ID A0A1A8W2X3_9APIC Unreviewed; 4144 AA.
AC A0A1A8W2X3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=POVCU2_0040980 {ECO:0000313|EMBL:SBS87122.1};
OS Plasmodium ovale curtisi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS87122.1, ECO:0000313|Proteomes:UP000078560};
RN [1] {ECO:0000313|Proteomes:UP000078560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; FLQU01000545; SBS87122.1; -; Genomic_DNA.
DR Proteomes; UP000078560; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17756; MCM5; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR031327; MCM.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00350; MCM; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF141571; Pentapeptide repeat-like; 2.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000078560};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 3214..3266
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 3729..3934
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 563..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2347..2376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4144 AA; 471114 MW; EBEAEE7BEF3BC735 CRC64;
MTVRRKTEPS CGKYVYRYTH LERIERRENG ENIKINTERV LHTDMKISRE KSTDTNIAKK
KKTDTNIARK KRTDTNIARK RSTETNIARE RNADMNGAFW RDHNVNIALG YGTDKGEIET
ERVDINNISQ GEKDQNKRYA IFFSYLSKAE RRKFLPDGVD KSILKRGIVF SSHLSYFIKI
FSELLIKYNL DLEIYNNKLY ITLKYIDNID IVIPYLRKEF FFKKKKEENV LLLLAKKYEV
LNLLSKSIYL SQKIKEFLKN KKQINDLFLE NNFKKNYELY RKFVAMNFFP NNNQVNTEKS
TFFTMSENKT YAKVTPAQGK REFALGENSA AEVSVEAVEL GEVRADTVAE GVVMAELDEI
GTISDVGRTR RTQLTQEEVI SGEGSLMGDS LQTREHIRKG VSTMENMEST KKRKDLGYSL
LRENSREEDK MRHGMVTVGK RKIIKNIKNE YVYYENVRLE DKKKQSMEKK KNKKNSGNSI
CSYENADVET CDRINDHAHM VRKKTVLCEE SDEDVLTERE EEHSEKINRA RQMEKKKLKM
MEERKKKEFM KRDKHINTKE NDEVKMKEKE KKRKEMEHKK KMKDIKKKKK NDEVIIVGTE
ENNESTCKKK KWRVQYLNGV KKEKGRIKYI KDEYRKINKK DNDISKNNHK CSRRKTKRGN
KDTINESITH SFKNNTLKHQ ENVTVLGSTK KGKKMKKKLS GKYNKHVEND CATSGGSSTQ
SEATHMEDGE GELHHAGENG SPINGLGVNG VTRNDMADKD VLGKDTIEMN TIEIDMAKRL
MSERGMDVVG KYLEMVGKYL ELVGRQGRIG RANMDLLESL GNGRIAENLL FLRNAYTRGF
YNNEMYFGRA HQGAPDLGRV PIGGVDFGRA DLGRAPIGGV DFGRAYLGRA PIGGVDFGRT
DLGRAPIGGV DFGRAYLGRA PIGGVDFGRA YLGRAPIGGV DFGRTDIVRA PIGGVDIERT
NLGRAPQGVD FGRTDLGRAP IGGIDFVRED LGRIPLGGVD FGRTNLGRGP LGVDFGRADL
GRGPLGVDFG RADLGRAPLG GVDFGREYMA RADMGRAPLG KAVQEKPVLG RVDVARADLG
KMAPDGSYQQ EQAHVRGIRD ENDLGEKSLS VPPLSNYNIF VERFTEGNYP RYDLNMELKT
YNVISRQKRT CDIVRTENIS SHCTHTTIDF SKKRKKDIRS DVGEDMGRVD VWVADVKETN
TEGASMSIGN VVGGNIAIDN TGAEATGMVN VEDTGVRRGK FDEEHVEKVN RRVGIEGKAH
GEKEELQEED EEKENIVVVT AEMENGKGED IVKTTVGTYC VRNSVGKDVE DASAVTGTVE
EKKKKKGTVT NIPNNVVDKI VAKGLVLSKH QMKSNEREGK KKKEEKKISL FGQVKPVDLI
NRGIDAYQVL HEDENLYVDV LIIGAGISGL AASYYLNKCN ASILVIEGRN RIGGRAFSTI
LPHRIVNNKI LPETVVDLGA NYLHCCDNID LSTGKINAQK KGSVIGKEKK DLYEDEEEIM
FGEREFDARG KGAKKKKTWK RKTKKKNNNG GDLRNDGSGS NGSWTSGNGR SGNGRGGNGR
