ID A0A0D9ZUD4_9ORYZ Unreviewed; 1291 AA.
AC A0A0D9ZUD4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM05G03670.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM05G03670.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM05G03670.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
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DR STRING; 40148.A0A0D9ZUD4; -.
DR EnsemblPlants; OGLUM05G03670.1; OGLUM05G03670.1; OGLUM05G03670.
DR Gramene; OGLUM05G03670.1; OGLUM05G03670.1; OGLUM05G03670.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_262245_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16571; RING-HC_SIAHs; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR10315; E3 UBIQUITIN PROTEIN LIGASE SIAH; 1.
DR PANTHER; PTHR10315:SF162; OS01G0122000 PROTEIN; 1.
DR Pfam; PF21362; Sina_RING; 3.
DR SUPFAM; SSF49599; TRAF domain-like; 5.
DR PROSITE; PS51081; ZF_SIAH; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 103..161
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DOMAIN 607..665
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DOMAIN 1006..1064
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 139891 MW; 9FD8C906A3E16420 CRC64;
MPPPPPPPPP PRPFSRKPSE PAAPSTRAVV AVAGVTVEDA DALECGVCFL PLRPPIFQCE
VGHVVCSPCR DKLAPAGRCH VCRVAVAGGE YRRCYALERL VDAIRVACPH AAHGCGATPA
YHALDAHRRA CPHAPCHCPG ERCGFVGSTA ALVDHFAAAH RWPCAWASEA VSVLLRDGLN
FLRVVDLRRP GDASHHRLVM LNVTREALGR AISVLCIHPL AAAAAAAKTM QCELELFVPL
NGDDGVDGGQ LRRRHYQKSE FPLGCGDLAD HKTTFKFVVP RCVVGDDDEG GIRIRDKVSE
SWPCTTNVRA GETVSVHLRD GLAFLRVHHH RRGGSATYSD HLIMLNVTRE PYGRVVSVLC
IRPHAAAEHQ VSSPPPPAMQ CELLLVSRFG YDGDGGHCRS HYQKSEFLIG CSDLADGLPD
REQNFQFMVP RCVVGDDDEG GIQIHRIRHD PKLTERKQWK QPTTLQRKMQ RSMASSSHPS
RRAMSEEEED DNGGGEEEES QRETAVVEEE EEESTGVHVG EAEMAASEEQ APPSSSRRAF
VTVADADALE CGVCRLPLRP PVFQCEDGHV VCSPCRDKLA AAAAVRCHVC GGGGYRRCHA
FERLVDAIRV ACPHAAHGCA ARVAYHGLDA HRRACPHAPC HCPGERCGFV GSTAALVDHF
AAAHRWPCAW ASEAVSVLLR DGLNFLRVVD LRRPGDASHH RLVMLNVTRE ALGRAISVLC
IHPLAAAAAA AKTMQCELEL FVPLNGDDGV DGGQLRRRHY QKSEFPLGCG DLADHKTTFK
FVVPRCVVGD DDEGGIRIRD KVSESRRVMA ALDHEGDTMA RKKRRVYVAI EEIESHGHEE
DDDGGEEVEE EDEQSHGEAD GDGDDAAAAM EESDGHDEEG DNGGDEPDQS PDGDDMEEEE
ERGGGGGGGV HGGEAEVETF RHSEQASSAR PVVAVAGVTV EDADALECGV CCLPLRPPIF
QCEVGHVVCA PCRDKLAPAG RCHVCRAAVA GGEYRRCHAL ERLVDAIRVA CPHAAHGCAA
RPAYHDVEAH RLACPHGPCH CPGERCGFVG STAALVDHFA AAHRWPCAWA SEAVSVLLRD
GLNFLRVVDL RRPGDASHHR LVMLNVTREA LGRAISVLCI HPLAAAAAAA KTMQCELELF
VPLNGDDGVD GGQLRRRHYQ KSEFPLGCGD LADHKTTFKF VVPRCVVGDD DEGGIRIRPL
GRAISVLCIH PHAAPAAEMQ CELRLHVSRP ADDAGGGLCI SHYQKSVFHI GYSDLADGVP
DRRRRFQFVV PRHVVGGDNE DGVQIRVRIK Y
//
