ID A0A1S2YJ20_CICAR Unreviewed; 1103 AA.
AC A0A1S2YJ20;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC101509426 {ECO:0000313|RefSeq:XP_004505248.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004505248.1};
RN [1] {ECO:0000313|RefSeq:XP_004505248.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004505248.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004505248.1; XM_004505191.3.
DR AlphaFoldDB; A0A1S2YJ20; -.
DR GeneID; 101509426; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000087171; Chromosome Ca6.
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:UP000087171};
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 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 628..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..114
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 61..108
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 123398 MW; 198317CCC1BD16C1 CRC64;
MEIDHEPPPS LDGSPLATDT PSSSSASSPR GSKGKEIEPT ASTAPPPAKY DDDDEEEEDV
CRICRNPGDA DNPLRYPCAC SGSIKFVHQD CLLQWLNHSN ARQCEVCKHP FSFSPVYAEN
APARLPFQEF VVGMAMKACH VLQFFLRLSF VLSVWLLIIP FITFWIWRLA FVRSLGEAQR
LFLSHLSTAV ILTDCLHGFL LSASIVFIFL GATSLRDYFR HLREIGGQDA DRDDEVDRNG
ARIARRPPGQ ANRNVNGDGN GEDAGGAQGV AGAGQVIRRN AENVAARWEM QAARLEAHVE
QMFDGLDDAD GAEDVPFDEL VGMQGPVFHL VENAFTVLAS NMIFLGVVIF VPFSLGRVIL
HYLSWFFSAS SGPVLSVVVP PTDTSLSLAN ITLKNALTAV KNLSSETQES GSIGQIAEML
KVNASELREM SNNVSASVSA DLLKGGSIGT FRISDVTTLA IGYIFILTLI FCYFGIVALI
RYTKGEPLTT GRFYGIASIA ETIPSLFRQF LAAMRHLMTM VKVAFLLVIE LGVFPLMCGW
WLDVCTIQMF GKTMVHRVQF FTASPLASSL VHWVVGIVYM LQISIFVSLL RGVLRNGVLY
FLRDPADPNY NPFRDLIDDP VHKHARRVLL SVAVYGSLIV MLVFLPVKLA MRMAPSMFPL
EILLSDPFTE IPANMLLFQI CIPFAIEHFK LRTTIKSLLR YWFTAVGWAL GLTDFLLPRP
DENGNQENGN GERARQERLQ IVQAGVHDQG MVPFAGDDLN RVTNADAGED YDNDEQSDSD
YAFVLRIVLL LVIAWMTLLV FNSALVVVPI SLGRILFNSI PRLPITHGIK CNDLYAFIIG
SYVIWTAVAG VRYSIEQIRK RRTSVLLNQI WKWCSIVVKS SALLSIWIFV IPVLIGLLFE
LLVIVPMRVP VDESPVFLLY QDWALGLIFL KIWTRLVMLD HMMPLVDESW RVKFERVRED
GFSRLQGLWV LREIVLPIIM KLLTALCVPY VLARGMFPVL GYPLVVNSAV YRFAWLGCLS
FSFLCFCAKR FHVWFTNLHN SIRDDRYLIG RRLHNFGEHV VKANEAETST GVQDTILVGT
NLNQQDRDAD VGLRLRRINQ QAG
//
