ID G0SCG6_CHATD Unreviewed; 1017 AA.
AC G0SCG6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CTHT_0057150 {ECO:0000313|EMBL:EGS19092.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS19092.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; GL988045; EGS19092.1; -; Genomic_DNA.
DR RefSeq; XP_006696037.1; XM_006695974.1.
DR AlphaFoldDB; G0SCG6; -.
DR STRING; 759272.G0SCG6; -.
DR GeneID; 18259753; -.
DR KEGG; cthr:CTHT_0057150; -.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_0_1; -.
DR OMA; NRCSFAD; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17755; MCM4; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 595..803
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 111881 MW; F5DC3F319674DE8A CRC64;
MSSPSKRSTR STRSSATPRP EGSDRTPRAT RASQLASSPL FYQSSSPLRQ SSEASQPGPS
QPPSSPLRQT ETQESRNDGD RTPRASGALI GDSSPIRYDP SSSPGRAAQH SDLRSESSAL
FVGSQRSLTF RSHRGDINSD LARTPRAPRR VFLDDAGRVI RDGSAVPTSD GNSFAHHNPH
TSEANALGGS SQSLVWGTTV SLEDTFVSFR DFLKNFTKKY RMWADGATEA ETNADPTANS
KPYMEALENM LLLGTNKLYL DLRDLKAYPR TVKLWHQTLN YPTEIIPVMD QCVHDCMIEL
ARIEMTNQRA AQVAASSNNS NNNNNNNNNN NAPQPSQQSS EFAYPSSDPA TPRPAGQQAT
REPTLEDQVM QTPYLVRPFG LDKTTNLRDL NPSDMDKLIS IKGLVIRTTP VIPDMKQAFF
KCSVCGHSVT VELDRGKIRE PTECPRARCK SKNSMQIIHN RCVFEDKQVI KLQETPDEVP
AGQTPHAVSV CVYNELVDFC KAGDRVELTG IYKVTPVRVN PRLRTVKAVH KTYVDVVHVQ
KVDRKRMGAD PSTLDLPEDE DMVHVSAGGQ SLDEVKKVTP EEEARIKEVA ARPDVYELLA
RSLAPSIYEM DDVKKGILLQ LFGGTNKTFD KGASPKYRGD INILLCGDPS TSKSQLLSYV
HRIAPRGVYT SGKGSSAVGL TAYVTRDPET RQLVLESGAL VLSDGGVCCI DEFDKMNDAT
RSVLHEVMEQ QTVSVAKAGI ITTLNARTSI LASANPIGSR YNPELSVPQN IDLPPTLLSR
FDLVYLILDR PDEKNDQRLA RHLLSMYLED KPETAQTNND ILPVEFLTTY ISYARSHIHP
VISDPAAQEL VSSYVAMRKL GQDVRAAEKR ITATTRQLES MIRLSEAHAK MRLSPVVEVS
DVREAVRLIH AALKTAATDA QGRIDMSLLT EGTSAAERKR REDLKGMVVK LLDEMTANGQ
SVRYSEVARR LAEVVGGPGG QVDSGEFGEV MRALEMEGAV MIVGEGPRKS VRRVTGV
//
