPESRRS NSKASKAPPS SAVGSARGHA SRRNSLSLSV
GSHSIPDPDL EAAGTSGQQG RREGSSTRAL KRSSASEPNI SFSPSPAKRP KAVSSHLLES
SSSGPSAPTT TPEVTEPRKA PASVSTKSKK RRLAAEPAPA RALSKKSASY PGPSGASSTP
SQKRKKADAS SLSSSSSSSL PSSSSAAGPL PPRSEASRAA KPTKLASKSA ASAKAGCSTV
TDSSSSSASS SSSSSSSSSA ATGTNSCAPQ GARLKQGKDQ SKARRSRSAS SPSPRRSSRD
KEQNKAAGSS KFDWTSRFNS KVNLPKPKLS LPGSAKAETS SKPGPSGLQA KLASLRKSTK
KRSESPPAEL PSCRRSTRQK TTGSCASTSR RGSGLGKRGA AESRRQEKMA DSDNNQDGAN
SSAARTEETP QGASASSSVA GAVGMTTSGE SESDDSEMGR LQALLEARGL PPHLFGPFGP
RMSQLFHRTI GSGASSKAQQ LLQGLQATGD ESQQLQAAIE MCQLLVMGNE ETLGGFPVKS
VVPALMNHAS RALTYMMEAL PRSSAVVVDA IPVFLEKLQV IQFIDVAEQA LTALEMLSRR
HSKAILQAGG LADCLLYLEF FSINAQRNAL AIAANCCQSI TPDEFHFVAD SLPLLTQRLT
HQDKKSVEST CLCFARLVDN FQHEENLLQQ VASRDLLTNI QQLLVLTPPV LSSGMFIMVV
RMFSLMCSNC PCLAVQLMKQ NIAETLRFLL CGASNGSCQE QIDLVPRSPQ ELYELTSLIC
ELMPCLPREG IFAVDAMLKK GSAQTTEGAI WQWRDDRGLW HPYNRIDSRI IETAHQNGED
EISLSTLGRV YTIDFNSMQQ INEDTGTARA IQRKPNPLAN PNTGGHLEVR REDARAQLMK
EDPELAKCFI KTLFGVLYEV YSSSAGPAVR HKCLRAILRI IYFADAELLK DVLRNHAVSS
HIASMLSSQD LKIVVGSLQM AEILMQKLPD VFSVYFRREG VMHQVKNLAE SEVFLTSPPK
ACTSGTASLC TTTITTATTT AASNVTPDLG SPSFQHSMDD SLDLSPQGRL SDVLKRKRLP
KRGPRRPKYS PPRDDDKVDN QAKSPTTTQS PKSSFLASLN PKTWGKLGTQ TNSANSEPSR
TAGVSGLARV PPKDSVSNNR DKIKAWIKEQ ASKFVERYFN SESVDGSNPA LNVLQRLCTA
TEQLNLQVDS GVECLEEISS IVSESDVSSF EIQHSGLVKQ LLLYLTSNSE RDTISRDERI
KRFLHVFFGC PIPGQEPLGR LDPTENGPLL ALVHKMNNCL SQMEQFPVKV HDFPSGNGNG
SRGSQALKFF NTHQLKCQLQ SHPDCTNVKQ WKGGPVKIDP LALVQAIERY LVVRGYGRIR
EEDEDSDDDG SDDEIDESLA AQFLNSGSVR HRLQFYIGEH LLPYNMTVYQ AVRQFSLQAE
EERESTDDEA NPLGRAGIWT KTHTIWYKPV REDEEGCKDA VGGKRGRAQT APTKTSPRNA
KKQDELWHEG VCPSVTNPLE SYLISDPPEG ITFDDPSMEV ILLLRVLHSI SRYWFYLYDN
AACKEIIPTG EFINSKLTAK ANRQLQDPLV IMTGNIPTWL TELGKTCPFF FPFDTRQMLF
YVTAFDRDRA MQRLLDTNPE INQSDSQDSR RTINRDELLK QAESVMQDLG SSRAMLEIQY
ENEVGTGLGP TQEFYALVSQ ELQRADLGLW RGEEVTLSNP KGSQEGTKYM FSSRGLFAVP
FGRTTKPAHI AKIKMKFRFL GKLMAKAIMD FRLLDLPLGL PFYKWMLRHE SSISSHDLVN
IDPGVAKSIQ HLEDIIRQKK RIEQDRSHTR ETLQQALESL NMNGCSVEDL GLDFTLPGFP
NIELKKGGKD VPVTIHNLEE YLRLVVYWTL NEGVSRQFES FREGFESVFP LHHLQYFYPE
ELDQLLCGSR SESWDVKTLM ECCRPDHGYT HDSRAVRFLF EVLSSFDAEQ QRLFLQFVTG
SPRLPVGGFR SLNPPLTIVR KTFESTENPD DFLPSVMTCV NYLKLPDYSS IEIMREKLLI
AAREGQQSFH LS
//
