ID W5MGU6_LEPOC Unreviewed; 897 AA.
AC W5MGU6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|ARBA:ARBA00019081, ECO:0000256|RuleBase:RU365058};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007605.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007605.1}
RP IDENTIFICATION.
RG Ensembl;
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: ORC is composed of six subunits.
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 EMBL; AHAT01015947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015211125.1; XM_015355639.1.
DR AlphaFoldDB; W5MGU6; -.
DR Ensembl; ENSLOCT00000007614.1; ENSLOCP00000007605.1; ENSLOCG00000006282.1.
DR GeneID; 102691222; -.
DR KEGG; loc:102691222; -.
DR CTD; 4998; -.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_0_1_1; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000006282; Expressed in ovary and 10 other cell types or tissues.
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; 1.10.8.60; -; 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:UP000018468}.
FT DOMAIN 46..171
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 211..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 99592 MW; 7ECAFE7333E4D2B4 CRC64;
MSRYLTRQRK RRVYTWNGKP TLIDRKLQFF YYDGFFMYAE GTSEASSIKL GQYILIEGDD
DDNPFIAKLL KLYGSGPRER ENKRAEVQWF ARFSEVPSNK RKMLGRAPHP QEIFLYDVTN
CDCEIDVETI LGAVEVRHVE PQAPFPVEQS NGTLYVKLSW NGKAFRAVTA EQVGQGSGAS
LAPAPRGSLP TPDVAVMKRA LAGAVSVGVP ASSQAESHHS SSKYSQSKGL SARRQAKCSS
TPGVRKKLQL SSPGKSAGAR LTRDDVLEEL LHTEIENQKS ELTSKVLATP PRPLAITVRL
SPIRSVAITS PAVRICPLQG AQDPAGSTRP DRNQESAKDT SGVSPLDGEV DKVRVSTRSS
KTPCKKEDTP RKSAVRPQKK EEAKDNNADT EQTAMTPRSK RKSAMLVSSR IRKQLNLLNG
VQDAHSDVDD DEDEGFIPSK KDLESSSEEE AEADSEGDSI AEKKSRRAAG ACTPRARRKA
STPSRTPRKT PSKKIAPSTP RTPHNATPSI PSRSLPAKKP GNILEEARAR LHVSSVPESL
PCREQEFQDI YSFVESKVID GTGGCMYISG VPGTGKTATV HEVMRCLLHA ADQDEIPPFN
FIEINGMKMT DPHQAYVQIL QKLTDQKATA DHAASLLEKR FSTPAPKRET TVLLVDELDL
LWTRKQNVMY NLFDWPTRRH AKLVVLAIAN TMDLPERIMI NRVASRLGLT RLSFQPYTFK
QLQQIITSRL NRVRAFEEDA LQLVSRKVAA LSGDARRCLD ICRRATEICE FSNNRNSSSG
LVGMSHVMEA LDEMFSSPYI TAIRCASLQE QLFLRAVIAE FRRLGLEEAT FQQVFQQHRA
LCRVEGLQPV SLSEGLAACL RLGACRLLLL EPSRCDLLLR VRLNVSQDDV LYALKED
//
