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Database: UniProt
Entry: Q7SHS5_NEUCR
LinkDB: Q7SHS5_NEUCR
Original site: Q7SHS5_NEUCR 
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}.
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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
//
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