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Database: UniProt
Entry: A0A0D9RYA5_CHLSB
LinkDB: A0A0D9RYA5_CHLSB
Original site: A0A0D9RYA5_CHLSB 
ID   A0A0D9RYA5_CHLSB        Unreviewed;       726 AA.
AC   A0A0D9RYA5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=ORC ubiquitin ligase 1 {ECO:0000313|Ensembl:ENSCSAP00000013594.1};
GN   Name=OBI1 {ECO:0000313|Ensembl:ENSCSAP00000013594.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000013594.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000013594.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000013594.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AQIB01099745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9RYA5; -.
DR   STRING; 60711.ENSCSAP00000013594; -.
DR   Ensembl; ENSCSAT00000015661.1; ENSCSAP00000013594.1; ENSCSAG00000017565.1.
DR   eggNOG; ENOG502QTFT; Eukaryota.
DR   GeneTree; ENSGT00390000013512; -.
DR   OMA; QLNPPWV; -.
DR   Proteomes; UP000029965; Chromosome 3.
DR   Bgee; ENSCSAG00000017565; Expressed in Ammon's horn and 7 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR   CDD; cd16562; RING-HC_RNF219; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039209; OBI1.
DR   InterPro; IPR035691; OBI1_RING-HC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14609:SF1; ORC UBIQUITIN LIGASE 1; 1.
DR   PANTHER; PTHR14609; RING FINGER PROTEIN 219; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          18..56
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          274..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          89..123
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          157..267
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        279..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   726 AA;  81151 MW;  2F950477B0347947 CRC64;
     MAQTVQNVTL SLTLPITCHI CLGKVRQPVI CINNHVFCSI CIDLWLKNNS QCPACRVPIT
     PENPCKEIIG GTSESEPTLS HTVRKHLRKT RLELLHKEYE DEIDCLQKEV EELKSKNLSL
     ESQIKTILDP LTLVQGNQNE DKHLVTDNPT KINPETVAEW KKKLRTANEI YEKVKDDVDK
     LKEANKKLKL ENGGLVRENL RLKAEVDNRS PQKFGRFAVA ALQSKVEQYE RETNRLKKAL
     ERSDKYIEEL ESQVAQLKNS SEEKEAMNSI CRRALPADGK GSKGSEEDVA SKNQGDSARK
     QPGSSTTGSS HLAKPSSSRL CDTSSARQES TSKAETNCSK NKDLYQKQVE IMLDVTDTSM
     DTYLEREWGN KPSDCVPYKD EELYDLPAPC TPLSLSCLQL STPENRESSV VQAGGSKKHS
     NHLRKLVFDD FCDSSNVSNK DSSEDDISRS ENEKKSECFS SPKTGFWDCC STSYAQNLDF
     ESSEGTTIAN SVGEIASKLS EKSGSCVSKR LNSIRSFEMN RTRTSSEASM DAAYLDKISE
     LDSMMSESDN SKSPCNNGFK SLDLDGLSKS SQGSEFLEEP DKLEEKTKLN LSKGSLTDDQ
     LENGNEWKPT SFFLLSPSDQ EMNEDFSLHS SSCPVTDEIK PPSCLFQTEF SQGILLSSSH
     RLFEDQRFGS SLFKMSSEMH SLHNHLQSPW STSFVPEKRN KNVNQSTKRK IQSSLSNASP
     SKATKS
//
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