ID A0A2J7QTN3_9NEOP Unreviewed; 719 AA.
AC A0A2J7QTN3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
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_4 {ECO:0000313|EMBL:PNF31951.1};
GN Synonyms=MCM7 {ECO:0000256|RuleBase:RU365012};
GN ORFNames=B7P43_G07945 {ECO:0000313|EMBL:PNF31951.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF31951.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF31951.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF31951.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF31951.1}.
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DR EMBL; NEVH01011194; PNF31949.1; -; Genomic_DNA.
DR EMBL; NEVH01011194; PNF31951.1; -; Genomic_DNA.
DR EMBL; NEVH01011194; PNF31952.1; -; Genomic_DNA.
DR EMBL; NEVH01011194; PNF31953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7QTN3; -.
DR STRING; 105785.A0A2J7QTN3; -.
DR InParanoid; A0A2J7QTN3; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
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; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 InterPro; IPR036388; WH-like_DNA-bd_sf.
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:UP000235965}.
FT DOMAIN 332..537
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 719 AA; 81341 MW; 302D537643C07FE4 CRC64;
MAGKDYINDK EKLKQFLIEF AAIDAEGHKD FKYVHQLVKI AHREKVALIF ELDDVYEFDS
GLAEAIVNNT RRYVSIASEV VYEMLPDYKQ REVTAKDSLD VYIEHRLLME QRLHQPGEQR
DPRNKYPPEL MRRFEIYFKD LSLNKPIPVR DVKAEHIGKL VTVRGIVTRC TEVKPMMVVA
TYTCDQCGAE TYQPVNSLTF MPLAMCPSED CRVNKAGGRL YLQTRGSKFI KFQELRIQEH
SDAVPVGNIP RSLTVLCRGE TTRQALPGDH VSVSGIFLPL LRTGFRQIAQ GLLSETFMDA
HRVVHLNKTE VDEAPAADLT PEEVQQLTHE DFYGLLASSL APEIYGHEDV KKALLLLLVG
GVDRRPQGMK IRGNINICLM GDPGVAKSQL LSYIDRLAAR SQYTTGRGSS GVGLTAAVMK
DPLTGEMMLE GGALVLADQG ICCIDEFDKM ADSDRTAIHE VMEQQTISIA KAGIMTSLNA
RVSILAAANP AFGRYNPRRT VEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV
HQHCKQPPAT VQALDMRVMR RYIALCKKQE PVIPEELTDY IVDSYVEMRK EARNGKDMTF
TSARNLLAIL RLSTALARLR LSEQVEKEDV KEAIRLTEMS KDSLNHAEDR HGRAQNVMDR
IYSVIRELAG ESKTVKMADV LERCASKGYT PDQVEECLEE YEELNVWLIN QARTKITFV
//
