ID A0A1S3FN16_DIPOR Unreviewed; 863 AA.
AC A0A1S3FN16;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|ARBA:ARBA00019081, ECO:0000256|RuleBase:RU365058};
GN Name=Orc1 {ECO:0000313|RefSeq:XP_012877745.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012877745.1};
RN [1] {ECO:0000313|RefSeq:XP_012877745.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012877745.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent, however specific
CC DNA sequences that define origins of replication have not been
CC identified so far. ORC is required to assemble the pre-replication
CC complex necessary to initiate DNA replication.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase. Interacts
CC with CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the
CC G1 phase and with less affinity during mitosis, when phosphorylated.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365058}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000256|ARBA:ARBA00008398,
CC ECO:0000256|RuleBase:RU365058}.
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DR RefSeq; XP_012877745.1; XM_013022291.1.
DR AlphaFoldDB; A0A1S3FN16; -.
DR STRING; 10020.ENSDORP00000005569; -.
DR GeneID; 105990001; -.
DR KEGG; dord:105990001; -.
DR CTD; 4998; -.
DR InParanoid; A0A1S3FN16; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04719; BAH_Orc1p_animal; 1.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 45..171
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 196..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 98107 MW; 134E82C866086283 CRC64;
MTPYSTRQKT RQIYSWVGRP LLDRQLHYQT YKEISMKTRS CPTEIRIQVG QFVLIEGDDD
EKPYVAKLIE LFEDDSKLHF KKRARVQWFV RFSEVPLSKQ HLLGRKPHKQ EIFWYDYPAC
NNNISAETII GPVEIVALAA DEMFPVDLKH EKTLFVKLSW NEKNFKPLSL ELLAELKKLQ
RVNSICQKPL EAKTMTQESP SLTTAEHVVK RIESSHSSSK SRQTPTHPVT PNARKRLELN
DCPRTPNTRI SQQTSCVALG SPGRTKRKAV FLESTSPYKK SQLDGVKASS PVLKVPGKTG
EVPYFCAEDD KKSSSECQMT LRTRVPTLKI METEESSLSP VRRNKRSSVV PSVILKPGKI
EKREAKEPEA GSEATITSHR IHRKSALLTL SRIRQHLWLL EDKKGDQEEE EFMPKAEVSD
LSSEEEDTST PSLPRRNPQR QSRILQPSLS PSMQTPSKTP KKPVKPRTPR HATPQIRSRN
LAAQEPASVL EEARLRLHVS AVPESLPCRE QEFQDIYNFV ESKLLDRTGG CMYISGVPGT
GKTATVHEVI RCLKQAAQTD DVPSFQYVEV NGMKLTEPHQ VYVQILQKLT GQKVTANHAA
ELLAKRFCTR GSSRETTVLL VDELDLLWTH KQDVLYNLFD WPTHKEARLV VLTIANTMDL
PERILMNRVS SRLGLTRMSF QPYTHNQLKQ ILVSRLKHIK AFEDDAMQLV ARKVAALSGD
ARRCLDICRR ATEICELDHQ KNDSPGLVTV AHLMKAVDEM FSSSFITAIK NASVLEQGFL
RAILAEFRQS GLEEATFQQI YTQHVALCRM EGLPYPTMSE TMAVCSRLGS CRLLLVESSR
NDLLLRVRLN VSQDDVLYAL KEE
//
