ID A0A1B8GBN3_9PEZI Unreviewed; 947 AA.
AC A0A1B8GBN3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN Name=MCM6 {ECO:0000313|EMBL:OBT93241.1};
GN ORFNames=VE01_08868 {ECO:0000313|EMBL:OBT93241.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT93241.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT93241.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT93241.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; 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|RuleBase:RU368064};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368064}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368064}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KV460256; OBT93241.1; -; Genomic_DNA.
DR RefSeq; XP_018126974.1; XM_018278287.1.
DR AlphaFoldDB; A0A1B8GBN3; -.
DR STRING; 342668.A0A1B8GBN3; -.
DR GeneID; 28842254; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0033260; P:nuclear DNA replication; IEA:UniProt.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 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; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
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:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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:0000256|RuleBase:RU368064};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368064};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368064};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956}.
FT DOMAIN 471..677
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 104479 MW; 6B096CC39C68D9AD CRC64;
MSDFDLNSGR IAPPMSGSIR SSSVRPRGPP SESLAPQSDD EGFADDQVPT GIARPRNIHD
RPIPRVEDKV GLSVQSNFET FLEKFEEEPS PSAAPVSSNA TAGNYYYIAQ IHGLRIYQLS
TLYIDYNHMK QFSGNLADAI VNDYYRFLPF LTKGLHNLIA KYESRYFKEH RQPTSSSNQA
SSAAGNVASE SLSDFQGDKT SNQQTDKLFA IAFYNLSHVD RVRSLRTAHI GQLLSISGTI
TRTSEVRPEL SLATFTCEAC RMVVPNIEQT FRYTEPTQCP NQNCGNRQGW RLDIRQSTFV
DWQKVRVQEN SSEIPTGSMP RTLDVILRGE IVDRAKAGEK CIFTGALIVV PDVSQLGLPG
VRPTAVRDDK NAPRSGDAGG TGVTGLKALG VRDLTYRLAF LACMVTPDTS TPGSVTSQQL
YGQASNILAS LNQTAPIDPN ESGDLAQEAV LASMTDAEIA ELREMVHSGH IYSRLVDSIA
PMVYGHTIVK KGLLLQLLSG VSKSTPEGMQ LRGDINICIV GDPSTSKSQF LKYICSFLPR
AVYTSGKASS AAGLTAAVVK DEETGEFTIE AGALMLADNG ICAIDEFDKM DISDQVAIHE
AMEQQTISIA KAGIQATLNA RTSILAAANP VGGRYNRKTT LRANINMSAP IMSRFDLFFV
ILDECNEATD RHLAEHIVKI HQFRDEAVEP EFTTEQLQRY IRFARTFKPE FNDEARELLV
QKYKELRSDD AQGGIGRNSY RITVRQLESL IRLSEAIAKA NCVGEVTAAF VTEAFDLLRQ
SIISVEKDDV EVDDEEEDLA GTLGGPTDVE GDAAMEDADG REAGTDGQRP KTKITHDKYL
KILKMIARRI EEEELATGNG VEGEVLIRWY LDEIEDEMDN EEDFHYEMNI ARKVLKKLIR
ENTLMAVRGD GLLPEDGEDD SAPADQVAYV MHPNYASDEI ELKQSKR
//