ID A0A0D2VAL1_GOSRA Unreviewed; 1124 AA.
AC A0A0D2VAL1;
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_013G045900 {ECO:0000313|EMBL:KJB79369.1};
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:KJB79369.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB79369.1, 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; CM001752; KJB79369.1; -; Genomic_DNA.
DR RefSeq; XP_012462068.1; XM_012606614.1.
DR AlphaFoldDB; A0A0D2VAL1; -.
DR STRING; 29730.A0A0D2VAL1; -.
DR EnsemblPlants; KJB79369; KJB79369; B456_013G045900.
DR GeneID; 105782110; -.
DR Gramene; KJB79369; KJB79369; B456_013G045900.
DR KEGG; gra:105782110; -.
DR eggNOG; KOG1609; Eukaryota.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000032304; Chromosome 13.
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 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 899..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..131
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 78..125
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 125037 MW; 6A257EE7226028F8 CRC64;
MEIAPAVPPS HPLDGENPVS SSDDVLADSG KPSPSTSTSS SSSEKDEKAT SSTASTVSLG
AVASRYDPDM EEEEEDVCRI CRNPGDADNP LRYPCACSGS IKFVHQDCLL QWLNHSNARQ
CEVCKHAFSF SPVYAENAPA RLPFQEFVVG MVMKACHILQ FFLRLSFVLS VWLLIIPFIT
FWIWRLAFVR SFGEAQRLFL SHISTTIILT DCLHGFLLSA SIVFIFLGAT SLRDYFRHLR
ELGGQDADRE DEADRNGARA ARRPAGQANR NFAGDANGED AGGAQGVGGA GQMIRRNAEN
VAARWEMQAA RLEAHVEQMF DGLDDADGAE DVPFDELVGM QGPVFHLVEN AFTVLASNMI
FLGVVIFVPF SLGRIILHYV SWLFSSASGP VLSAVMPMTD TTLSLANITL KNALTAVTNL
TSEGQDNSML GQVAEILKAN SSAVGEVSSN KSAPFSADLL KGATIGASRL SDVTTLAIGY
TFIFSLVFFY LGIVTLIRYT RGEPLTMGRF YGIASIVETI PSLFRQFLAA MRHLMTMIKV
AFLLVIELGV FPLMCGWWLD ICTIRMFGKS MSQRVQFFSV SPLASSLIHW VVGIVYMLQI
SIFVSLLRGV LRNGVLYFLR DPADPNYNPF RDLIDDPVNK HARRVLLSVA VYGSLIVMLV
FLPVKFAMKM APSIFPLDIS VSDPFTEIPA DMLLFQICIP FAIEHFKLRT TIKSLLRYWF
TAVGWALGLT EFLLPRPDEN GGQENANVEP GQLDRPQIVQ LGGQEQAMVA FAADDDPNRG
LLASGNSNVL EEFDGDERAD SDRYGFVLRI VLLLVVAWMT LLIFNSALII VPISLGRALF
NAIPLLPITH GIKCNDLYAF VIGSYVIWTA IAGARYSIEH IKTKRAAVLF GQISKWSAIV
VKSSMLLSIW IFVIPVLIGL LFELLVIVPM RVPVDESPVF LLYQDWALGL IFLKIWTRLV
MLDHMMPLVD ESWRVKFERV REDGFSRLQG LWVLREIVFP IIMKLLTALC VPYVLARGVF
PVLGYPLVVN SAVYRFAWLG CLCFSCLCFC AKRFHVWFTN LHNSIRDDRY LIGRRLHNFG
ENSEEKQNEA GSYSETQISD LRDTGIIQHD REVDVGLRLR RAAN
//
