ID A1CQ43_ASPCL Unreviewed; 801 AA.
AC A1CQ43;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=ACLA_024800 {ECO:0000313|EMBL:EAW07764.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07764.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07764.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07764.1; -; Genomic_DNA.
DR RefSeq; XP_001269190.1; XM_001269189.1.
DR AlphaFoldDB; A1CQ43; -.
DR STRING; 344612.A1CQ43; -.
DR EnsemblFungi; EAW07764; EAW07764; ACLA_024800.
DR GeneID; 4701146; -.
DR KEGG; act:ACLA_024800; -.
DR VEuPathDB; FungiDB:ACLA_024800; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR OMA; YEDHPWE; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IEA:EnsemblFungi.
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:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:1902969; P:mitotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:EnsemblFungi.
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 InterPro; IPR036390; WH_DNA-bd_sf.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000006701}.
FT DOMAIN 99..234
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 88471 MW; FCD6CF6120E31E30 CRC64;
MAVTLTDEVE ETPARRRNAR QRAQLWMTKG GLVRDDSDDE LGDEDHPWHW VYETELEEIK
NEESAPAAAN ESEEKSARKR SARSSRRQPN IVGARMGTFE CRLGEIVLLK SPEPGKDWVG
IITEFFEEEG DENEDEVVKS VNIMWFASPD EFMSTKNKRR ADALPNEQYL TADFNVNPIN
SISGKATVMS TGAFYAKYPN GTPPKGKEEL ADFNKCIICR RGVNQVQGRY TDEFVWEEVY
RKDKISELIA LIKDGLKAAK KRKHVDDDYV ETKDDEEFAP TTPRKRQKVA SNATPQSRRK
KALTTPSHKR IIVKKPLEFT PLGTRVLPPS HFDSPYRQAR TLLHVSTVPT SLPCRKTEFD
TVYNHLSAAI MEGTGTCIYI SGTPGTGKTA TVREVVAQLN SAVLAEEMDD FIFVEINGMK
VTDPHQSYSL LWEALKGDRV SPSHALDLLE REFSHPSPRR VSCVVLMDEL DQLVTKNQSV
MYNFFNWPAL RHSRLIVLAV ANTMDLPERT LSNKISSRLG LTRITFPGYK HTDLMEIITT
RLASVPGNIV DADAIQFASR KVAAVSGDAR RALDICRRAV EIAEQAREAA KVEDLDSEEN
ADDAESLPPT PSKTPARRQK ASIKKNLKTE SPQKNPKQLV GRVTIATIKQ AIQEATSTPL
QQSLRCLPLS AKLFLAALLA RIRRTGISES TFGDVIDEAK RIADAAVAVA GAAGAGIKDF
LLAGNNGARV RALGFAAMEL MNSGVLALEN GAGAKGPLGS SAIPHRGDRS GKVRLRVAAE
DVRAAFREDA EAKGLGLGVD Q
//
