ID A0A251JZ08_MANES Unreviewed; 1118 AA.
AC A0A251JZ08;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=MANES_10G078500 {ECO:0000313|EMBL:OAY39236.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY39236.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY39236.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY39236.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CM004396; OAY39236.1; -; Genomic_DNA.
DR EMBL; CM004396; OAY39239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251JZ08; -.
DR EnsemblPlants; OAY39236; OAY39236; MANES_10G078500.
DR EnsemblPlants; OAY39239; OAY39239; MANES_10G078500.
DR Gramene; OAY39236; OAY39236; MANES_10G078500.
DR Gramene; OAY39239; OAY39239; MANES_10G078500.
DR OMA; HCEISII; -.
DR Proteomes; UP000091857; Chromosome lg10.
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:UP000091857};
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 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..125
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 72..119
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 124454 MW; 21D1BE3D31E46988 CRC64;
MEISSAAAPP PPNQRYSNDT MGPSSPSSSS SSSTASNRDL IEKEESNGAS SAPAAVSASR
SYEDDEEEED VCRICRNPGE AENPLRYPCA CSGSIKFVHQ DCLLQWLNHS NARQCEVCKH
AFSFSPVYAE NAPSRLPFQE FVIGMAMKTC HVLQFFLRLS FVLSVWLLII PFITFWIWRL
AFVRSFGEAQ RLFLSHISTT VILTDCLHGF LLSASIVFIF LGATSLRDYF RHLREIGGQD
AEREDEGDRN GARGARRPPG QANRNFAGEL NADDAGGGQG IAGAGQIIRR NAENVAARWE
MQAARLEAHV EQIFDGLDDG DGAEDVPFDE LVGMQGPVFH LVENAFTVLA SNMIFLGVVI
FVPFSLGRII LHYVSWLFSS ASGPLLSAVT PVIDSELSIA NWTMKSALNA VTNLTSEGQD
GGLLGQVADA LKVNASGLNE VSKNISTPLS ADLLKEANIG TSRLSDVTTL AIGYMFIFSL
VFFYLGIIAL IRYTKGEPLT LGRFYGIASI AETIPSLFRQ FLAAMRHLMT MIKVAFLLVI
ELGVFPLMCG WWLDVCTIRM FGKSMAQRLQ FFSVSPLASS LVHWVVGIVY MLQISIFVSL
LRGVLRKGVL YFLRDPADPN YNPFRDLIDD PVHKHARRVL LSVAVYGSLI VMLVFLPVKL
AMRMAPSIFP LDISVSDPFT EIPADMLLFQ ICIPFAIEHF KLRTTIKSLL RYWFTAVGWA
LGLTDYLLPK PEDNGGQENV NQEPGRQDRL PAIQPGAQDR ALVALAAADD SNRSLLDRGS
SNAAEHESDE QSDSECSFVL RIVLLLVVAW MTLLIFNSAL IVVPISLGRA LFNAIPLLPI
THGIKCNDLY AFIIGSYVIW TALAGARYST EHVRTNRATV LLSQIWKWCG IVLKSSALLA
IWIFVIPVLI GLLFELLVIV PLRVPVDESP VFLLYQDWAL GLIFLKIWTR LVMLDHMMPL
VDESWRVKFE RVREDGFSRL QGLWVLREIV FPIIMKLLTA LCVPYVLARG LFPVLGYPLV
VNSAVYRFAW LGCLSFSALC FCAKRFHIWF TNLHNSIRDD RYLVGRRLHN YGEDREERQS
EALSSELQNS NLIGSGLIQN AGEADVGMRQ RRVHQQDA
//
