ID F2PS59_TRIEC Unreviewed; 787 AA.
AC F2PS59;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=TEQG_03988 {ECO:0000313|EMBL:EGE04815.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995735; EGE04815.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PS59; -.
DR VEuPathDB; FungiDB:TEQG_03988; -.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_012774_1_1_1; -.
DR Proteomes; UP000009169; 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; 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 SMART; SM00382; AAA; 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}.
FT DOMAIN 75..209
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 86762 MW; AC57ACEAA53009EE CRC64;
MATQDTPETK SKRAQEIARQ WLTKGGIFHE DSDDELGSED LPWEWIYEEP QPSPAKPSKG
KKSGPKIIGA RMGSFECRIG HIVLLKSPEA GKDWAGIIYE FLDDLDPDSG EIVKSMSLMW
FTSPDEFLST KNKKRADALP NEQYITTDFN INPLMSINGR ATVMSKDAFY KKYPDGKPPK
GKAAAAEFNK CIICRRGVKQ LQGRYTDEFI WEDIYTESED GVFELVEFIR EALSRARKRA
QKGTGPAKDK QDDYAPSTPR KRQKTESAAG TPQSRQRQKY LTTPTHKRIK VKRPLEFTPL
STRTLSPSHF TASPYRQARN LLHVSSVPTS LPCRDAEFNS VYDSLHTAIS DGTGTCIYIS
GPPGTGKTAT VRDVIAHLNT RVLDEEMDDF IFVEINGMKV TDPHQSYSML WEALKGDRIS
PSHALDLLSR EFSRPSPRRV PCVVLMDELD QLVTKNQSVM YNFFNWPALR HSRLVVLAVA
NTMDLPERTL SNKISSRLGL TRITFSGYKY QELMEIIGSR LENVPGNIVD ADAIQFASRK
VAAVSGDARR ALDICRRAVE IAEQISETKA REKHKSLIAS ANANGDADLE FLPPTPSKSV
SRRKAAAAIL SSPRKGDKKG AESTTEDSLP RVTIATIKQA IQEATSTPLQ QALRCLPLAS
KVLLAGLLAR IRRTGINEST VGDILDEAKR ISDAATSVSS SSSTKLKETL ICNSRIQGMG
FATVDLIDAG LVVLEGGHGT KSGDGMSHAL GKGNRSSKVR LRIAAEDARA AFRDDPEGNM
LGLGVEG
//
