ID A0A010RVV9_9PEZI Unreviewed; 743 AA.
AC A0A010RVV9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=CFIO01_08155 {ECO:0000313|EMBL:EXF84701.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF84701.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF84701.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF84701.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF84701.1}.
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DR EMBL; JARH01000150; EXF84701.1; -; Genomic_DNA.
DR RefSeq; XP_007591691.1; XM_007591629.1.
DR AlphaFoldDB; A0A010RVV9; -.
DR STRING; 1445577.A0A010RVV9; -.
DR KEGG; cfj:CFIO01_08155; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
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; cd00009; AAA; 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; IPR048867; ORC1_wHTH.
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; PF21312; ORC1_wHTH; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF82061; BAH domain; 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:UP000020467}.
FT DOMAIN 80..205
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 81939 MW; C25BECB96B34F475 CRC64;
MSVSAPETAP RGRRQSTKST GVIRDDSDDE LGIDDLPWEW ILASNDADTS QDHGDDTQTS
RKRRRANTEI RIIGARMGKF ECFVGDCVLL KAEGSNEAWV AIVCEFLQEE DGEKAANFMW
FSTEKEIRNK ERKRSDFLPN ELYISPSWDV NPLAAVNGTA VVISHQAFHQ KYPSGKIPRS
SPDFGKTFIC RRACNTRTAT YTDEFVWEEV YHASEQGVSD LIGFVKSQTK STRHGQAARQ
STPEQSYKMI SDRLAGASTP KRTPRADHST PKGDARITTT PGSRKRIVVK KTLEFTPLGT
RKLSPKRLQS SPFQLARSQL HVASVPRSLP CRESEFNLVY SHLEAAIADG SGSCIYIAGT
PGTGKTATVR EVISRLEDSV TADELDDFIF VEINGMKITD PHQSYTLLWE ALKGERVSPT
QAIDLLEREF SNPSPRRTPC VVLMDELDQL VTKNQSVMYN FFNWPGLRHS RLIVLAVANT
MDLPERTLSN KISSRIGLTR ITFPGYNHEQ LMKIIQSRLE CVPGSIVEAD AIQFASRKVA
AVSGDARRAL DICRRAVELA EGDSRVEKLA GDPEARRPNP SNGRPSDAPV KVTIATIKRA
INEATTNPVQ QYLRSLPFGP KLFLCSLLVR MQRSGAAETT FGDVVDEIHR IIKLDSTALE
STPLGALSTG PSGGDVGQGN GSIRVVQSLA LPQAALELMG AGIIVLEAHK PERPSKARLA
VGDEEVKMAF RDDGEVKALG LFF
//
