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Database: UniProt
Entry: A0A016VN64_9BILA
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ID   A0A016VN64_9BILA        Unreviewed;       719 AA.
AC   A0A016VN64;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN   Name=Acey_s0007.g3545 {ECO:0000313|EMBL:EYC29014.1};
GN   Synonyms=Acey-mcm-7 {ECO:0000313|EMBL:EYC29014.1}, MCM7
GN   {ECO:0000256|RuleBase:RU365012};
GN   ORFNames=Y032_0007g3545 {ECO:0000313|EMBL:EYC29014.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC29014.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYC29014.1}.
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DR   EMBL; JARK01001343; EYC29014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016VN64; -.
DR   Proteomes; UP000024635; 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   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:UP000024635}.
FT   DOMAIN          328..533
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   719 AA;  79983 MW;  56C2F7C3B5C450D5 CRC64;
     MGTVFYYRED IQRIAEREQV ALYVNLDDIN RFDESLAVLI EGNARRFHQI FNEVIDEMVQ
     EILGDRQPPI RDALDAFIFQ RVYMDDQSKI ADGYLGGTIQ EARKKYPPQL LRRFEVIFKN
     RDAMKPLAAN CVGKLVTVSG IVIRATEVKP IVEVMTYACD TCGAEVYQPV NGPSFMPAVN
     CPSKDCVESK ANGRLHMQVR GSKFGKFQEI KIQETSDQVP VGSIPRTLTV NIYGEATRQC
     APGDHVRISG VLIPLMRTGF RQGGGGLVAE TFLEAHVRSL FFPFGSKGSV FISNVLQFVE
     NIRSSVDEKD TDDDLTEEEV ELLAQDNLYD MLAYSIAPEI YGLTDVKKSL LLALVGGVDR
     NASGMKIRGC LNVLLMGDPG VAKSQLLSYV NRLAPRSQYT TGRGSSGVGL TAAVVKDPVT
     GEMTLEGGAL VLADRGICCI DEFDKMMESD RTSIHEVMEQ QTISIAKAGI MTTLNARVAI
     VAAANPAFGR YNPKRTIEQN IDLPAALLSR FDLLWLIQDK PDRDGDKRLA SHITYVHMNA
     KQPEVDGMKP IDMRLIRRLI EVAQRKQPVV GDTLRERLVE MYVDMRRVAR ESDDSTFTSP
     RLLLSVIRMS TALARLRLSN VVLPDDIEEA IRLMQASKDS LRPEMLQQEI RQSPIDRAFA
     VLRELNSSAG DAVIALQTAV EACARKGISE EALRDAITVH QSNGVIMVDS QQRIRFVMN
//
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