ID A0A139HNX6_9PEZI Unreviewed; 1058 AA.
AC A0A139HNX6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=AC578_4893 {ECO:0000313|EMBL:KXT04103.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT04103.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT04103.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT04103.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KXT04103.1}.
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DR EMBL; LFZN01000024; KXT04103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HNX6; -.
DR STRING; 321146.A0A139HNX6; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000070133; 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: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 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; 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 PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 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 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.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 637..845
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 115457 MW; E514AB4EA2A8ADA6 CRC64;
MVDSSPASRR STRSNNNTPR RSQRASQAPR SSAAPPSDPP QPDDDAANSQ LQSEADAASS
RNGTPRGTQN SNSQSQAPPT SSPLFFRTSP AGSQSQSQSQ SQSLGVPARG SVNGSSPLRQ
RSDAQTPAGL SSEGGRTPRA NGANIGDSSP IHYATSSDAA APRTNGNRQH GTSSTGLFVR
SGLGSQPSAR ERRHDINSDL LDSSTRRRQL FVDENGAPVA VDPSDAATFS NLNPNTSDAA
ALGGRGTRLI WGTNISVQDS WSAFKDFLFN FQKKYRMVQD GELTEGEDLD NEHPGLEKSA
LAQCETMLEL GTKCFYLDCK DLKAYPGTQK LYHQLQSYPS EIVPLMDGAV KDTLMELAEK
KMGERRSQAS QNGRTTDRSS SMPPMPSSDI DNDMNGGATP RPAPQPSADE QDLYAEVESS
SYRVRPFGLD KNINLRDLNP KDMDQLVSVK GLVIRTTPII PDMKDAFFRC SVCHHTVKVD
LDRGKIAEPT RCPREVCSAS NSMQIVHNRS GFADKQVIKL QETPDSVPDG QTPHSVSLCA
YDELVDICKA GDRVEITGIF KCNQVRVNPR QRTVKNIFKT YVDCLHIQKV DKRRMGIDPS
TIEEQLAEQA AGSMEEVRKV SEEEEERIKE VASRPDVYEL LARSLAPSIY EMDDVKKGIL
LQLFGGTNKS FEKGGSPKYR GDINVLLCGD PSTSKSKMLE YIHKIAPRGV YTSGKGSSAV
GLTAYVTRDP ETRSLVLESG ALVLSDGGVC CIDEFDKMSD STRSVLHEVM EQQTVSIAKA
GIITTLNART SILASANPIG SKYNVNLPVP QNIDLPPTLL SRFDLVYLVL DRIDESADRK
LARHLVGMYL EDTPENASRD EVLPVEFLTS YISYARTNVH PKISQPAADA LVRHYVAMRK
LGEDIRASER RITATTRQLE SMIRLSEAHA KMRLSEIVSE EDVEEAVRLI QSALKQAATD
ARTGLIDMGL LTEGTSASER KRKEDLKNGV ISVLDELLRG GSSSVRYGDV VRTLSEQSSV
AVEGQEFAEA VRSLEAEGKV QVVGEGPRRS IRRVTGVA
//
