ID F9F348_FUSOF Unreviewed; 893 AA.
AC F9F348;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=V-type proton ATPase subunit B {ECO:0000256|ARBA:ARBA00013419};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|ARBA:ARBA00030314};
GN ORFNames=FOXB_00823 {ECO:0000313|EMBL:EGU88657.1};
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:EGU88657.1};
RN [1] {ECO:0000313|EMBL:EGU88657.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88657.1};
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 -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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:EGU88657.1}.
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DR EMBL; AFQF01000304; EGU88657.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F348; -.
DR STRING; 660025.F9F348; -.
DR PaxDb; 5507-FOXG_00954P0; -.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 36..333
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 868..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 97550 MW; 8B3F873E37D92B5F CRC64;
MSLLRSSVCR ACRRSQQIRW HRGLATASNQ SYDNRVRLVE VGPRDGLQNE KKAISLETKI
ELIERLARTG VSTIEAGSFV APKWVPQMSN SSEILQHILD GKVSSPGPIS YSFLAPNGKG
LKSAADVLSA NSGKFATQLE PAAGAEAATK PSVEVAVFAA ATESFTQKNL NCDIKTSLER
FKEVIRDSKA IGLRVRAYIS VVLGCPFEGF DVDPHKVAEI ATDLLEAGAD EISLGDTTGM
GTAPRTGALL QCMSAAGIRT EDIAMHFHDT YGQALVNTAV SLEHGIRTFD SSVGGLGGCP
YSPGATGNVS TENMVYFMET LGMDTGINLD AMSDIGDWIT KELGKENGST TFSRLYLQAS
RSAPIFSFAP SFNRPITDPS PIMADPRESS SYSVIPRIRY NTVGGVNGPL VILDNVKFPR
YNEIVTLTLP DGTERSGQVL EARGDRAVVQ VFEGTSGIDV KKTKVQFTGQ SLKIGVSEDM
LGRIFDGSGR AIDKGPKVLA EDYLDINGSP INPYSREYPE EMISTGISAI DTMNSIARGQ
KIPIFSASGL PHNEIAAQIC RQAGLVQKQG ITNKGVHDGH EENFSIVFGA MGVNLETARF
FTRDFEENGS LERVTLFLNL ANDPTIERII TPRLALTTAE YYAYQLEKHV LVILTDLSAY
CDALREVSAA REEVPGRRGY PGYMYTDLST IYERAGRVEG RNGSITQIPI LTMPNDDITH
PIPDLTGYIT EGQVFIDRAL DNRGIYPPIN VLPSLSRLMK SAIGEGMTRK DHGDVSNQLY
AKYAIGRDAA AMKAVVGEEA LSAEDKLSLE FLEKFERQFI SQGQYESRSI YESLDLAWSL
LRIYPKELLN RIPAKVLNEF YQRAAKESKA KGKARADTEA RSQQQTEENL IDA
//
