ID A0A0F8W6E1_9EURO Unreviewed; 1816 AA.
AC A0A0F8W6E1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=ARAM_000887 {ECO:0000313|EMBL:KKK13425.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK13425.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK13425.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK13425.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC 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:KKK13425.1}.
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DR EMBL; JZBS01003804; KKK13425.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8W6E1; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005774; C:vacuolar membrane; 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:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17755; MCM4; 1.
DR CDD; cd07751; PolyPPase_VTC4_like; 1.
DR CDD; cd14480; SPX_VTC2_like; 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; 3.20.100.30; VTC, catalytic tunnel domain; 1.
DR InterPro; IPR003807; DUF202.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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; IPR004331; SPX_dom.
DR InterPro; IPR018966; VTC_domain.
DR InterPro; IPR042267; VTC_sf.
DR PANTHER; PTHR46140; VACUOLAR TRANSPORTER CHAPERONE 1-RELATED; 1.
DR PANTHER; PTHR46140:SF1; VACUOLAR TRANSPORTER CHAPERONE 4; 1.
DR Pfam; PF02656; DUF202; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR Pfam; PF09359; VTC; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 1705..1725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1732..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1774..1793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 595..803
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT DOMAIN 1015..1176
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1551
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1816 AA; 203784 MW; 5244832D5E93CDA2 CRC64;
MSSPASSRRR GRPARDSATA SPARSTRSQQ QPLTSSPSQS TPRASRRIRG EAAVPSSSPM
FFQSSPVKGN SSSAETPDAR MEEPSSPIRA SSAMDEGEMT PRGNGAALRD SSPIRYVSSS
SPSRTPRQVG RSDIPSSSSG LFVSSRQGLD AHRVASRRSD INSGGFGSTP SRRRRVFVDA
NGIPATDGEI QSDATFSNIH PDTSEAEAMG GSSTRVIWGT NISIQDSMSA FKNFLYNFTT
KYRLWADGAT EDETRIMGQM AEEKEYIKML NTMRQLGVTS LNLDAKNLKA YPSTLKLWHQ
LHAYPQEIIP LMDQTVKDVM VELAIKEVER LRSQSQRSQN SQRDLSSAPV IPSSDALSES
GRMPQSEIPD LVTEAETKTF KVLPFGLDST INMRDLDPAD MDKLVSIKGL VIRATPIIPD
MKEAFFRCER CHHSVQVDID RGKIAEPTIC PRPVCNERNS MQIVHNRCIF ADKQVIKLQE
TPDSIPDGQT PHSVSLCVYD ELVDVCKAGD RVEVTGIFRC NPVRVNPRQR TQKSLFKTYV
DVLHVQKIDR KKLGIDVSTV EQELSEQAAG DAEQIRKITA EEEERIRRTS TRPDLYELLS
RSLAPSVYEM DDVKKGILLQ LFGGTNKSFQ KGGNPRYRGD INVLLCGDPS TSKSQLLRYV
HKIAPRGVYT SGKGSSAVGL TAYVTRDPET RQMVLESGAL VLSDGGVCCI DEFDKMNEST
RSVLHEVMEQ QTVSIAKAGI ITTLNARTSI LASANPIGSK YNPNLPVPQN IDLPPTLLSR
FDLVYLVLDR VDEQEDRRLA KHIVNMYLED RPENASEQEI LPVEFLTAYI TYAKTKVHPV
LTPAAGKALS DAYVNMRKLG DDIRSADRRI TATTRQLESM IRLSEAHARM RLSTEVTADD
VDEAVRLIRS AIKQAATDSR TGLIDMSLLT EGTSASERRN KEALKRGILG VVDELSGSGG
AARWAEVYRV LSDQASSGVD NGQFTDAVRA LESEGVVNIL GEGSRRSIRR AAGTVVFGEH
LRSSMIKEYY WYYINYETLK KALKTGYVTE PTPDNSKPDR KPWTEDDEKH FVTILESELD
KVFNFQKIKS DEIVRRIQAS EKEVNDVVSR LDSSGRPSAQ APTDEDFLLL EQVLSDIIAD
VHDLAKFTQL NYTGFQKIIK KHDKETGWHL KPVFAARLNA KPFFKDNYDA FVVKLSKLYD
LVRTKGNPVK GDSAAGGSQQ NFVRQTTKYW VHPDNITELK LIILKHLPVL VFNPSKEFEE
DDSAISSIYY DNPETWELYM GRLKKTEGAE AIRLRWYGGM GSDQIFVERK THREDWTGEK
SVKARFALKE KYVNDYLAGR LTVDRIFEKM RKEGKKSEAE IADLERLARE IQYRVISRGL
KPVTRSFYHR TAFQLPGDAR VRISLDTELT MTREDNLDGR QRTGNNWRRM DIGVDWPFSQ
LPPDDVERFP YAVLEVKLQT QAGQEPPQWI RDLASSHLVE AVPKYSKFIH GTATLFPERI
HLLPFWMPQM DVDIRKPATR PFGIQRPLTS TSMSANETPE DEEDSDDEVS DEAQASNGGA
RTSRLPPPEA EQDALFDETD GNALDIEERI AAQPLPGDED YPLYDSDEEY MDSDELEEAR
RVGGRYYYEQ LAKYYAQNFA TGLITVLKAL IPRPRPTNMP PPEQRGIAVM GNKRTVKRFV
APKGKRIHVP VRVEPKVYFA AERTFLSWLE FSILLGTIAA TLLNFGEDYI TFACSWAFTI
LAAIALVYSL MLYVWRVDKI RKRRDVKRVY YEKWGPTIVG VGLVAIMLAN FGLRIRQSGF
MAKDGDSSGD LRGGEL
//
