ID A0A194QVJ9_PAPMA Unreviewed; 1686 AA.
AC A0A194QVJ9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=RR48_13131 {ECO:0000313|EMBL:KPJ09497.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ09497.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ09497.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09497.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ09497.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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; KQ461073; KPJ09497.1; -; Genomic_DNA.
DR STRING; 76193.A0A194QVJ9; -.
DR InParanoid; A0A194QVJ9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase 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 CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR000008; C2_dom.
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:SF443; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 1166..1188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1234..1256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1279..1297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1318..1338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1409..1430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1462..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1493..1516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1528..1550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1571..1589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1601..1623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..195
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 263..296
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 589..622
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 644..677
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 736..991
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 254..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 189348 MW; 2ECDB8476C4BFA34 CRC64;
MHNVRPLEFI SRISEPHRSR SSSWSSWRRN NDIQRSEPRF SLQYQTDENS FLLRLKIIGA
FSLAKKDIFG ASDPYVRVEL QKIDGDVTVE TFLTKTKKKT LNPVWNQEFI FRTLNPVWNQ
EFIFRKIENG GDKYQESISV YLCLSIEDST VKPQEQKLLI QVFDENRLTR DDFLGMVEIP
LAGAPTESAA APRPPPAKYP LRPRRSVARS RVRGHIEVYV ALVGRVGEAE DESEASPAPA
ADGWEMVEPE AQTGTVQPTI GGDPLPPGWE ERQDANGRTY YVNHIARSTQ WERPTFTRNI
STETQAERME TAATEFQRRF HISADDEHTN SPQTGSHQDD MSDRRADSTS TEVTPFSTPV
RSPQTANASA TAPDNVPTET SNLSNDCDTN VREDNDNDVI DAPTSAIADV DNVTTEEIPE
TVETNVNTTE DAQDTSGNEI ASTSQINTVE NVAVDNNTES TSNNETDELV RQQSNDDAQS
QSTAETNASE EANDNVEEVR VNGDEVRPAG DDDDEEVELI EIVAESLTFD ENHFSTPTAG
SPESRTPISR RRRTTASSMD DSEDETDAST ESTRSSSTSS QSQNLPNSDG LPPGWSMQRA
PNGRIFFIDH NQKTTTWIDP RTGCASSLPT AAGSSSAAEA DELGALPEGW EERVHTDGRI
FFIDHNTRTT QWEDPRLSNP QIAGPAVPYS RDYKRKYEYL KSQLRKASNV PNKFEIKVRR
NYILEDSYRI ISSVSRLDLL KTKLWVEFES EVGLDYGGLA REWFFLLSKE MFNPYYGLFE
YSAMDNYTLQ INPNSGVCNE EHLNYFKFIG RVAGMAVYHG KLLDAFFIRP FYKMMLGKSI
ALQDMESVDL EYYNSLMWIK ENDPSELYLT FSVDEEQLGK TVQRELKPGG ANIPVDNDNK
FEYIKLVIQW RFVSRVQEQM CAFLEGFDGL VPLPLLKIFD ENELELLVCG IQHIDVRDWR
ANTLYKGDYH ANHLVVQWFW RATYVLIHEQ KLVCVRWPAV GCPAHEHAPE HAPDHAPDHT
PEHAPEHAPD HASEYAPDHA PDTHIQETSF ATFPPLYALE EWTRCQGAED VYCMVDAALV
ARTHSPLLHL LQEYSAQTLK HYNRTVVHRG VCVSRCGQVG DDGGWTEAAQ QCVNQSVLQY
GLEAEVISAQ WCTTPKPDRP SSSARFLAVL CIALLVLAVL ATGLHILGDC CSTVEGNKYL
LAFSLKRNWS ILNYDRTKPR SDDRMKNLTA MEGIRFIGIQ CVIFSHVLWI YVYSYIDNPQ
YVENMYDHFA WKMVLNSPLW LQVFFSLSGF LTAYSVLITT DTNPITFGKC VLSVINRWIR
LTPVAGFALW FTISWFPLLG SGPQWGLLVR REAADCAQRW WYHLLYVHNH IPLGKMCMGH
TWYLAADMQL HVAGVLLLLV VVRWRRLAAP LLAGPVLAAA LAAGLVAYFY NLTPIITAQP
PELLRNLFGG SQILPLLYLP SWMNLAGYLG GVATAFLLHY TQTNAVNLAE HKLFNLLFHA
SLSLGGAVVI GGVVFLSDTP PPQWVTALYA ALDRTLVAMF FNIFMLGCFT RCKSVVRSAL
EWRGFHALGR LSYCAYLVHF IVLRLTLAGN TQLGHASLLS MISLLITASV LTYIVSVPLC
LMVELPAIQL WKAATGAEGG GGAGGQRAPA RRDPCARPPR AQPQLTQVRL SISYTTQCCL
ILTVIY
//