ID A0A182QP62_9DIPT Unreviewed; 1170 AA.
AC A0A182QP62;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF014097-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF014097-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF014097-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 EMBL; AXCN02001375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QP62; -.
DR STRING; 69004.A0A182QP62; -.
DR EnsemblMetazoa; AFAF014097-RA; AFAF014097-PA; AFAF014097.
DR VEuPathDB; VectorBase:AFAF014097; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000075886; 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; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF320; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 408..441
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 575..608
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 831..1170
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1138
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1170 AA; 130628 MW; C51AB23B516DB0A2 CRC64;
MSGVCEDEPE REPPVVADGG ELALEQDGGG GLAAGGGSRD GQGTLESEDD DDDEDEDDDD
DDDDDDEDDD DDDDDEEEEE EEEPPELRGA GQQDFPPTPY EECLDLRMFE IRTDADEPTV
PNPAASQEPV RVAAPEATPS TSGVRRKSEP LVNGCPEPAA HPPDPEESNA NGTKKKVRRP
NRLSPDGERP VGGRRKQYWA AHRPLERSWP PKLQPAVPAD GFTFDIIDMD EQERDEREEE
EEEDESEEPE GAVGGPDAVD AATPLRRMRL DRNGNDGPSR QPTSATVRPH RPLARTPSNG
RERRVVGLPA AVIDPSVHTA RSPASPGRGR LVPELVCPPT PTHHARNRAR ALSAPAEGFG
PPELRLQRQD ETGEVTAEVR HVPSMRLPSI PERVRAMAAA TAGGTVEDPL PPAWEARMDS
HGRIFYIDHA TRTTSWQRPG PLTATVTAAH GPHAPDPHRQ QLDRRYQSIR RTIYEHMRHE
NGASGSGASR TRSGPSSTPG PGPAAHFHPA LLLICRSDFY SLLHTTPEAL QIYNRNAALK
HMVSRVRRDP AACFARYQHN RDLVALVNCF ALPAHDLPTG WETKLDQGGK QFFIDHVNRR
TSFMDPRLPI EASRGARQQP LTPPPPPPPP PPLPPPVPPP RPPGTIGTGR ASHAATGSPE
VPVAYNDKVV AFLRQPNILE ILRERHGAAA CSRQLREKIN AIRVEGTTAL DRYGHDLELT
ILLSLFEDQV MTYVPPRARS PPEQPPMAMP STVHGGAGSH ATPKTGGSGV GGGRHVQRAP
APMRRDFEAK LRNFYRKLES KGYGQGPHKL RLEVRRAHLV EDAYERIMAA SRRDLQRCRL
NIVWDTEDGL DYGGPSREFF YLLSRQLFSP YRKMFEYSAN DIYTVQIAPE RPTDREDILE
WYRFSGRVLG LALVHQYLLD AFFTRPFYKA LLRLPVSLSD LESLDSSFHQ SLLWIRDNNM
DNCGELGLNF TVTEERADGS SIDIELKPNG RNITVSERNK RDYLERIIKW RLERGVLEQT
EWLVRGFNEV VDHRLVAVFD ASELELVISG TVEIDVHDWR ANTEYRGGYH DAHHVIVWFW
AVIDRLSNEQ RLRLLQFVTG TSSIPHDGFA GLRGSNGLRR FCIEKWGKAN ALPRSHTCFN
RLDLPPYPTP DILYEKLVLA VEETNTFGIE
//
