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Database: UniProt
Entry: V2XQ71_MONRO
LinkDB: V2XQ71_MONRO
Original site: V2XQ71_MONRO 
ID   V2XQ71_MONRO            Unreviewed;      1984 AA.
AC   V2XQ71;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Helicase sen1 {ECO:0000313|EMBL:ESK95021.1};
GN   ORFNames=Moror_14026 {ECO:0000313|EMBL:ESK95021.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95021.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK95021.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95021.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK95021.1}.
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DR   EMBL; AWSO01000117; ESK95021.1; -; Genomic_DNA.
DR   RefSeq; XP_007845742.1; XM_007847551.1.
DR   STRING; 1381753.V2XQ71; -.
DR   KEGG; mrr:Moror_14026; -.
DR   HOGENOM; CLU_000459_1_1_1; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18042; DEXXQc_SETX; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR024481; Helicase_Sen1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887:SF545; -; 1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF12726; SEN1_N; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ESK95021.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:ESK95021.1};
KW   Hydrolase {ECO:0000313|EMBL:ESK95021.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ESK95021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          84..821
FT                   /note="Helicase Sen1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12726"
FT   DOMAIN          1296..1578
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          1585..1781
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
FT   REGION          924..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1817..1961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1465..1492
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        987..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1817..1831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1839..1855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1856..1887
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1888..1906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1928..1953
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1984 AA;  222734 MW;  D2C68A90157253DC CRC64;
     MGDAASAADT AHVHEQLLKL RDKPAGNDQC SDQILQLVYV YLLNGRSSGA ENHWFCSQAN
     ATTVEAATFL LRLFAYSSPQ VEKWKEVLQG CLMNCSGCVL ELEKVKITSR TTYFGAFTSN
     VLNNFWDQFN QWELQTVLER LSSLGVTLDS TSTSSIPSPI AYRMVTNLPI FRDARIQSMI
     HKHLSLQQYS DWPSDPIPPG VLALLMHDDQ AVRRWASQQA TRAGVIPISN EILTPLFKDV
     VNSVVSSLMS NYDGSNSAAL VMTTVKDPVM LWKSFHEFVR FVHPDFLVSN GRNDIRHFTT
     SHLHDHGPEL EHILRCFILI LKRLNDRLWS GETPEYPQVV FDALKDNPSF TSLIQIEASS
     LEKTPWSLSW LSEYLYAIRS QSVYPEVLAK ITEYLCGELQ HERFGDARPT IMLYATKLLK
     SQVKNQSSTV ADLMDIHADM FTAVLFAASH SEARWSNARG ATRDLVHQAL VRDTVNISDA
     ITRLCRWQAY LELKKKQPEI EEKEKAPFRI REQIWKKMYS AFQSGDLDGL RSILSIVAQA
     AHLDYLSENS LSQILKVKLQ GVKELIQAVN QALTVIRTGF LDAITKFTDY NVPTATLDVL
     QRDGTVKDVV RLMLSPVDVI RNGAQMLIGH AFDVDIRADC YRALIGKFPG HALDGMFEFL
     TTFVSYASTV PEACSLAKSL VRCFTDILEA LCASPDGHLH KPQFLQSLHA GGLHTKLVAL
     WKSMCKAMNV IFKRTPQWSP LFTPNVMIEW MRDALIFERD LLAHRTILET AVNTPSGGRH
     VSDPRNPSAT GKRMIQDLHE TLPELTRWLR LTDSELLHQS FTLLQSLLDC FREARIPPPE
     AGLKKIATTV KVAREGDPNK GSRLDDARLS KLEDAIASFE DEVEIQEIQV KAEKGKKKEK
     THGVKQEDND VEFVSMTKAS QKPIITDKLM SKSKLKDEAK TQPSASNKVA PPSKVPVPAT
     TKALKSSAYQ FKSSDQEKLD AAHSLPKFRK TSTTTVQPSS ARASSAPKSA SSRAPSPSAV
     SDSSSDESEE ESQRTTLAQL AKAQKSPKIK KQPERRGIKQ IDIPTMTKNP MEERIRQREE
     LRRKALRLRP DITGLHRELL SWNYDHPGAE PPGRKLSLLT VPDRFTDFNH YRRVFEPLLL
     LECWSQLANS KQERLDYFQC KIVSRQYTGD WSDLDISITE GVRKEWYLTE NDVVLLRHPD
     GKTSFLGKTL NYRGTPTEIQ ASIRCLVPAS IVDPLQLNST WEIAKVFSLS TLHREFAALV
     SAEYYDCAQQ VLNPQLSGIP KLDESTIKQT MERHSVNKPQ ATAIAASLRT GGFSLIQGPP
     GTGKTSTICG LVAAFLSDPP RRPVTINAGK PVEKPVSPKI LICAPSNAAI DEIVGRLKDG
     IRGLTRKEGV LKVVRIGAEQ AMSLNVKEVS LDRLVDIKLN SSGQQANTDI GNEIATVRRD
     LESVKQLRLQ KIQEKNEVHD NSARLRALDD EIARLNSRRM TLTQQFDRLK DQQKAESRTI
     DASRRKARQE VLQEADVICS TLSGAGHEIL EAFDFDMIII DEAAQAIELS SLIPLKFRCD
     RCVMVGDPQQ LPPTVLSRQA CKLQYDQSLF VRLQKQKPEA VHLLSIQYRM HPDISRLPSK
     IFYDGRLQDG PAMDTKTAQP WHSSSKFGTY KFFNVAKGQE EKSGQSTKNR SECQIAVALF
     NRLRKEFYNI DFNLKIGIVS MYRAQIVEIR NTFQQRFGRD IVGQVDFNTV DGFQGQEKDI
     IILSCVRAGP GLTEIGFLSD VRRMNVAITR ARSSLFILGH APTLERSDEV WRNVIQDARS
     RGCLVEVDEA YFTAPSAILS GSSSPPKRQK PKKTQPVTAI PDDLTTPQQL KQSMEKKPSR
     TFDSKPEPSN PAGRDDKQGK RKREDSISTS TPAVPSFSTH LDKSSTDLPP PQRLKPESGD
     IQLPSSNRLL PPRPPPITEN QVKMPPQKRP KPQPNIFLPK QKNKNKVVNA CQFTFFAIPD
     VWNS
//
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