ID Q7SHS5_NEUCR Unreviewed; 1013 AA.
AC Q7SHS5;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 142.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=NCU02539 {ECO:0000313|EMBL:EAA36434.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA36434.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA36434.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002236; EAA36434.1; -; Genomic_DNA.
DR RefSeq; XP_965670.1; XM_960577.2.
DR AlphaFoldDB; Q7SHS5; -.
DR STRING; 367110.Q7SHS5; -.
DR PaxDb; 5141-EFNCRP00000002018; -.
DR EnsemblFungi; EAA36434; EAA36434; NCU02539.
DR GeneID; 3881804; -.
DR KEGG; ncr:NCU02539; -.
DR VEuPathDB; FungiDB:NCU02539; -.
DR HOGENOM; CLU_000995_7_0_1; -.
DR InParanoid; Q7SHS5; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; 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 Cell cycle {ECO:0000313|EMBL:EAA36434.1};
KW Cell division {ECO:0000313|EMBL:EAA36434.1};
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:UP000001805}.
FT DOMAIN 593..801
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 111576 MW; 1980D7DB790AFF3E CRC64;
MSSPAKRRTT RSSQSATPRT TRSSQAGPSS ATPRQTRASQ LASSPLFYEP SSPANGAAPV
SSPLRQMSNT QSTAHQGNAP SSPLRQQTET QSDADRTPRA NGRSQLIGDS SPIRYASSSS
PGRQLTQQSD LRSESSQLFV SSQRSVAGRS RRGDINGDPL RTPAQIPRRI ILDDAGRVIR
DAPGSDANSF VTNNPNTSEA DALGGQSQGL VWGTTISLDD SFSAFKDFLR NFTRKYRMWA
DGADEAETIG HPDADSKPYW EALENMLLLG TNKLYLDLRD LKSYPRTLKL WHQAQHYPTE
IIPVMDQCVH DCMMELAQKE MASQRASQNS RTAPGASQSS EPNFPSSERS EEPPTPRPAQ
TAAPTIEDQV SQMAYVVRPW GLDKITNLRD LNPSDMDKLV SIKGLVIRTT PVIPDMKDAF
FKCSVCGHSI TVQLDRGKIR EPTECPRARC ASKNSMQIIH NRCAFEDKQV IKLQETPDNV
PAGQTPHSVS VCVYNELVDF CKAGDRVELT GIFKVTPVRV NPRMRTVKSV HKTYVDVVHV
QKVDRKRMGS DPSTLDLAEE EEAHANGQSM DEVRKVSPDE EERIKETAAR PDIYDLLSRS
LAPSIYEMDD VKKGILLQLF GGTNKTFEKG GSPKYRGDIN VLLCGDPSTS KSQLLSYVHR
IAPRGVYTSG KGSSAVGLTA YVTRDPESRQ LVLESGALVL SDGGVCCIDE FDKMNESTRS
VLHEVMEQQT VSVAKAGIIT TLNARTSILA SANPIGSRYN PDLSVPQNID LPPTLLSRFD
LVYLILDRVD EKNDQRLARH LLSMYLEDKP ESAQQANDVL PVEFLTSYIS YARSHIHPAL
TPEAGRELVD AYVEMRKLGQ DVRAAEKRIT ATTRQLESMI RLAEAHAKMR LSQTVTRDDV
REAVRLIKSA LKTAATDSQG RIDMSLLTEG TSAAERQRKA DMKDAVIRLL DEMTSGGQVV
RYSEVARRLG EGAGVQVEPA EFAEVMRALE MEGAVMVTGE GARKSIRRIT ATI
//