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Database: UniProt
Entry: A0A094DNU5_9PEZI
LinkDB: A0A094DNU5_9PEZI
Original site: A0A094DNU5_9PEZI 
ID   A0A094DNU5_9PEZI        Unreviewed;       896 AA.
AC   A0A094DNU5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=V497_00114 {ECO:0000313|EMBL:KFY67979.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY67979.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY67979.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY67979.1}.
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DR   EMBL; JPJZ01000010; KFY67979.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DNU5; -.
DR   STRING; 1420910.A0A094DNU5; -.
DR   HOGENOM; CLU_014059_0_0_1; -.
DR   OrthoDB; 5473721at2759; -.
DR   Proteomes; UP000029268; 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:UP000029268};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          40..326
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          354..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  98314 MW;  6CC8647F5E65A764 CRC64;
     MALLRPTVRC VRRLNARQIR SFAFATASES TAPPPRDNRV RIVEVGARDG LQNEKKTISA
     DTKLDLISRL AKTGLRDIEA GSFVSPKWVP QMATSNEILE SIIKDTPDSK FPINYSFLAP
     NVKGFEAAMA VLKAGGHTAR PNAPKIEFSV FAAATESFTQ KNLNCDIATS LERFKPVIQG
     AKDAGYRVRG YISTVLGCPF EGYDVDPHKV AEVATDLLEM GVDEIALGDT TGMGTAPRTA
     ELLRAMTAAG IRNEDMAMHF HDTFGQALVN TAVALEHGIR TFDSSVGGLG GCPYSPGATG
     NVATEDMVYF LESLGMDTGV DLDAVTDIGA WITNEIEKPN ASSVGKAVLG RRTVAKSPDT
     TPLQQEHPHP PLSPPNFAAM TTDPRESSSY NVTPRIRYNT IGGVNGPLVI LESVKFPQYN
     EIVNLRLPDG TVRSGQVLEA RGTRAVVQVF EGTSGIDVKK TRVEFTGQSL KLGVSEDMLG
     RIFDGSGRAI DKGPKVLAED YLDINGSPIN PYSRVYPEEM ISTGISAIDT MNSIARGQKI
     PIFSASGLPH NEVAAQICRQ AGLVQKQGVT NKGVHDGHEE NFSIVFAAMG VNLETARFFT
     RDFEENGSLE RVTLFLNLAN DPTIERIITP RLALTTAEYY AYQLEKHVLV IMTDLTAYCD
     ALREVSAARE EVPGRRGYPG YMYTDLSTIY ERAGRVQGRN GSITQIPILT MPNDDITHPI
     PDLTGYITEG QIFIDRQLYN RGVFPPINVL PSLSRLMKSA IGEGNTRKDH GDVSNQLYAK
     YAIGKDAMAM KAVVGEEALS SEDKLSLEFL EKFERTFISQ SPYESRTIYE SLDQAWGLLR
     IYPKELLNRI PAKVLAEFYQ RSERKTKKRQ GQKDTRDNTE DPSKSGQQQE ENLIDA
//
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