ID A0A016VQR3_9BILA Unreviewed; 899 AA.
AC A0A016VQR3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=Acey_s0006.g2770 {ECO:0000313|EMBL:EYC29068.1};
GN Synonyms=Acey-mcm-2 {ECO:0000313|EMBL:EYC29068.1};
GN ORFNames=Y032_0006g2770 {ECO:0000313|EMBL:EYC29068.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC29068.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EYC29068.1}.
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DR EMBL; JARK01001342; EYC29068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VQR3; -.
DR STRING; 53326.A0A016VQR3; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd17753; MCM2; 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; IPR008045; MCM2.
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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 467..673
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 32..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101771 MW; 5C69E9DAF04F5B42 CRC64;
MLLDQCFVAV QFQAFIHKFH NVICFRMSSR RDEDSAEQNE QPLGQQYDEE EDAIDELFNN
ENEDVEDEEG ENLFGDDMER DYRPQPELDV YSESGLDDAS DLDELSASAR QAAEREMAQR
DQLLDEDALF YEEGDEEQRR RRRRRGVREE GAEEVEMEEE VPIDILENLR GRSTKDHVSD
EAVAREIERR FKNFLRAFKD PETRKAKYLQ AMSQMASENK ESLEVDFRDL ADENGEPNIC
YFLPEAPVQV LKILDKAATD VVLTIYPYYG RVCSEIKVRI SHLPVEEDIR MLRQIHLNML
IKTSGVVTVA TGILPQLSVV KYDCVACGYI LGPFVQREDE EVKPSICPSC QGRGPFELNV
ENTVYHNYQR ITIQESPNKV APGRLPRSKD CILLGDLCDS CKPGDEIEVT GVYSNNFDGA
LNYKQGFPVF NTLIHANHIT NKDKIACSQL TDEDVKAIRE LSKDPHIAER IFASIAPSIY
GHDYVKQAIA LALFRGEAKN PGEKHRLRGD INVLLCGDPG TAKSQFLRFA AHTAPRAVLT
TGQGASAVGL TAYVQRHPVT REWTLEAGAM VLADKGVCLI DEFDKMSDQD RTSIHEAMEQ
QSISISKAGI VTSLHARCTV IAAANPIGGR YNPTRTFAEN VDLTEPILSR FDVLCVIRDT
VDPVEDERLA KFVVGNHIKL HPGRQDENEE ENEEENDVDA RTGVTLVPQD LLRKYILFAR
ENCHPTLHEK HSDKLATVFA QMRKQSMATG SVAITVRHVE SMIRLAEAHA KLHLRTFVND
DDVQAATRIM LESFINTQKA SIMRQMRKTF SKYLTANRSS SELLLFILKQ LIREQMHYET
ARGKGGADIT SISIAESDFI DKAQQLKIEN VKPFYSSDLF NANHFTYDAS LKQITQAIF
//
