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Database: UniProt
Entry: A0A3P9CP98_9CICH
LinkDB: A0A3P9CP98_9CICH
Original site: A0A3P9CP98_9CICH 
ID   A0A3P9CP98_9CICH        Unreviewed;       899 AA.
AC   A0A3P9CP98;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|ARBA:ARBA00019081, ECO:0000256|RuleBase:RU365058};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005023854.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005023854.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005023854.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_004569395.1; XM_004569338.1.
DR   AlphaFoldDB; A0A3P9CP98; -.
DR   STRING; 106582.ENSMZEP00005023854; -.
DR   Ensembl; ENSMZET00005024638.1; ENSMZEP00005023854.1; ENSMZEG00005017849.1.
DR   GeneID; 101484023; -.
DR   KEGG; mze:101484023; -.
DR   CTD; 4998; -.
DR   GeneTree; ENSGT00530000063498; -.
DR   OrthoDB; 118994at2759; -.
DR   Proteomes; UP000265160; LG17.
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:0043009; P:chordate embryonic development; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR   CDD; cd00009; AAA; 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:UP000265160}.
FT   DOMAIN          44..167
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          171..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100204 MW;  6DAD673A3A75223C CRC64;
     MKYFTRMKIR RVYEWSGRAR SFNRRLKTHD YDSFAISVEG LSKIIINTGQ HILIEGYDED
     NPYVAKVTRL YGDENGQQMK AVVQWFMRVS ELPVNKLKLL GREPHPQEIF YYECRNCDNE
     VNVESILRPV KVKHLDSNDP FPDSSDKDTL YVKLSWDSKV FGVVNSTVME SPAEPAPASS
     PPSCLKPSLP ISPSCSQSAA TPRGPSRRVL PTPDHAIMQK ASLGEVGCSS VGTPANVEAE
     SLHSATKLSA SKCLSAKRRN ATARTPGVRK RLELSSPDKS VTGEEVLSQL LNEELESKVT
     LTRRLPPSAA HPLPVTHSLT PLRKAHRPTG ARCGVPSSVF LNKLSDSDSP LSPAKDDSTR
     ATTVSQKKEL KTIKEPVLSV LAEVENEKSP MVTETPRSSK RKSAMVVSSR IKKQLNLLEN
     DQDLNSSGEE EDEFVPSKND LLSSSEEEGQ DEDGPNIDDQ VSAKKFRYVA TGSGNSRSKR
     KSYSSARTQR RTPAKKISPG TPKTPRHATP SIPIRSLQTQ QPANILEEAR ARLHVSSVPE
     SLPCREQEFQ DIYSFVESKI IDNTGGCMYI SGVPGTGKTA TVHEVIRCLQ HAADMDEIPS
     FHFIEINGMK MTDPHQAYVQ ILQKLTGQKA TPDHAAVLLE KRFSNLAPRK ETIVMLVDEL
     DLLWTRKQNV MYNLFDWPTR RHARLVVLTI ANTMDLPERI MINRVASRLG LTRMSFQPYS
     FKQLQEIIMS RLNKLKAFEE DALQLVSRKV AALSGDARRC LDICRRATEI CEHSAADPSS
     TGLVGMSHVM EALNEMFSSA YITAIRCAST QEQLFLRAAI AEFRRLGLEE ATFQQVFVQH
     QALCRIEGLR PIGVSEGLAV CQRLGACRLL LLEPSHLGVL QHIRLNVSQD DIFYALKAD
//
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