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Database: UniProt
Entry: M3BVI2_SPHMS
LinkDB: M3BVI2_SPHMS
Original site: M3BVI2_SPHMS 
ID   M3BVI2_SPHMS            Unreviewed;      2307 AA.
AC   M3BVI2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=AAA family ATPase {ECO:0000313|EMBL:EMF11329.1};
GN   ORFNames=SEPMUDRAFT_68831 {ECO:0000313|EMBL:EMF11329.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11329.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF11329.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF11329.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC       {ECO:0000256|ARBA:ARBA00010378}.
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DR   EMBL; KB456266; EMF11329.1; -; Genomic_DNA.
DR   RefSeq; XP_016759450.1; XM_016909841.1.
DR   STRING; 692275.M3BVI2; -.
DR   GeneID; 27906978; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   eggNOG; KOG1807; Eukaryota.
DR   HOGENOM; CLU_001133_0_0_1; -.
DR   OMA; GNMETFM; -.
DR   OrthoDB; 2971338at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 2.
DR   CDD; cd17936; EEXXEc_NFX1; 1.
DR   CDD; cd06008; NF-X1-zinc-finger; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 6.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR43392; AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43392:SF2; AAA-TYPE ATPASE FAMILY PROTEIN _ ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   Pfam; PF00004; AAA; 3.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF17866; AAA_lid_6; 2.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          484..792
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1304..1440
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1589..1737
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          1866..2003
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1185..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2099..2186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2207..2270
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1185..1230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1241..1255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2107..2146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2147..2164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2167..2186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2307 AA;  255678 MW;  EDA234432E1B8EE3 CRC64;
     MAEFSQNGTT STRGDRLSRL LHAFITGLRP LQSARDCQQF VEAICAQANH ADCIEKLGCS
     TSGLTALHRG VRFDESVSFI NGTLQNLLLY LAVPEVKRLC NGEFLKRVLK ALVSPPSLWN
     ALTLAHQNNE LSPQTTLSFA FVLLELLNWT ADSPSDVDGV ARIITEQKTF LTSQDQQLRA
     MGCRIEHILS AKGAGRKPTV SGPGGRHDND FVDFRQVAIF PTEDELASKE LPYFTPAHML
     SKIPIPERVA HHLSNQFRLL REDFLAELRE DLATSSSKKS NRRQRMRLSG LELYGIRTGA
     DKSRVPTALK ISVGKGLGAL ANASNARSFL KDNNNFIKHQ SCGYFVDQGT VIAFGTIARD
     VDLLCLKPPV IAIRTPGAGA LKKLLLSLRT SQTLEFVVID TAVFAYEPVL HCLQDKLEFP
     LWKYLLCPED AIDDLELPDL SDNLSDIARK IELERGHDIQ PILGLRKPVE LDDSQTTSLL
     AGMRQAVSLI QGPPGTGKSF IGALLAKALH DNSSENLLVV CYTNHALDQF LEELMDIGVP
     SSSMVRLGSK STARTQPLSL REQAPARSRT QENWGAINRL GEETTTHADA LLQTVKDFRK
     TQATKSQLLE YLEFSEDDHE YFEAFEVSES LDGFATVGEN GSVIDEGYLL SRWIQGKDAG
     VLQKPISPRH VEIWNMDEAD RQSKLRQWED AMLAEAADEI IARAQVFDAS QHTLQEALHQ
     RDTELIQSKR IVACTTTASA MYARQLQSAA PAIVLVEEAG EIMESHVLTA MTPNTKQLIL
     IGDHKQLRPK VNNHALTVEK GDGYDLNRSL FERLVLAGFP RATLQQQHRM CPEISDLVRQ
     LTYPSLLDAP STMQREALRG LQSRVVFIKH TKLELISQVA DRRDQGASVS KQNAYEVKMV
     KKIVKYLAQQ GYGTSDQVVL TPYLGQLSLL RQELAKENDP VLNDMDSFDL IRAGFLSPAS
     ASQTKKPLRL STIDNYQGEE KDICVVSLTR SNPDGDIGFL VSPERLNVLL SRARKALIVI
     GNPATFVASK KGGELWSSFF TLLARKNSIL DGLPVRCAQH PEREMILATP EDFDLKCPDG
     GCSAPCGVKL SCGMHDCQQK CHRMADHSKM PCSFRIREKC PQGHRLSWRC SEGRPASCYA
     CDSETAARLA QQERDTKLDQ ERQARQIAYA LQLADIQAEL DRIHQKAADK RTQEQQETEL
     SQRRTDLDNA KALAAQREAR ERDAEERSRS PAKAPPLSSR DAHQPSGSEA QTDWEQQKAV
     EGAKNDAIDE IMNMIGLEAV KEQFLEIKSK IDMLVRQDLS VAKERFGAAL LGNPGTGKTT
     IARIYANFLC SVGALPGKVF IETTGAKLAT GGVQGCKKLL DDLLNRGGGA FFIDEAYQLA
     SGSNFGGGAV LDYLLPEVEN LTGKVVFILA GYNTQMEKFF QHNPGLPSRF PRRMQFADYE
     DDELLAIMNY NIEKRYEGRM QLQEGPGGLF ARIVARRIGR GRGKEGFGNA REVENVVSKI
     ASRQAKRVRN ARKVKRRTPG QGDPDDMLFT DTDLLGAEPT HDALAGNKSW LKLQKLTGLQ
     SVKESVKALL YSLQLNFQRE LAEEPLVEYS LNKVFVGNPG TGKTTVAKLY GQILADIGML
     SSGECVLKKP ADFIGNVIGA SEANTKGILD AAVGKVLVID EAYGLYGGQG GQGSSSDPYR
     TAVIDTIVAE IQSVPGDDRC VLLLGYEEQM EEMMQNVNPG LARRFPIDSG FVFEDFDDQD
     MEAILDMKLQ DQGFRVTERA KSVALGMLQR ARNRPHFGNA GEVDIALNDA KMRQQKRTGD
     DKTAAKGILE AQDFDPDFDR GDRANTNVAM LFKDSVGCDS IVAQLQGYQN IVANMRQLDM
     DPREQIPFTF LFRGPPGTGK TTTAQKMGKV YYDMGFLSKA EVVSCSASDL VGEYIGHTGP
     KTRKLLESAL GKVLFIDEAY RLSGGHFAQE AIDELVDSLT NERFFRKQIV ILAGYDADIN
     RLMSVNPGLT SRFPETIVFE PLPPQACLDL LIQYLGKKKG LDLSPITTMP PTTTSEVLQH
     FNILASLQNF ANARDVQTLG KTIFGTIIKH VGPKRSGGMI VSCQLLLTEL RNMISERARR
     EHDATAPGAS ASSSKQDLFA PTRPDNKQQP TTQNKFHMQT RSATKQQTHA VEEETSKTED
     DLQQTPSGEE ESNTCCGENR SERTPPTTEV LLVQRDSGVT DAIWEQLQAD RMKAEQEEAE
     FQRLVEEERK LRAWLKACAD EKRQRELEEL ERVRKEAEER KRKEASVQAK LLKMGCCPVG
     YHWIKQGGGY RCAGGSHWMD EASVGAL
//
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