ID A0A068TMK6_COFCA Unreviewed; 1108 AA.
AC A0A068TMK6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=GSCOC_T00014464001 {ECO:0000313|EMBL:CDO97197.1};
OS Coffea canephora (Robusta coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=49390 {ECO:0000313|EMBL:CDO97197.1, ECO:0000313|Proteomes:UP000295252};
RN [1] {ECO:0000313|Proteomes:UP000295252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
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; HG739085; CDO97197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068TMK6; -.
DR STRING; 49390.A0A068TMK6; -.
DR EnsemblPlants; CDO97197; CDO97197; GSCOC_T00014464001.
DR Gramene; CDO97197; CDO97197; GSCOC_T00014464001.
DR InParanoid; A0A068TMK6; -.
DR OMA; WLHYSLV; -.
DR PhylomeDB; A0A068TMK6; -.
DR Proteomes; UP000295252; Chromosome 2.
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:UP000295252};
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 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 840..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1003
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1015..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..116
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 63..110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 123344 MW; 08D42247D4364956 CRC64;
MEIAPMVPAS SDGRDRGSLS VSSPKAEPTS SASASSSSVV KEVTSNSAAV SRFDDDDEEE
DVCRICRNPG DTDNPLRYPC ACSGSIKFVH QDCLLQWLNH SNARQCEVCK HSFSFSPVYA
ENAPTRLPFR EFLVGMAMKA CHVLQFFLRL SFVLSVWLLI IPFITFWIWR LAFVRSFGEA
QRLFLSHIST TVVLTDCLHG FLLSASIVFI FLGATSLRDY FRHLRELGGQ DADRDDEGER
NGARAARRPP GQANRNLAGE GNGEEAVGQQ GAGGAGQIIR RNAENVAARW EMQAARLEAH
VEQMFDGLDD ADGAEDVPFD ELVGMQGPVF HLVENAFTVL ASNMIFLGVV IFVPFSLGRV
ILYYLSWLLS SATSPVLSTV MPLTESALSL ANITLKNALT AVANLTSDNQ DSNLLGQVAG
MLKVNGTGLN EGSSNLTTSF SSELLKGQAV GPSRLSDVTT LAVGYMFIFS LIFFYLGVVA
LIRYTRGEPL TMGRFYGIAS IAETIPSLLR QFVAAMRHLM TMIKVAFLLV IELGVFPLMC
GWWLDVCTIR MFGKSIAQRV EFFSVSPLAS SLVHWVVGIV YMLQISIFVS LLRGVLRNGV
LYFLRDPADP NYNPFRDLID DPVHKHARRV LLSVAVYGSL IVMLVFLPVK LAMRVAPSIF
PLDISVSDPF TEIPADMLLF QICIPFAIEH FKLRTTIKSL LRYWFTAVGW ALGLTDYLLP
KPEDNGAHDN GNGDLGRQDR ANGHLGGQDR ALVGVVPDDV NRARNAVGNA SMSEELDNDE
HSDTDRCSFV LRIVLLLVVA WMTLLIFNSS LIVVPVSLGR TLFNALPLLP ITHGIKCNDL
YAFVIGSYVI WTAVAGARYS IEQIRTNRAT ILFKQIWKWC GIVIKSTALL SIWIFVIPVL
IGLLFELLVI VPMRVPVNES PVFLLYQDWA LGLIFLKIWT RLVMLDQVLP LVDESWRIKF
ERVREDGFSR LQGFWVLREI VFPIIMKLLT ALCVPYVLAR GVFPIFGYPL VVNSAVYRFA
WLGCLGLGLL WYCAKRFHVW FTNLHNSIRD DRYLIGRRLH NYGEGVERQN GSVSQEGQNS
NEHGTSLLQS EPDAADVGIR QRHVRQDA
//
