ID A0A2A4JZB4_HELVI Unreviewed; 2272 AA.
AC A0A2A4JZB4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=B5V51_8055 {ECO:0000313|EMBL:PCG77116.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG77116.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG77116.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG77116.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG77116.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) 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 ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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:PCG77116.1}.
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DR EMBL; NWSH01000352; PCG77115.1; -; Genomic_DNA.
DR EMBL; NWSH01000352; PCG77116.1; -; Genomic_DNA.
DR STRING; 7102.A0A2A4JZB4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.720.50; -; 2.
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; 2.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 904..981
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1973..2272
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1779..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2239
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2272 AA; 245829 MW; AF433B6DEA87F5C5 CRC64;
MAEQHITPSS HSALTRESSG SSPSRVVGGR WLRQVRRTSH SRRSRRNVTS PLPRSTSRHS
SSRVSDAEPY THVEPRRSSR LIHAQPRSDY SITERWSYGT DVYETRCDTT EFKGGDAHKS
SVHPKRGRTS SHDRKKRKTI SNNSAEECVA YCTRSRTALK SSESACEQIP NHLKPHTLTQ
PPLNQNATAT STQANPPEGG LLPLDERDFA YSPYSSSTVT ELLDSDYSVY SPTASRRKGK
KRKRSTHRSL SSRKSSCLLS VDECRKKFKI DSHSKDETDT SSTGRSSKHE LDKSELNSAS
QTSCTYLLRN RSSHFGPPTS TVISDHSVNP PGEAVHTPLA GRISSASESI ASIPSTPPPP
DRDIQEASSS KAHSSASKLL IVPRDLPYLR QTNARRSIAA ATGATLGACL TRGASTSQRQ
RQDTQSKRQV SGSEGAGSSA AGGRRARARD MPQPQPASTR RDKRGKSSLG SCASTGGASS
RSHPQPLTTG AVASTSSTPP ASASASMPDN AASDAKPKGK ASSSSEECAG GGSGVGGSGS
GAGAEESSSE EGEVGRLQAL LEARGLPPHL LGALGPRMQH LLHRTVTANS AASKAAQLLA
GLQATGDEGQ QLQAVIEMCQ LLVMGNEDTL AGFPVRQVVP ALVNLLAAEH NFDMMNHACR
ALTYMLEALP RSSGAVALAV PAFLDKLQAI TCMDVAEQSL TALDMLSRRH SKAILQARGV
SACLMYLDFF SINAQRAALS ITANCCQNLT PDEFHLVRDS LQLLANRLTQ QDKKSVECVC
LAFSRLVDSF QHDPARLQEI ATPELLTNLQ QLLVVQPPLI SGATFITVLR LLWVMCCACP
QLALALHQRS IADTLLCLLT GSTLHQEQVE LIPRLPQELY EITCLIGELM PRLPTDGIFA
VDSHLDRPWS ASTERTAHWQ WRDDRGVWRS YSWAESRALE AGAAAGEEEV CLTTLGRSYT
VDLTAMQQLN DHTGTARPVQ RVAPAPAEPA AAAPAPDPRV ALLRAHPGLA RALLAVLHEV
YWSSAGPAVR SQALKAILRC VYYADAPLLR QILKMQVISS HIAGMMASSD LRIVVGSLQL
AEILMQRLPD EMGVQFRREG VLHQVAQLAE RAPPAQPARH HPVKSPGGGS VRSSGGSSPP
ASTSATSLEH QNNLSLAFSA SGSFVASTMQ AGAAAGEEEV CLTTLGRSYT VDLTAMQQLN
DHTGTARPVQ RVAPAPAEPA AAAPAPDPRV ALLRAHPGLA RALLAVLHEV YWSSAGPAVR
SQALKAILRC VYYADAPLLR QILKMQVISS HIAGMMASSD LRIVVGSLQL AEILMQRLPD
EMGVQFRREG VLHQVAQLAE RAPPAQPARH HPVKSPGGGS VRSSGGSSPP ASTSATSLEH
QNNLSLAFSA SGSFVASTMP AAGSDGSGSE PGQASASTHA QMSSTSVHRS GSPLQLAEML
KRKRAVKRSG GSGVVSGGRS ATRVGGASKT SSFLSSLNPS RWGRSPHAHK DSALLASPHA
SANLTVQNKE KLRDTMLHHD VSPFEVNHSG VLGALLQFLT GAETESEAGE ARDGDGEGRD
DALAAAEDRL RLFLHVFADM PLTIESEWSG AGAWGCAALA ALVGKVNACV SHLEQFPVRV
HDLPARPATS ALKFFNTHQL MCDLKRHPTC TNLKQWKGGV VRIDPLALVQ AIERYLAQRG
YASGRSRSES GGAPHSDDDA ASDDDVEDSL ATPPHHPTDS DHKLEFLIGD TVLPYNMTVY
QAVRQFGEQT DADTDTETPL ANAGIWVQTH TIYYRAVEAG EQPRPDTTAS RKGKGQPTKL
SSRRKPDLLW NDFINAKRHN VLRQAEHVMH EFAHSKALLE IQYENEVGTG LGPTLEFYAL
VSQELQRADL DLWHGSENFK QKPTSFGGEI VKSQPPVVTD RSADAAARLA SSVRDALNLD
EERSPEPSDL EKETSIPSPA PDATYVTWPC GLFPQAVGRN ARASHVSRVK AKFRFLGKFM
AKAVMDSRMV DIPLSVSMYR WLVSEEQWLS LSDVRHVAPE LWRSLCRLRS VAERARQLAA
DPRHSPEQRT QLISALELDG CPIEELGLDF ILPGDGCTEL RRGGRDLPVT AHNLHNYIDL
VTHWLLYEGV TKQMEAFREG FESVFPLANL KIFYPEELEQ VFCGSPSGGR DQRWEPRMLT
ECIRPDHGYN AESRAIRMLI DILASYNREE QRLFLQFVTG SPRLPTGGFK ALNPPLTVVR
KSLESSLDPD EYLPSVMTCV NYLKLPDYTS AEVMRAKLRL AASEGQHSFH LS
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