ID A0A498MXN5_LABRO Unreviewed; 1143 AA.
AC A0A498MXN5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=ROHU_006193 {ECO:0000313|EMBL:RXN24274.1};
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:RXN24274.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN24274.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN24274.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN24274.1};
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 -!- 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:RXN24274.1}.
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DR EMBL; QBIY01012545; RXN24274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MXN5; -.
DR STRING; 84645.A0A498MXN5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
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; IPR035892; C2_domain_sf.
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:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
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; 3.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Ligase {ECO:0000313|EMBL:RXN24274.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MXN5};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 577..610
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 665..698
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 716..749
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 808..1142
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1110
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1143 AA; 128157 MW; BD9C641835338A9B CRC64;
MHFASRRSNT DPLSETCTSH AEENGLTNTG RSSSEALMQS SLHMKVTPGQ LALALPPLSP
EYGNLQRHST VFIPKVNGSR KSTLQISLQT CKQSGEADGS SAGEDGELAS CEGGNGDGGS
CSSSTTSDAG YCSSNSIFEA DVPDRKSISR RKPRAPLRRC SSLVIFPRSP CTTPPASPVS
PVASPMIPPL PPSARSSFQT SHQMQLSSVD ASNDDTSKGS VATAVNGLRL SKTSTSAEHR
DAKPIVHFSV PPEQPPGPER TERHSSVLLH FANQRPLPSG KASSAKTKVN IDCSKPLEGP
QTDNVPERAK LFRSTSACML PSGRPSSTER RHATFPTSGS SDKSTRKGSH HFLHRSISLE
VPCANAEISC HVSNAADVHS KNGPPHVHIH VSHGTGARRS NTLQDNSIND KPDHVRTCTE
RNATTRDDFL GQVDVPLHQI PTENPNNERP YTFKDFLLHP RSHKSRVKGH LRLKMTYMPK
NNDTEDDPAE QNENLDSWEI ITADESTLYN SHSERSPPPP HSPMEFTGFC EEFNRLQPGN
DRRTSLTPQG HGSRRGSGQT LTVEEHPVHP VLLPTSAGLP PGWEEKQDSK GRIYYVNHNS
RTTTWTRPLI QLIQPPSEAS SSSAAAAVAG GAMSLSQNPT GYAPPLLSPD VSPQHAHAHT
PEHVGMMPAG WEVRSAPNGR PFFIDHNTKT TTWDDPRLKV PVQMRRRVSL DPTDLGPLPP
GWEERVHSDG RIFYIDHNTK NTQWEDPRLQ NSAITGPAVP YSRDYKQKYE YFRKKLKKPS
DIPNRFELNV RRNAVLEDSY LRILSVKRSD LLKARLWVEF EGEKGLDYGG VAREWFFLIS
KEMFNPYYGL FEYSATDNYT LQINPNSGLC NEDHLSYFKF IGRVAGMAVY HGKLLDAFFI
RPFYKMMLQK PITLQDMESV DSEYFNSLRW ILENDPTDLD LRFTIDEELF GQTHQHELKL
GGADIVVDDT NKKEYIHLVM QWRFVDRIQR QMTAFKEGFY ELIPQDLIKI FDENELELLM
CGLGDVDVND WRENTKYKNG YNPNHPVIIW FWKTVLLMDA EKRIRLLQFV TGTSRVPMNG
FAELYGSNGP QLFTIEQWGT RDKLPRAHTC FNRLDLPPYE SFEELREKLH MAIENAQGFD
GVD
//
