ID C3YLJ2_BRAFL Unreviewed; 1535 AA.
AC C3YLJ2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BRAFLDRAFT_128503 {ECO:0000313|EMBL:EEN58929.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN58929.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58929.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN58929.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666527; EEN58929.1; -; Genomic_DNA.
DR RefSeq; XP_002602917.1; XM_002602871.1.
DR STRING; 7739.C3YLJ2; -.
DR eggNOG; KOG0939; Eukaryota.
DR InParanoid; C3YLJ2; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1199..1535
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 51..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 856..884
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1502
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1535 AA; 169162 MW; FC079F9C3CD804B0 CRC64;
MDIETMGGNM VLNQVKAQHR SWHGSVIVED WFAGDLKLTL FLFLTVSDGE SSGTTSGADS
QPSTSTGTTE GSASSSETPT SEGQSAASTA ETTQAGPGNE ELNSLLGSDV QLPEGVDPSF
LAALPEDIRQ EVLRTQLGIR RTPPTAQAGN SSGSSTSTTA PDNVQVSPEF LAALPPEIQE
EVLQYERMEQ QRLEAQRAAA NPEQPVDPAG FIQNLPSSLR QQVLADMDDT VLAVMPPEIA
AEARNLRREL EERHRQLMQE RLFSAASGLA SRLGGRGIHY IQSALPQHHR NTWRWGTQHN
RAATATTANQ VRLRGRQLLD HEALACLLVL LFVDEPKLNT SRLHRVLRNL CYHNGTRLWV
VHALLSILDR TGDNVCKPLL EITDGSEKGS GKKSRPSSSS SQDMAMDTRT SQPSWLSISL
DAALGCRANV FQIQKTGGKK HVERHSGAVH IHPQASPIVC RHVMDTLISL AKVFPGHFIP
GKAREAGTCS TSSSSSSSQT QANKVKETPP AAGTVATNRV GSSKTDTDFW DVLVKLDSMS
VGRKGKGTAK SHAGASTSES DPSGESLETS PLGSLLQMLA HPVIRRSSVL TDKLLRLLSL
VSIALPEEMK KAEEQAREEA ARREESRTEE SAAESGATGG TEAAAVEQRP AEQTVTVQST
LELVPTATST PSPTPSRKDT VIPRPTSTSS VFEDSAGRAT NIMLEKQLQL AVDILTSHSC
SEEGLEDATN VLLQLSRIDN QTRESVLKLL LQGGRQLGHT LCEQIFQLLQ EVRDHISRLK
QTGAEGGMEE LSSPEEAGTS QARQRGVISN RFDSQMVVVA APTKVKGGRE LQLPSMAQLT
SKTSTQSFFL RILKVIIQLR EAARRAVKKA RDAEKRQALE AEAEAIIEMV GRRERERLQR
ENSAPAAPGT AAAGASTSTE DQAAPAEAPA DPAAGPALGD IIGEAPMELE PQATGAAAPA
AQAPAAQEPA AQAPAAEETP AQTEEQQAAG KKEKEEAEEP ELPRLSSQLT LEDLWDTLSE
CLTALSDTTD HHAVLVLQPA VEAFFLVHAA EKEKKTTEQR QSERQRHDSH LSDHAPMSPL
PATPADSGTS LGRQESVASV SSAANITGLP HDTQKFLRFA KTHRTVLNQI LRQSTQHLAD
GPFSVLVDHT HILDFDVKRR FFRQELERMD EGIRREDLAV HVRRDHVFED SFRELHRRTP
EELKNRLYIV FEGEEGQDAG GLLREWYLII SREIFNPNYA LFTTSPGDRV TYRPNPSSHC
NPNHLSYFKF VGRVIGKAIY DNKLLECYFT RSFYKHILGK NVKYTDMESE DYQFYQGLTF
LLENNIEESG LELTFSTEIQ EFGVTEVRDL KQNGRNITVT EDHKHEYVKL VCQLKMTGSI
RKQIDAFLEG FYEIIPKRLI SIFNEQELEL LISGLPNIDL DDLKANSEYH KYQSNSLQIQ
WFWRALRSYD QADRAKFLQF VTGTSKVPLQ GFSHLEGMNG TQKFQIHRDD RSTDRLPSAH
TCFNQLDLPP YETYEKLHYM LKIAIQECSE GFGFA
//
