ID   Q7SHS5_NEUCR            Unreviewed;      1013 AA.
AC   Q7SHS5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   02-SEP-2026, entry version 153.
DE   RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|ARBA:ARBA00073498};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=DNA replication licensing factor mcm4 {ECO:0000256|ARBA:ARBA00074938};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00047995};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|PROSITE-ProRule:PRU01410, ECO:0000256|RuleBase:RU004070}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01410}.
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DR   EMBL; CM002236; EAA36434.1; -; Genomic_DNA.
DR   RefSeq; XP_965670.1; XM_960577.2.
DR   AlphaFoldDB; Q7SHS5; -.
DR   SMR; Q7SHS5; -.
DR   FunCoup; Q7SHS5; 941.
DR   STRING; 367110.Q7SHS5; -.
DR   PaxDb; 367110-Q7SHS5; -.
DR   GeneID; 3881804; -.
DR   KEGG; ncr:NCU02539; -.
DR   VEuPathDB; FungiDB:NCU02539; -.
DR   HOGENOM; CLU_000995_7_0_1; -.
DR   InParanoid; Q7SHS5; -.
DR   OrthoDB; 10251574at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0071162; C:CMG complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR   GO; GO:0097373; C:MCM core complex; IEA:EnsemblFungi.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IEA:EnsemblFungi.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR   GO; GO:0030875; C:rDNA protrusion; IEA:EnsemblFungi.
DR   GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:EnsemblFungi.
DR   GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006271; P:DNA strand elongation 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:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
DR   CDD; cd17755; MCM4; 1.
DR   FunFam; 2.20.28.10:FF:000003; DNA helicase; 1.
DR   FunFam; 3.30.1640.10:FF:000011; DNA helicase; 1.
DR   FunFam; 3.40.50.300:FF:000217; DNA helicase; 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; PF17855; MCM_lid; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   Pfam; PF21128; WHD_MCM4; 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|PROSITE-
KW   ProRule:PRU01410};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PROSITE-
KW   ProRule:PRU01410}; Cell division {ECO:0000313|EMBL:EAA36434.1};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|PROSITE-
KW   ProRule:PRU01410};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01410}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU01410};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU01410}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805}.
FT   DOMAIN          593..801
FT                   /note="MCM C-terminal AAA(+) ATPase"
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   MOTIF           662..669
FT                   /note="Walker A"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01410"
FT   MOTIF           726..729
FT                   /note="Walker B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01410"
FT   COMPBIAS        1..10
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..120
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..587
FT                   /note="Basic and acidic 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
//