GenomeNet

Database: UniProt
Entry: A0A094HD64_9PEZI
LinkDB: A0A094HD64_9PEZI
Original site: A0A094HD64_9PEZI 
ID   A0A094HD64_9PEZI        Unreviewed;       873 AA.
AC   A0A094HD64;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=V502_06689 {ECO:0000313|EMBL:KFZ13310.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ13310.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ13310.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFZ13310.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPKE01002454; KFZ13310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HD64; -.
DR   STRING; 1420915.A0A094HD64; -.
DR   HOGENOM; CLU_014059_0_0_1; -.
DR   OrthoDB; 5473721at2759; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          39..325
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          841..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   873 AA;  95674 MW;  65CD0AD6E8477781 CRC64;
     MALLRPTVRC VRRLNARQLR GFAFATTADP APPPRNNRVR IVEVGARDGL QNEKKTISAD
     TKLDLISRLA KTGLRDIEAG SFVSPKWVPQ MATSNQILES IIKETPDSKF PINYSFLAPN
     VKGFEAAMAV LKAAGHTASP NGPKIEFSVF AAATESFTQK NLNCDIATSL ERFKPVIQGA
     KDAGYRVRGY ISTVLGCPFE GYDVDPHKVA EVATDLLEMG VDEIALGDTT GMGTAPRTAE
     LLRAMTAAGI RNEDMAMHFH DTFGQALVNT AVALEHGIRT FDSSVGGLGG CPYSPGATGN
     VATEDMVYFL ESLGMDTGVD LDAVADIGAW ITNEIERPNS SSVGKAVLGR RTLATLAAMT
     TDPRESSSYN VTPRIRYNTI GGVNGPLVIL ESVKFPQYNE IVNLRLPDGT VRSGQVLEAR
     GTRAVVQVFE GTSGIDVKKT RVEFTGQSLK LGVSEDMLGR IFDGSGRAID KGPKVLAEDY
     LDINGSPINP YSRVYPEEMI STGISAIDTM NSIARGQKIP IFSASGLPHN EVAAQICRQA
     GLVQKQGVTN KGVHDGHEEN FSIVFAAMGV NLETARFFTR DFEENGSLER VTLFLNLAND
     PTIERIITPR LALTTAEYYA YQLEKHVLVI MTDLTAYCDA LREVSAAREE VPGRRGYPGY
     MYTDLSTIYE RAGRVQGRNG SITQIPILTM PNDDITHPIP DLTGYITEGQ IFIDRQLYNR
     GVFPPINVLP SLSRLMKSAI GEGNTRKDHG DVSNQLYAKY AIGKDAMAMK AVVGEEALSS
     EDKLSLEFLE KFERTFISQS PYESRTIYES LDQAWGLLRI YPKELLNRIP AKILAEFYQR
     SERKTKKRQG QKDTRDNTED PSKAGQEENL IDA
//
DBGET integrated database retrieval system