SGNGGIVSGN HFDTREMGER LANNLRLFKE EYAKLFREFP TLHLSEETTS RRIFERDSCI
MKSHDKIVLA NIRGDEISRS DCDYLSIKNK RTREKKKIKE NMLFRMRNNI DNIYHLYEDY
YKEKKKDVFH FLKSIDENMY FYGTLSDSEF NPSILSRFTV RSSPPKNEKK KFKILSVNKD
TRRRREFDKS LTQLAQKLKP KVTPVCGKDN WESTFYAYWY NNESGKKIKS FKIYRINLLC
DKIRVRAARK IRSFLFINES IYDKEIADGA DDGDSDRDNI QEKCVSNGRE EKKKKKRNPY
EYVNDHATRS KKNRCGGILR NGGKGESGKS GEKVLNTKNS LRIASRLTKS NDVRGEIAKG
SALRLGVKKN IISYRNDVGK MERSRKDDNT SQVGRKKKNG KQTGKGNGGN EKGGCGNGGN
VKGGCGNGGN VKGGCGNGGN VKGGCGKSGK WKGGCGKGGN IKTKGVITHL DTIQYDEDAI
IYDNYYNYGK EYYDIVKETS ERKKHSRDTT NTVLYKENNE RRSMWDLLME CTEEIFDEMN
LNQCNFSLEE WKILMVTLQS RYGYGSDLRE TSIAMSRLPF SSYLDIDMCP NYGSDSYIMK
NIKYYDKIKK NEQTPHITAF KDNGSADKIV LDGWKWIIDY LSEDIQNKIF INTVAEVVLI
REEGEKVKDN KGTSKHSVCT SFSLESTSYE DNSWQNDQVE KMRSAPVSHI PITRSSGRAT
HAYQLRRARE DDYPVLVKCK TYDTSMKNIN KHFHGTSDLN NCDSKNVNIY AKYVIVALPL
GCLRNGDEDK NRSESRSDSE SDVLSNSEEK EKTRSHFEGT TRLKFIPKLH PLKVKALNNY
KMGNHNKIVL RFFPYNFTWP FDSLQLNCID QKFQFLNLHA YGKVGCILVH CFPPWSCTYG
YIKKENYIVN ECLHTLNKMF EKSGKRLPIL VDYIITKWQD DNFSCGSYAY PYVNCNDNDL
IYLRSPHPVD NPKVVFCGEY LSKSYFQCVD GAFDTGIRAA EDIAHIGLRL KGFDKKNYNT
DVFFFPDNNC PFTNLPLPNI KSSLLGFYIT DGSDEALTDY ESLSDEEDAP VSNMPLSVVK
EEHSFLSYTL NKIHHFFDHL KGEGSFVKKG KHSGNQNSCT QGTSLGSRSF LDLQERNMHY
DVTKSRDGSS NNSRDLVERK DSTFNLDNFY NRKGIAKETA IATATVTEWE ENASTNEEGG
HTISCDDNVS GGIPPARSFQ RGAHCNEVEN MAKYENEWDV EGEYSGGATD MAHSAKSTSR
MGTSSIGRSA LGNEKKCDHL LEDEIAKRRS LLLRKHRENI DLYVDKYMIK FNDVIFYNYN
QIEWNVQGRE SFISPILEKS KMMLSHSLST VLNKYYRFQF FILKELLSKV EDVKHGLLQD
FDFDFDFANV EEMGIFPLLE GNVKDSLCVQ NGEKKKKKND KSEIMYEQTR ISSTTKKNDH
FENGKNAIFT VCTGEIKNCN TIGNEIKNGK VAAYGGTTDA EEENYLFDKN HLLIDGTIDA
SKMNCAGKSG ANGIISYEQD NMDNGGIGKN YDQNRKTEET SETESACRQL DFYYEKKKKI
YAQNKQICQL NFYLRYVLNH LFISKKNVEE NIMDMRYYNR IKLNSTCFLF FFCNLVQHIM
KEIKYDIRNS ATDYKVIVQL LCDYIYHLAF YKHDVLCYKC MNGGELVLCD FSNCPNGWHS
YCLRSKDAHS ESKSDDSWFC PNCISPSLSN PAQRGCYNQN EIIQNYWKRR IYIYKLHTHI
LLFGNDEEAS PYRTLMRSLY VRNHLYLESY PGAEYLTNPL KENIRAWEER NFIKKEVVKL
DNLYMLGIQE GRAFFNAARN PNSRPENNIR LEDNLPSLNE VYNYFQDFLS RYSSNTLKEG
NLKRTLFENV KNNNFTLDLK LDDIYKQQTV FENNEISATP ISERKIKKPE NYSAILARAL
SERPLTYLPT VERVCYEVCE TANILSDEDE HLNYIQINLL NTFIRPTPIR GLLAATQERF
VVVPGIIVQA SKPQHKMRKI TLQCRYCDHK MSIDVPLWKD KPQMPPYCRY SSTMKSSMGV
ANPMDNQLGC NGVLEPYVIL PNECTFVDIQ SLKMQELPEA VPTGDMPRHL QLNATRYLCE
KMIPGDRVYV HGVLTSYNPN PKPSRADGTN FSYLHVLGFQ KYDDMTGNDL NFDVEERNEL
TLLAAEHDIH EKIFKSVAPE LYGMDEVKKA CACLLFGGTR KRIGEETKIR GDINMLMLGD
PSVAKSQILK FVNRCAPVSV YTSGKGSSAA GLTAAVMRDS QGVFSLEGGA MVLADGGVVC
IDEFDKMRDD DVVAIHEAME QQTISISKAG ITTMLNTRCS VIAAANPSFG SYDDSQDTTD
QHDFKTTILS RFDIIFLLRN KQDIEKDTLL CNHIVALHAS KHKSQEGEIS LSKLTRYIQY
AKKEIAPLLS KEARDSLRNF YVQTRAEYRG DRRSVTKKIP ITLRQLESLI RLAESFAKME
LSQFATEKHV QMSIDLFSAS TAETAKQCLI FETMSPLEQK AVKQAEDAIL GRLGKGQRAS
RVNLFRELQL RGFDRAALSN VSYFVVSYVS TASLCCVDNS VHFMMSTGHI DQKGGAPRKG
GSIC
//
