ID A0A182RXM4_ANOFN Unreviewed; 1198 AA.
AC A0A182RXM4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-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};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN011042-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN011042-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN011042-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; A0A182RXM4; -.
DR STRING; 62324.A0A182RXM4; -.
DR EnsemblMetazoa; AFUN011042-RA; AFUN011042-PA; AFUN011042.
DR VEuPathDB; VectorBase:AFUN011042; -.
DR VEuPathDB; VectorBase:AFUN2_007408; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
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; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 3.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF395; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 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 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; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 174..207
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 609..642
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 657..690
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 860..1198
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 200..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1166
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1198 AA; 131048 MW; B8E34483029B5DAF CRC64;
MNKLEYSRRN GTQKIRITIL CARNLARKDL FRLPDPFAKI LVEGTTQEYT TEICKASLDP
RWNSHYDLFL GKNDNIIISI YNHRKLHKRQ AFLGCVRIVA SSIQLLRDTG YQRLELVKRS
QDDPDPVKGQ IIVSLMSRDS ATGGNPLAIV SPAGDVRVPD DDDTVDDTLI VEQQQLPQGW
EERSTQAGRT YYVNHYTKTT QWPRPTEPAG PPGRQSSNNA VNGGTVNGGG VPVQQHILGS
PTNGPANGVG EEPGCPTIPA GPSKSATNNS INSIQSNDSG SRRHSAEILV SSNNKENCIN
QHHHQQQQQH NGKDHSHRNG GKDVDGNGVR EGLVNGNGAG TPAHNRHRND AKSPVRIQDE
SILITPSSSN TSPLSEINSP IASPKQQDVS PRSGNGGREP QQVTGVTNAI GTLAIDTPST
VRSPSSTNPS SGGQCVVLVN GNGGGVTNFS SPNHQHSRSG GDSSVPAPGG GGPNHPAAKP
TVPSYLPLNV SNSSATNGAT NNSTSNGVSN HSNSSSGPDT IGGGTGGGGG GGGGGGGRSQ
QQHHHGTPAG ESCHREGSAS RYRTRSGRHA EDPNRRRTSR DRPPRPSMGG IVIAGHQTRS
GVPFIRPAVD LPLGYEIRTT QQGQVYFYHI PTKQSTWHDP RIPRDFDTQN LTTETLGPLP
HGWEQRKTAS GRVYFVDHNN RTTQFTDPRI NMHILQMIRR QNSAAASPPP ATTATTGTNG
CSSVALSPLS GAGPQVPNGS SGGSSRHAAL AEAVNAITNG VRTRGGIEIE DRYSNHLFIP
QDAHHHSPRG ATVSNNIPDL PQGLMDSADL LPKYRRDLVG KIRALRQELQ LLQPQSGHCR
LEVSRNEIFE ESYRLIMKMR PKDMRKRLMV KFKGEEGLDY GGVAREWLHL LSREMLNPQY
GLFQYSRDDH YSLQINPDSG VNPEHLSYFH FVGRILGIAV FHNHVLDGGF TLPFYKQLLN
KPITLSDIED VDPDLHRSLT WMLENNMTGV IDSTFSVENN SFGVLKVHEL KPNGASIPVN
EDNKREYVKL YVNYRFMRGI EQQFLALSKG FGELILSHLL RPFDERELEL LISGISQIDV
NDWKANTRLK QCTADTPQIV WFWQIVESYS PEMRAQLLQF VTGSCRVPLQ GFRALQGSTG
AVGPRLFTIH LTADVPIQNL PKAHTCFNRL DLPMYDSYQL MYDKLTQAVE ETCGFAVE
//
