ID F9FML5_FUSOF Unreviewed; 1622 AA.
AC F9FML5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000256|ARBA:ARBA00018860};
DE EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473};
GN ORFNames=FOXB_07645 {ECO:0000313|EMBL:EGU81850.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU81850.1};
RN [1] {ECO:0000313|EMBL:EGU81850.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81850.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029433}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00029427}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:EGU81850.1}.
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DR EMBL; AFQF01002285; EGU81850.1; -; Genomic_DNA.
DR STRING; 660025.F9FML5; -.
DR PaxDb; 5507-FOXG_01804P0; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.230.30; Impact, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR036956; Impact_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR020569; UPF0029_Impact_CS.
DR InterPro; IPR022878; V-ATPase_asu.
DR NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF01205; UPF0029; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00910; UPF0029; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1358..1458
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT REGION 524..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1622 AA; 179954 MW; 867752D402213102 CRC64;
MDAQNQELNF DVCVVGAGPL GLLALKNLRE QGLNAKSFER QEYVGGTWHA SNNIEQTTAL
EYTTANTSKQ CCSITDFPMP DDFPVHPPQK DLERYFESYA EQFGLYPHIR FSVSVDHIER
DEPRKAWRVF LKDVKTGVEE VRTFGRVVVA TGMLNTRHLP HVKGLERFSG DAIHSRQFKD
ASKYQGKNVV VVGIGATGVD STSFLVKAGT NKVYLSHRGT VFVLPRRVKG KAFEHTLSRR
LMTKMMINMR DKEWPHLKEV FGTRPVDGVL HRVPLFSEHL ADNLKDGTVK SVQGIKEVTG
PKTITLTDGT VLEDVDAIIF CSGYGYDFSI VEGPGDPTDP AIAPDHHKRI EATKFYGEEN
KFARLFHGFI SEQFPDSLAF LGHMIIMRPP FVLYDLTTMA LASLWSGDYP MPSAEERRRD
IDDHYDYVVK TLQRGPAPHP GFRWRAKPTY EFLNQAAGTG VTDRLGCFTW EAWKLWWNDR
KFYNLLMDGT DVPAVYRLFE TGRGRKPWPA ARESIEKTNQ EVKELGEQWE RENKDKKTKK
AKRQNQLFRT QLMLGIRPTL RARRSLLDLI RTRGEDDDNN SQREQGSDSD DDSLSSGSGA
RGSRYRGSFS DKAPAPPVNV ATVRDPTRKA SSSSWLHSRA GKARAAALAL VDVARQVPLP
NSPPPSPSPS LSPYSPSSRP QPSSQPPPSS TLSPGSAASS IRPQSPHSPI SPHLQLDNAP
VLSLKMPPKT SKAANNSSKT NEEDGYQTGK IYSISGPVVV AEDMIGVAMY ELVRVGHDNL
VGEVIRISGD QASIQVYEET SGVMVGDPVT RTGKPLSVEL GPGLLNGIYD GIQRPLEAIS
KMAKSIYIPR GIAVPALDRE KKWEFTPSVK VGDHLSGGDV WGSVFENSFL ADHKILFPPR
ARGTVTKIAA KGEYTVVENI LEVEFDGKKT EYPMMQTWPV RVPRPSNDKK SADQPFIVGQ
RVLDALFPSV QGGTVAIPGA FGCGKTVISQ SVSKFSNSDV IVYVGCGERG NEMAEVLKDF
PELTIEVDGR KEPIMKRTTL IANTSNMPVA AREASIYTGI TVAEYFRDQG LNVAMMADSS
SRWAEALREL SGRLGEMPAD QGFPAYLGAK LASFYERAGR VQTLGSPERE GSVSIVGAVS
PPGGDFSDPV TTSTLGIVQV FWGLDKKLAQ RKHFPSINTS LSYSKYNTIL DKYYEKNYPD
FPRLRDRIKQ LLSDSEELDQ VVQLVGKSAL SDPDKITLDI AGLIKEDFLQ QNGYSDYDQF
CPIWKTEWMM KLMVGFHDEA QKVIAQGQSW AKVREATSDL QANLRQLKFE VPTDGQDVIS
KRTCNGTNDG FNKLKTQGPQ SPFNQPLTAR TMSEELQDEV EAINSIYGDD SLVPTEDDSS
VFILKLPGDA SSLRLKFPSD YPSKPPSALS THHSSGGVKG AGARDLALFR DALGEVFQEG
LVCLFDAVEE FTRRAEEQKP EPESEPQAPS TPEEEDYEQP DFPPPEWVLS DLVTESKSTF
LAHVARVTSP DQARYYVQLL LSSDKRIRSA THNMTAWRIR GPGATSFQDC DDDGETAAGG
RMLHLMQVMD IWDAMVVVTR WYGGVQLGPR RFALINAVAR DGFVKSGLVK EERQEKKRGS
EQ
//
