ID A0A0D2PYF1_GOSRA Unreviewed; 1123 AA.
AC A0A0D2PYF1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=B456_005G236600 {ECO:0000313|EMBL:KJB32343.1};
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:KJB32343.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB32343.1, 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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM001744; KJB32343.1; -; Genomic_DNA.
DR RefSeq; XP_012480216.1; XM_012624762.1.
DR AlphaFoldDB; A0A0D2PYF1; -.
DR STRING; 29730.A0A0D2PYF1; -.
DR EnsemblPlants; KJB32343; KJB32343; B456_005G236600.
DR GeneID; 105795236; -.
DR Gramene; KJB32343; KJB32343; B456_005G236600.
DR KEGG; gra:105795236; -.
DR eggNOG; KOG1609; Eukaryota.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 804..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..130
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 77..124
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 125090 MW; 40C424DA084E836E CRC64;
MEIAPAAPPL PHPPGGDSAA SSTVAVIADN IHPLPSTSSA SSEMEEKATS SSMSFGAAAE
AKYGADMEEE EEEEDVCRIC RNPGDAENPL RYPCACSGSI KYVHQECLLQ WLNHSNARQC
EVCKHAFSFS PVYAENAPAR LPFQEFVVGM AMKACHVLQF FLRLSFVLSV WLLIIPFITF
WIWRLAFVRS FGEAQRLFLS HISTTVILTD CLHGFLLSAS IVFIFLGATS LRDYFRHLQE
LGGDVEREEE VDRNGARAAR RPPGQANRNL AGDGNGEDAG GAQAIGGAGQ MIRRNAENVA
ARWEMQAARL EAHVEQMFDG LDDADGAEDV PFDELVGMQG PVFHLVENAF TVLASNMIFL
GVVIFVPFSI GRIILYYVSW LFSSASGPVL SVVMPLTDTA LSLANITLKN ALTAVTNLTS
EGQENGMRGQ VAEMLKANST AIAEVSSNTS APFSADLLKG VTIGASRLSD VTTLAIGYMF
IFSLVFFYLG IVTLIRYTRG EPLSMGRFYG IASIAETMPS LFRQFLAAMR HLMTMIKVAF
LLVIELGVFP LMCGWWLDVC TIRMFGKSMS QRVQFFSVSP LASSLIHWVV GIVYMLQISI
FVSLLRGVLR NGVLYFLRDP ADPNYNPFRD LIDDPVHKHA RRVLLSVAVY GSLIVMLVFL
PVKLAMRMVP SIFPLDISVS DPFTEIPADM LLFQICIPFA VEHFKLRATI KSLLRYWFTA
VGWALGLTDF LLPSPEENGG QDNVNVEPGQ QDRLQVVQLG GQEQPMVAFA ADDDPNRGLM
ASGNSSVAEE FDEDEQTDSD RYSFVLRIVL LLVIAWMTLL IFNSALIVVP ISLGRALFNA
IPLLPITHGI KCNDLYAFVI GSYFIWTAMA GARYTIEHIR TKRAAVLLSQ IWKWSAIVIK
SSVLLSIWIF VIPVLIGLLF ELLVIVPMRV PVDESPVFLL YQDWALGLIF LKIWTRLVML
DHMMPLVDES WRIKFERVRE DGFSRLQGLW VLREIVFPII MKLLTALCLP YVLARGVFPV
LGYPLVVNSA VYRFAWLGCL GFSLLCFCAK RFHVWFTNLH NSIRDDRYLI GRRLHNFGED
MQEKKSEAGT PSEAPLVSNM RGTGIIRQLD RDADVGLRLR HVN
//
