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Database: UniProt
Entry: A0A319EH50_9EURO
LinkDB: A0A319EH50_9EURO
Original site: A0A319EH50_9EURO 
ID   A0A319EH50_9EURO        Unreviewed;      1847 AA.
AC   A0A319EH50;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=BO71DRAFT_415048 {ECO:0000313|EMBL:PYI00149.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYI00149.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYI00149.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYI00149.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; KZ825797; PYI00149.1; -; Genomic_DNA.
DR   STRING; 1448320.A0A319EH50; -.
DR   Proteomes; UP000247810; 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:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:UniProt.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008046; Mcm3.
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; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR033443; PPR_long.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
DR   PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR   Pfam; PF00493; MCM; 2.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   Pfam; PF17177; PPR_long; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01659; MCMPROTEIN3.
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; PS50051; MCM_2; 1.
DR   PROSITE; PS51375; PPR; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT   REPEAT          197..231
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          1293..1476
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          822..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          987..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1642..1777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..851
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..942
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1667..1687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1722..1776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1847 AA;  207459 MW;  FE43811EAB88A454 CRC64;
     MSLVPQSLLA FAEHLRRVKV TRKDDIVNFI LHNIFLNPEF AETTSTETLL VLLQKFHNLQ
     ILNFRHYFNL IKTLQASQNR PTFMGNHHPP SSLVEAFLTR LTQFDITTGI PYFLDEFANF
     FKKPSVNAYK HALIGYSRAG DVAKVNEVFQ RFLSDHGLPQ SRRILAPVLY VHSRLGDAQE
     TLRQFKRISH EFGLVPDTVC WNILVTAYAK SGDLDGSFVV FKQMLEQGVE ASSYSFGTLM
     GLCANRGDID RVHDFLDLAK QHKVQVTAPM IDTLVEAHCN KQEWDVAERV ADNCLGLDVK
     GSRVRMWNIL LWNYAFKMDL EAISRVRSRM EAAGLQPDDM THAALMLSLV LLGQTDSARR
     ILRTLHRGRR LFVTEFHYAI ILYGYLKDRN RDMVHVVYRE IQERYNQPGL GSKLLHLKSQ
     IQRDLQLMSA EGRAGDNANV RLVNSEKFLA ETIAEHHTSH LATKYPLPGS GGMPARKAFP
     AVYYEYIISA YGTKGASKAA QRVFDEFITT QPPQNTENEH DIAPLLLVTA LMRAHLKAEQ
     FEKVEECWNI ALPRALKIAN SSSPEIDNWL SERIPGHHSQ PPPLPSQAAL LVNAESHTET
     KPSILTAYRF MLSRPLSLYL RSLAYRNELS KIPQVIAKFV EAGFSMTTFN WSTAVQLLAS
     SDAPADQIEA FTIFEDKFMP NFTDWKYIRR GFGARPADAP PSLDAMEDPN RTGPPGVLGK
     AARRYWSNMQ PDFMQPTYVS LIYLAAALQG VRERSITEGG AEMDALYHVA PKTIAAIASM
     PYLREKFQGV LLRSREEQPT HSDYYGGKHA VWTGGVLGVG GEMRSGSTDE PVSESAGEDE
     SMTEEGDDGI WEQPDTIPFS NIQMHDEWDY DRERTIDYPD EHDLEMESHL EAMSRKYGTT
     EEFMDVQQKA TYDDNFDESE FESDNELDES EYEGEDEVDE SKPAEYDGFG EAEYRNRDDP
     NELQDQLVIP NRRNRRKVMH GFVPQLTQQG TRRHPPSTST RDHTRFRAPG FISGPRDTSH
     LSFPSPFPFR SPVRSSWECP APWREPLTTT HRIVCVPPSS FWIQPMLERV SIDEVRAHNR
     EMADGLLTSP YDYSDAFEKA LKEIIKTLPN RPSKETADDV DYHCGFVGAF GEFSCNPRTL
     GASHLNRMIS LEGIVTKCSL VRPKIIQSVH WSERGRKFLT RKYIDATMTA SGATSMSIYP
     QEDEEKNPEM PERAPAGQLP RSVDVIIDDD LVDRAKPGDR IQNASSSSAT FRTLVLANNI
     IQLSSKSGGG IAQATITDTD IRNINKISKK KGLFELLSHS LAPSIYGHDY IKKAILLMLL
     SGMEKNLDNG THLRGDINIL MVGDPSTAKS QLLRFVLNTA PLAIATTGRG SSGETGERRL
     EAGAMFDKMS DVDRVAIHEV MEQQTVTIAK AGIHTSLNAR CSVLAAANPI YGQYDPHKDP
     HKNIALPDSL LSRFDLLFVV TDDIEDSKDR MVSEHVLRMH RYRQPGTEEG APVREQLHQT
     LGVGLEDTQD SNQPTDVYEK FNVMLHAGMA HMNRGKNKNI EILSIPFIKK YVQYAKSRVK
     PVLTKGAADH IVATYSALRN DELSGNQRRT SPITARTLET LIRLSTAHAK SRLSNRVEER
     DAKVAESILR FAMFKEVLED ERRKRRKVTT FDEDSESSES DSDDDDNTPA QTSSATPRST
     TRAGLRNRAV NARSALNKDT EMDADGDNVS EDGDGLYSAS PRGQRLRSSQ TSRTQTQTQS
     QSRMSVASSQ PESQLVQSQT DNSQSQPTSA ISSEPIQPAR LTVFRQALGP LLGTRLFTHG
     DTADVEELIG AVNTALRSAP SLGESHVFQR TEAIEALRAM NERNELM
//
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