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
//