ID V9IIR5_APICE Unreviewed; 1492 AA.
AC V9IIR5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=ACCB10866 {ECO:0000313|EMBL:AEY61028.1};
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7461 {ECO:0000313|EMBL:AEY61028.1};
RN [1] {ECO:0000313|EMBL:AEY61028.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AEY61028.1};
RA Sun L., Zheng H., Wang Y., Xie X., Zhu Y., Gu W., Wang S.;
RT "Decoding the brain transcriptome of the Eastern honeybee (Apis cerana)
RT based on pyrosequencing.";
RL Submitted (NOV-2011) 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};
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DR EMBL; JR049645; AEY61028.1; -; mRNA.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 6.10.250.1630; -; 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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 2: Evidence at transcript level;
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1156..1492
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 16..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1459
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1492 AA; 169243 MW; F9E8BCF80C829BB3 CRC64;
MQNWENDVKD VKCNTLLRKK NEKDNKDGKD HLNNTESGSS TIISMDEQIS TASTSQREET
NNFVPRFETC VETTRLERTL DEDIIDVTGE MDATIQEDEE RPPPPPPEEQ PTEPRDPRIS
NRNPTLELAE SIVDSVLGPC ASEASRLRQS ERTVEGSNTN ETSSRPNTSI VVDFSQEPNE
DLLRESDSSE WIRILTDDSQ SNVERNANIL NQIPTTSASE NINPEISEQQ QQQQQQQQPS
LQQQQQQEPQ QSQEQSQRQQ QNQQSQEQQL PDGVDPSFLA ALPEDMRDEV IAEQLRLQRI
RQRAQATVVE ELTGPVEVNP EFLAALPPAI QEEVLAQQRL EQQRHAAASA NPEDPVDAAA
FFQNLQPSLR QAILTDMEES QISVLPPDLA QEAQNLRREW EARNRHIMQD RFLNHVSQGN
AALSSILRNS GRGRGGGTRY AIHTVAQRGW QPWSNGDPSI THHGAGLRLR GRQLLDHESM
ACVLVLLFVD EPKINTLRLH RVIRNLCYHG STREWVVRAL LSIMERSNDE NKDIAMDFGG
KIRRKSLVPM MHHDYCAPKI FDQRSNAQSW LNISIDAALG CRANVFHIIR HGGKKSERQG
SSIAIHPQAA PTVCRHTLEL LISLAKGFPG YFVPIKSKES DEKESNKEKD SSNKEEIGSK
GKSTSKPGKS DQPDFWDMLL KLDSCASKKG KSVARSHSNS NLGNDTEHNT TTFESSAFGQ
LISMLNWSVI KRSSQLTDKV LKLLSLISIG LTEVNPYRRQ EGNKNKRTDV NKEQSIAAPE
EHLKLAVQVL TSKSCSEEGL EDATALLLNL SHCPDPTRQL ILKLLLEGAM ELANVVCEHI
KDLLMELKVL NRELRRNSIE EQPSTSTGGS RWVLLDRFTN ESVVITAPSK VKAGSDLQLP
SMAALVSKTS SQAFFLRILK VIVQIREAVR LANNKKTSTQ SSESSVDTEN TNQASESGED
KLPLLSESLV LDHLWETLSA CLLELEYTPD QHAVLVLQPA VEAFFLVHSS SSTSRDRHLS
TSTENREVVP DLTPVSPIYS DNEGTSQSEA TINTSWDIQP TPQKTLPPDQ LKFLKFAETH
RTVLNQILRQ TTTHLADGPF SVLVDHTRVL DFDVKRRYFR TELERMDEGI RREELAVHVR
RNNVFEDSFR ELHRRNADEW KNRFYIVFEG EEGQDAGGLL REWYVIISRE IFNPMYALFT
VSPGDRVTYM INSSSHCNPN HLCYYKFVGR VIAKAIYDNK LLECYFTRSF YKHILGILVK
HTDMESEDYS FYKGLVYLTE HNIADLGYEL TFSTEVNEFG VNDVRDLIPN GRNIIVTEET
KLEYIRLVCQ MKMTGAIRKQ LNAFLEGFYD IIPKRLISIF NEQELELLIS GLPNVDIEDL
KANTEYHKYN ANSLQIQWFW RALRGFDQAD RAKFLQFVTG TSKVPLQGFA ALEGMNGIQK
FQIHREDRST DRLPSAHTCF NQLDLPVYET YDKLRTNLLK AIHECSEGFG FA
//
