ID F6Z2N2_HORSE Unreviewed; 801 AA.
AC F6Z2N2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN Name=ORC1 {ECO:0000313|VGNC:VGNC:21050};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000007647.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000007647.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000007647.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000007647.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000007647.4};
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: 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 AlphaFoldDB; F6Z2N2; -.
DR STRING; 9796.ENSECAP00000007647; -.
DR PaxDb; 9796-ENSECAP00000007647; -.
DR Ensembl; ENSECAT00000009960.4; ENSECAP00000007647.4; ENSECAG00000009370.4.
DR VGNC; VGNC:21050; ORC1.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_0_1_1; -.
DR InParanoid; F6Z2N2; -.
DR OMA; CKQHLLG; -.
DR TreeFam; TF313743; -.
DR Proteomes; UP000002281; Chromosome 2.
DR Bgee; ENSECAG00000009370; Expressed in inner cell mass and 21 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:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR CDD; cd04719; BAH_Orc1p_animal; 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; 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 SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT DOMAIN 38..164
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 177..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 90344 MW; 67E2C73679413BEE CRC64;
MKSRQTYSWV GRPLLDPKLH HQTYREMSVK VEGCSTELHI HVGQFVLVEG NDDENPYVAK
LVELFEDGSE PRSRKRARVQ WFIRFCEVPV CKQHLLGRKP AAQEIFWYDY PACDSNINAE
TIIGPVQVVA LAPDEVIPTD LKNEKTLFVK LSWNEKKFSP LSPELFAQLE KLQEGSPRCQ
KSVEAKTKNI ESPSCTTAER AVKRVESRHS SSKSRPAPTH PVTPRARKRL ELSSSPRTPN
TRISRQTSWA SPDSPRRTKR KAALSEITSP SKRSQPDGLQ TPSPARKAPE KTGEIQRRSC
AKDDKKVSAE RHMTLRPRVP ALKTTVLSEE RRLTPTRGGR RSSMVPSVIL IPENIRKREA
EEPEAQDEAV SSRHHTSRKS SLLTLNQIKQ QLRFLGKSES DSEDEEFLPA AEIPDSSSEE
EEDSTSPLPR TPSGASRNLR SSTKLSLQTP SKTPKKTPKP RTPHHATPRI RSRNLAAQEP
ASVLEEARLR LHVSAVPESL PCREQEFQDI YNFVESKLLD QTGGCMYISG VPGTGKTATV
HEVIRGLQQA AQANDVPPFQ YIEVNGMKLT EPHQVYVQIL QKLTGQKATA IHAAELLAKR
FRTQGSSQET TVLLVDELDL LWTQKQDVMY NLFDWPTHKE ARLVVLTIAN TMDLPERIMM
NRVSSRLGLT RMSFQPYTHS QLQQILGSRL KHLRAFEDDA IQFVARKVAA LSGDARRCLD
ICRRATDICE FSCQKPGSPG LVTVAHLLEA VDEMFSSSYI TAIKNSSVLE QSFLRAILAE
FRRSGLEEAT FQQWLVMFLL E
//
