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Database: UniProt
Entry: A0A2D0PUS9_ICTPU
LinkDB: A0A2D0PUS9_ICTPU
Original site: A0A2D0PUS9_ICTPU 
ID   A0A2D0PUS9_ICTPU        Unreviewed;       615 AA.
AC   A0A2D0PUS9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN   Name=mcm7 {ECO:0000313|RefSeq:XP_017309186.1,
GN   ECO:0000313|RefSeq:XP_047007643.1};
GN   Synonyms=MCM7 {ECO:0000256|RuleBase:RU365012};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017309186.1};
RN   [1] {ECO:0000313|RefSeq:XP_017309186.1, ECO:0000313|RefSeq:XP_047007643.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017309186.1,
RC   ECO:0000313|RefSeq:XP_047007643.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365012}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|RuleBase:RU004070}.
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DR   RefSeq; XP_017309186.1; XM_017453697.3.
DR   RefSeq; XP_047007643.1; XM_047151687.2.
DR   GeneID; 108256626; -.
DR   CTD; 4176; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000221080; Chromosome 2.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   CDD; cd17758; MCM7; 1.
DR   Gene3D; 2.20.28.10; -; 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; 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; 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|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|RuleBase:RU365012};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU365012}.
FT   DOMAIN          225..430
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   615 AA;  68746 MW;  D4844E8AC4FBF1AF CRC64;
     MMEGRGRDPA DTRDPRNQYP AELMRRFELY FRPPSSTKLK VIRDVKADSI GKLVTVRGIV
     TRASEVKPMM AVATYTCDQC GAETYQPIAS QSFMPLIMCP SQECVTNRSG GRLYLQTRGS
     KFVKFQELRI QEHSEQVPVG NIPRSMTVSV RGENTRAAQP GDHVTITGVF LPLLRSGFRQ
     AVQGLLSETY LEAHSITLMN KTEDDELGIE DLTDDELRQI TEEDFYEKLA GSIAPEIYGH
     EDVKKALLLL LVGGVEQNPR GMKIRGNINI CLMGDPGVAK SQLLSYIDRL APRSQYTTGR
     GSSGVGLTAA VMRDPVTGEM ALEGGALVLA DLGVCCIDEF DKMADADRTA IHEVMEQQTI
     SIAKAGIMTS LNARCSILAA ANPAFGRYNP RKSIEQNIQL PAALLSRFDL LWLIQDKPDT
     QKDLQLAQHI THVHQHCKQP PTHYTPIDMK LMRRYISKCK KKQPVIPEGL TDYITAAYVE
     MRKEARVSKD TTFTSARTLL SILRLSTALA RLRMVDVVEK EDVNEAMRLM EMSKDSLQPD
     KSTTTRSQRP ADVIFSLVRE LVSEGGKVRA VRMADAEHRC VSRGFTPAQF NAALQEYEEL
     NVWQINNTRT RITFV
//
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