ID G3AY54_CANTC Unreviewed; 763 AA.
AC G3AY54;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=CANTEDRAFT_118425 {ECO:0000313|EMBL:EGV65772.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV65772.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996512; EGV65772.1; -; Genomic_DNA.
DR RefSeq; XP_006684346.1; XM_006684283.1.
DR AlphaFoldDB; G3AY54; -.
DR STRING; 590646.G3AY54; -.
DR GeneID; 18248639; -.
DR KEGG; cten:CANTEDRAFT_118425; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IEA:UniProt.
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; 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; SM00439; BAH; 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|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Hydrolase {ECO:0000313|EMBL:EGV65772.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT DOMAIN 49..165
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 186..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 86103 MW; 440C5B78A51D23FD CRC64;
MLPINKLKGW TYSFLESEDN GDNESPRRSG RRRGAVSNKI MIKRDKDGLE LKAGDSIEVQ
QQKISDTQIA LIISIEFGIS SVVKLEVLWF NRSSEIDLTI NSDRSLEEKE LFITPFKDII
PVDVVKENVN VMTHEAYMEL SKKEHRAYFC RMASDEDGQH LSQPLSYDVV LATLKQDPKT
LVELIGDMTE ENDKKQRTET PTQKRNPEAS ESASQKARQS EKKLINISSE ESDSEDDRDV
EEIDLDSSDE EFHSAQTSPK KRRATSKPTT PRKTSLRKPR APPQNDRGFQ ESEEFMKKVL
GRKVMIYNSL PVPTLSSPKK RTKKNDSTYG NLDTSSTAFK DLKKKLHTSA KLSSLPCRED
EFTTLYLNVE NSIKEQTGCC LYISGTPGIG KTATIQEVMS SMEDLKEKGE VNDFDYVEIN
ALKLINPNYA YSVLWSKISG LDVSPSYAAL FLDAYFKEDS PSKKPIVVMV DELDSMATKK
QNVMYNFFNW PTYPNSKLIV LAVANTMDLP ERVLTNKISS RLGMRRIQFI GYTFEQLGCI
IDHRLSMIQR QSKQKVIIES DAINFASRKV ASVSGDARRA LQICRRAVEI AELEYQTSAN
GDEHSSDVFH VKIPHIAKAI NESTNSPIAQ YVASLSMASK LILCALLLRQ RRSGLAENPL
GDIIDEIKIL LRMASSKSLR LSGTISGHID VAEALLDGRM TNDQAKTSIR IENFKFLIFE
LIENGILNAQ DIKSERYRLV SLNVSQDEVM STLKRDDQVS GFL
//
