OBI1_PONAB
ID OBI1_PONAB Reviewed; 726 AA.
AC Q5RD97;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ORC ubiquitin ligase 1 {ECO:0000305};
DE Short=OBI1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5W0B1};
DE AltName: Full=RING finger protein 219;
GN Name=OBI1; Synonyms=RNF219;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin ligase essential for DNA replication origin
CC activation during S phase. Acts as a replication origin selector which
CC selects the origins to be fired and catalyzes the multi-mono-
CC ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S-
CC phase. {ECO:0000250|UniProtKB:Q5W0B1}.
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:0000250|UniProtKB:Q5W0B1};
CC -!- SUBUNIT: Associates with ORC complex. Binds to chromatin; association
CC is cell cycle-regulated, absent from mitotic chromosomes, is associated
CC with chromatin from G1 and partially released from chromatin from mid
CC S-phase. {ECO:0000250|UniProtKB:Q5W0B1}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q5W0B1}.
CC Note=Association to chromatin is cell cycle-regulated, absent from
CC mitotic chromosomes, is associated with chromatin from G1 and partially
CC released from chromatin from mid S-phase.
CC {ECO:0000250|UniProtKB:Q5W0B1}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q5W0B1}.
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DR EMBL; CR858019; CAH90260.1; -; mRNA.
DR RefSeq; NP_001125115.1; NM_001131643.1.
DR AlphaFoldDB; Q5RD97; -.
DR SMR; Q5RD97; -.
DR STRING; 9601.ENSPPYP00000006186; -.
DR GeneID; 100171997; -.
DR KEGG; pon:100171997; -.
DR CTD; 79596; -.
DR eggNOG; ENOG502QTFT; Eukaryota.
DR HOGENOM; CLU_023039_0_0_1; -.
DR InParanoid; Q5RD97; -.
DR OMA; PTNFAEN; -.
DR OrthoDB; 487392at2759; -.
DR TreeFam; TF329331; -.
DR Proteomes; UP000001595; Chromosome 13.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR CDD; cd16562; RING-HC_RNF219; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039209; OBI1.
DR InterPro; IPR035691; RNF219_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14609; PTHR14609; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="ORC ubiquitin ligase 1"
FT /id="PRO_0000055878"
FT ZN_FING 18..56
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 274..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..129
FT /evidence="ECO:0000255"
FT COILED 155..270
FT /evidence="ECO:0000255"
FT COMPBIAS 295..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0B1"
SQ SEQUENCE 726 AA; 81126 MW; 145F573D401BA636 CRC64;
MAQTVQNVTL SLTLPITCHI CLGKVRQPVI CINNHVFCSI CIDLWLKNNS QCPACRVPIT
PENPCKEIIG GTSESEPMLS HTVRKHLRKT RLELLHKEYE DEIDCLQKEV EELKSKNLSL
ESQIKTILDP LTLVQGNQNE DKHLVTDNPS KINPETVAEW KKKLRTANEI YEKVKDDVDK
LKEANKKLKL ENGGLVRENL RLKAEVDNRS PQKFGRFAVA ALQSKVEQYE RETSRLKKAL
ERSDKYIEEL ESQVAQLKNS SEEKEAMNSI CQTALPADGK GSKGSEEDVA SKNQGDSARK
QPSSSTSSSS HLAKPSSSRL CDTSSARQES TSKAELNCSK NKDLYQEQVE VMLDVTDTSM
DTYLEREWGN KPSDCVPYKD EELYDLPAPC TPLSLSCLQL STPENRESPV VQAGGSKKHS
NHLRKLVFDD FCDSSNVSNK DSSEDDISRS ENEKKSECFS SPKTAFWDCC STSYAQNLDF
ESSEGNTIAN SVGEISSKLS EKSGSCVSKR LNSIRSFEMN RTRTSSEASM DAAYLDKISE
LDSMMSESDN SKSPCNNGFK SLDLDGLSKS SQGSEFLEEP DKLEEKTELN LSKGSLTNDQ
LENGSEWKPT SFFLLSPSDQ EMNEDFSLHS SSCPVTNEIK PPSCLFQTEF SQGILLSSSH
RLFEDQRFGS SLFKMSSEMH SLHNHLQSPW STSFVPEKRN KNVNQSTKRK IQSSLSNASP
SKATKS
