ID I2GUQ7_TETBL Unreviewed; 863 AA.
AC I2GUQ7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN Name=TBLA0A00580 {ECO:0000313|EMBL:CCH57859.1};
GN Synonyms=MCM7 {ECO:0000256|RuleBase:RU365012};
GN ORFNames=TBLA_0A00580 {ECO:0000313|EMBL:CCH57859.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH57859.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH57859.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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:RU365012}.
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:RU365012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365012}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; HE806316; CCH57859.1; -; Genomic_DNA.
DR RefSeq; XP_004177378.1; XM_004177330.1.
DR AlphaFoldDB; I2GUQ7; -.
DR STRING; 1071380.I2GUQ7; -.
DR GeneID; 14493386; -.
DR KEGG; tbl:TBLA_0A00580; -.
DR eggNOG; KOG0482; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; I2GUQ7; -.
DR OMA; AQHVTYV; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
DR GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; 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:0031298; C:replication fork protection complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProt.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17758; MCM7; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
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:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 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 PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
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|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU365012};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU365012};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365012};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365012};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365012};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 410..616
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 835..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 96306 MW; D82D84A03D5F2BBD CRC64;
MSTTLPSIQI PVDYATLQNE INDFIQHFKN DSIVPTTTET DLSGEMHDST VGTGPKYLNI
LLQVANRDLD TVTIELDDLL KYESEKFLTD PTRSDTSLVR AIQENAKHFI ELFCKAIDDY
MPLPTKDINY QDDVIDVILN QRRLRNERMI SDRTDEIRTE NLMDMDSAPA SSLNEALREV
VAEEAELFPP NLTRRYYLYF KPPSLQNPKT HSAKSYSKAG SSIPLSVRQI KGCHIGKLIT
VRGIVTRVSD VKPAVLVIAY TCDSCGYEIF QEINSKTFTP LSECTSKECE QNQTKGQLFM
STRASKFSPF QELKIQELSQ QVPVGHIPRT LTIHVNGSLV RSMTPGDIVD VAGIFLPSPY
TGFKALRAGL LTENYLEAQY VNQHKKKYSS FQMNTDTERH IQELVNSGNV YETLAKSIAP
EIYGHLDVKK ALLLLLVGGV NKTVGDGMKI RGDINICLMG DPGVAKSQLL KAICKITPRG
VYTTGKGSSG VGLTAAVMRD PVTDEMILEG GALVLADNGI CCIDEFDKMD DTDRTAIHEV
MEQQTISISK AGINTTLNAR SSILAAANPI YGRYNPRLSP LDNINLPAAL LSRFDVLFLM
LDVPSRESDE KLAEHVAFVH MYNKQPDLDF QPIETSQMRE FIAYAKTKRP VMNETVNDYV
VQAYIRLRQD SKRDINTKFS FGQATPRTLL AIIRLAQALA KLRLSETVDI EDVEEALRLV
RVSKESLYQE TNKSIEDENP TTKIFTIIRK MVQESGSANK KVLPYDTIIK TVRARGFTTA
QLNSCIQEYS YLNIWHLTNE NTILRFVDDD TVEASEGSGI RTPVVSQGTK AVNFSTSQAP
IMRPNQPASS PQPDTDADGD ISL
//
