ID A0A1I8N5R9_MUSDO Unreviewed; 934 AA.
AC A0A1I8N5R9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=101897810 {ECO:0000313|EnsemblMetazoa:MDOA011825-PJ};
GN Synonyms=LOC101897810 {ECO:0000313|RefSeq:XP_011292469.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA011825-PJ};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA011825-PJ}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA011825-PJ};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_011292469.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_011292469.1};
RG RefSeq;
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_011292469.1; XM_011294167.2.
DR STRING; 7370.A0A1I8N5R9; -.
DR EnsemblMetazoa; MDOA011825-RJ; MDOA011825-PJ; MDOA011825.
DR VEuPathDB; VectorBase:MDOA011825; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd04033; C2_NEDD4_NEDD4L; 1.
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; 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:SF443; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR SMART; SM00239; C2; 1.
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; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 4..130
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 201..234
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 456..489
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 507..540
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 599..933
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 901
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 934 AA; 107273 MW; 82319F285E6EEB4F CRC64;
MAEALAEGQV HGYSDNDTTD TCHLRIVIIN GQSLAKKDIF GASDPYVRID LNTINGDINI
DSVLTKTKKK VRKTLNPTWN EEFVFRVKPT EHKLVFQVFD ENRLTRDDFL GMVELTLVNL
PTEQEGRTIA PQSYPLRPRR SVGAKSRIKG TLEIYHAFIH EQRETVEPDT STGEWEHVEN
VSMTGAAPAN AFVANGGSHH DPLPPGWEER QDANGRTYYV NHTARTTQWE RPTTMNTNHA
NINMEAAASD FQRRFHISVD DSETNRSNDT LSLASSTEEN TATTTNSITP LRSANTNESS
SSSTCPIHQN NNNNDGNNNA DDDENDNDAV IDPTTEDHRI RYLYNSLRHP TSRLEISATS
LQNDLRPVRQ INDPDYIIER IRFPNGQPLS RQALENLRNR NNSSGQTFRE SSQNEDGDQT
DSGNRSQTSA SSTRRNSVED NNAATTEPAA ANTDEEPLPP RWSMQVAPNG RTFFIDHASR
RTTWIDPRNG RASPMPNQTR RVEDDLGPLP EGWEERVHTD GRVFYIDHNT RTTQWEDPRL
SNPNIAGQAV PYSRDYKQKY EYFKNHLRKP TNVPNKFEIR VRRTSILEDS YRIISQVTKT
DLLKTKLWVE FEGETGLDYG GLAREWFYLL SKEMFNPYYG LFEYSAMDNY TLQINNGSGL
CNEDHLHYFK FIGRIAGMAV YHGKLLDAFF IRPFYKMMLE KPIDLKDMES VDTEYYNSLV
WIKENDPRQL ELTFCVDEDT FGQKSQHELK PGGANIEVTD ENKDEYIKLV IEWRFVARVK
EQMTAFLQGF GSIIPLNLIK IFDEHELELL MCGIQNIDVK DWRENTLYKG DYHQNHIIIQ
WFWRAVLSFP NEMRSRLLQF VTGTSRVPMN GFKELYGSNG PQMFTIEKWG TPNNYPRAHT
CFNRLDLPPY EGYLQLKDKL IKAIEGSQGF AGVD
//
