ID A0A1X7RSR0_ZYMTR Unreviewed; 2177 AA.
AC A0A1X7RSR0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=ZT3D7_G5598 {ECO:0000313|EMBL:SMQ50445.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ50445.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ50445.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC {ECO:0000256|ARBA:ARBA00010378}.
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DR EMBL; LT853696; SMQ50445.1; -; Genomic_DNA.
DR STRING; 1276538.A0A1X7RSR0; -.
DR Proteomes; UP000215127; Chromosome 5.
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:UP000215127}.
FT DOMAIN 371..679
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1198..1334
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1480..1619
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1754..1891
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1105..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2036..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1053..1098
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2076..2129
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1105..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2177 AA; 241226 MW; 497AF4EAE7F4C738 CRC64;
MVSPTSLWDK FVQAQQRNHL TAEAQRSFAW LLLEILLWSS DQPPGAEAVA SEITAQRTFL
DSSDRHLRAI GYRIEHILKA KKTGTNIPTA SGPGGRHDND FIDFRHVAIY PTKDELTTKD
PPYYNPAHTL YQVPSEERVA HHLSNQFRLL REDFLAELRL DLNPVPGKGA RRPRTKLSNL
QFRGVFNGGE KNRSSTAIVV SAKKGFGELA NSTNPRAYLK HNHTFLKHSS FGYFIDRGDV
VAFGTIHREE DLLCQKPPAI AIRTPGSGAM RRTLLALAES TTVQFVIIDT AVFAYEPVLK
CLQAKHELPL WEHLLCSEDS SKRLGLSQPS EALSEVTNAI QSKQDLQAVL GLAKSITLDD
SQTESLLAGL RQSVSLIQGP PGTGKSFVGA LLAKALHDNT SENILVVCYT NHALDQFLED
LMDIGIPNSS IVRLGSKSTA RTQPLTLYEQ APAKFRTREN WDAINRLGEE TTSHAATLDQ
ASTTLRSLKA SGPQLLQYLE LSEHDYEFFE AFEVPESEEG FTTVGQDGRE IDESYLLQRW
IHGDDAGVFG QEMSPWHHEI WSMDPYARQA KVGEWQYAML VEAVDDVVDR AHACDASQYT
LSQALSRKAT EMIQQKRIVA CTTTGAAMYS SQIQSAAPGI VLVEEAGEIL ESHVLTAMTP
DTKQLILIGD HKQLRPKVNN YSLTVEKGDG FDLNRSLFER LVMAGFPHTT LTQQHRMCPE
ISNLVRQLTY PDILDAPSTL QREALRGLQN RVVFIEHTKL ELLSPVADRR DHGASVSKQN
EHEVEMVKKI VKYMAQQGYG TSSQVVLTPY LGQLSLLRRK LAEDNDPVLN DLDSFDLIQA
GLLTPASASQ IKRPLLLSTV DNYQGNEADI VIVSLTRSNP DGDIGFLISP ERLNVLLSRA
RKALIIIGNS ATFKASKKGG ELWSSFFNLL AETNSMQEGL PVQCSQHPDR KMLLTCPDDF
DQQCPDGGCS APCGVLLNCG KHACERKCHQ LADHSKIACS FPIQGLCAKG HRLRWTCATG
HPVSCRTCDI EAAALRAQQE RNAKLDQERQ ARQAAYALQL AAVQEELDRL RQTAKDRRTE
EEQAAELAQR QLDLVNARTL AAQREAAEKK KASDSARAKP TKAQVDRIST TSSDDNAENS
ESEAQLDWNR QKATEGASNK AIDSLMAMIG LEAVKDQFLE IKSQIDLLVR QDLSVEKERF
GAVLMGNPGT GKTTVARIYA KFLCSIGALP GDVFVESTGA KLASEGVAGC KKMIEDLLDQ
GGGAFFIDEA YQLASGSNFG GSAVLDFLLP EAENLTGKVV FILAGYNKQM EKFFQHNPGL
PSRFPRRMQF ADYEDHELLA IMNYNINKRY NGRMELKDGA AGLFARIVAR RIGRGRGKEG
FGNAREVENV VSKIAARQAK RVRKERRKVK GKRQDTNDLL FTDRDLIGPE PTNALLTNQS
WKKLQQLTGL RDVKEAIQSL LDSIKLNYER ELAEEPLVEY SLNKVFLGNP GTGKTTVAKL
YGQILADLGM LSSGEVVIKT PTDFVGAVIG ASEANTKGIL DAAVGKVLVI DEAYGLFGGH
SGTTDPYRTG VIDTIVAEVQ SVPGEDRCVL LLGYKEQMEE MMQHVNPGLA RRFPMDSGFI
FQEFDDEDME AILEMKLKAQ AFKITDRAKD VALGMLQRAR NRPHFGNAGE VDIILNDAKL
RQQKRISRDS SVAKGIFEAE DFDPDFERGE RANTNLAALF KDSVACDGIV KQLQGYQNVV
ARMREHNLDP REEIPFTFLF RGPPGTGKTT TARKMGKVYY DMGFLSKAEV VTCSASDLVG
EYVGHSGPKT RKLLESALGK VLFIDEAYRL AGGHFAQEAV DELVDGITNE RFSRKLIIVL
AGYNDQINQL LRTNPGLNSR FPESIVFVSF PPKECLNLLI KNLRKKKLLD IACITSMSPS
EEGQILQRFQ TLASLQNFGN ARDVETMART IFGSLLKSAP SKTASMSVTR DLVLSVLDEM
VTERSRREID STVAGAAFPP APFRAQESTT HATKAETYTA TNTQHICAPE VAADPGAVEE
SPANPADAVD EPPSSPPFTS SVRRDVGVSD AIWEQLQLDQ AKADREEQDF RRLQEEERKL
AEWLKACEDA KQREELRELE RKRKAVEEER CKQILAQEKL KQMGCCPVGY HWIKQASGYR
CAGGSHFMSD DAVDAML
//
