ID A0A0D2U5D0_GOSRA Unreviewed; 1528 AA.
AC A0A0D2U5D0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=B456_009G420400 {ECO:0000313|EMBL:KJB63186.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB63186.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB63186.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR EMBL; CM001748; KJB63186.1; -; Genomic_DNA.
DR EnsemblPlants; KJB63186; KJB63186; B456_009G420400.
DR Gramene; KJB63186; KJB63186; B456_009G420400.
DR OMA; FESRCAE; -.
DR Proteomes; UP000032304; Chromosome 9.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF10; E3 UBIQUITIN-PROTEIN LIGASE UPL4; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1187..1524
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1528 AA; 170884 MW; AC8E64CAE1203BC6 CRC64;
MGSRGQKRTE TADELPADKR ACSSLEFRPS SSNCSSIRTH LNSPNSIPDA DMETSSSTSA
SSRSDGEHEK EDESTYGSCD SDDAEQQPRH HILRDYQRRR SSSDHGKLNT ILSNLNEGNG
GSGQLAALTE LCEVLSFCNE DSLSSLMADS LSPVLVKLAK NESNANIMLL AIRGMTYLCD
VYPRSSGFLV RHDAVPALCE RLLAIEYVDV AEQCLQALEK ISRDQPVACL QAGAIMAALN
FIDFFSISVQ RVALATVVNI CKKLPLEGPA PFVEAVPKLC DLLQHEDQQL VESVATCLIK
ISERMCQSSE LMEELCKHEL INQVTLVMKS NSRTTISQPI YNGLIGLLVK LSSGSFVAFR
SLYELNISNI LKDVLSTYDL SHGISPPDLV DGNCNQVHEV LKLLNELLPA STGDQANQVV
LDKESFLADH HDLLQRFGMD LFPVLVQVVN SGANIYVCYG CLSVISKLVV LSKPDMLGEL
LKTANIPSFL AGVFTRKDHH LLMLALQIAE IILKKLSDVF LSSFIKEGVF YVIDALLMPE
KCSQLMLPVF GGIQPSFDSS QKSSAREFQR CLCYAFDMVP SSSVSSCKID KDTVCNLAKH
IKTNYFAPEL VESEKGMTDV LQNLRTLSAA LSSLINMPVD DGTTVQHEEK FYSILHQIML
KLNGREPVST FEFIESGIVK SLMHYLSDGM HMRGNVEFTG SYDHLVVLGK RFEVFTKLFF
SYSDILVEDL PLSILIQKLQ SGLSTLENFP VIPSHGFKQR NSFATVPNGR CVMYPCFRVR
FVRAEGENCL SDCAEDVLAV DPFSPLDAIE GYLWPKVFTE RTEYGELDAE ELEQREVLPN
LLPSNANSTQ AKSSGFIDSM SIDLPEMQED EANFSQIASE QVHFRELNSG ETMSLDETNM
GSAGKEQEFP TESTKNMRTP CSASGDNDIK DSSARLLLYL EGHQLDRTLT LYQVILQQLL
NSEKEFMTWA KLWSRVYMIT YKRALESNQD DPQEHTYQER KFSVSDQKIA SIQNMGYFAS
MFACKLTSDL DKSSPIYDIL FLLKLLEGIN KYSFHLMSCE RVRAFAEGRN DNLDNLKVMV
RSVSQNEFVS SRLTGKLEQQ MQDAFTLSTG GMPSWCNGLV SSCPFLFSFE ARCKYFRLAA
FGPRRGQLNA ISRSNSGTSS DRQTTSGGLP RKKFLVSRDQ ILDSATRMMD LHARHKGLLE
VEYNEEVGTG LGPTLEFYTL VSHEFQKFGL GMWRGDHCSF ITSTTLPTES VILRNSSGLF
PRPCSPKSDA NNGIQFSQVL KKFVLLGQIV AKAIQDGRVL DVSFSKAFYK LILGQDLSLY
DIQSFDPELG RTLLEFQAII VNQKRHQESI CVENAALKQD LCFRNTRIED LYLDFTLPGY
PDYVLSSECN LKMVNSANLE EYVELVVDAT IHSGIARQVE AFKSGFNQIF SISHLHIFTE
EELERLLCGE CDIWAFNELL EHIKFDHGYT ASSPPIVNLL EIIQEFEYSQ RRAFLQFVTG
APRLPPGGLA SLIPKLTIVR KVRIIIEP
//
