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Database: UniProt
Entry: A0A0A2J6N9_PENEN
LinkDB: A0A0A2J6N9_PENEN
Original site: A0A0A2J6N9_PENEN 
ID   A0A0A2J6N9_PENEN        Unreviewed;       487 AA.
AC   A0A0A2J6N9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=ATPase, V1 complex, subunit B {ECO:0000313|EMBL:KGO50999.1};
GN   ORFNames=PEX2_094650 {ECO:0000313|EMBL:KGO50999.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO50999.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO50999.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO50999.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO50999.1}.
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DR   EMBL; JQFZ01000311; KGO50999.1; -; Genomic_DNA.
DR   RefSeq; XP_016594011.1; XM_016746735.1.
DR   AlphaFoldDB; A0A0A2J6N9; -.
DR   STRING; 27334.A0A0A2J6N9; -.
DR   GeneID; 27682155; -.
DR   HOGENOM; CLU_022916_3_0_1; -.
DR   OrthoDB; 5473721at2759; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR   CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR   CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR   CDD; cd01135; V_A-ATPase_B; 1.
DR   Gene3D; 3.40.50.12240; -; 1.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   PANTHER; PTHR43389:SF4; ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 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:UP000030143};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          24..87
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          216..349
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   REGION          461..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53976 MW;  B07ADF78701C3A0E CRC64;
     MPGFIDPRMA SVKPRIRYNT IGGINGPLVV LDNVKFPRYN EIVSLTLPDG TERSGQVLEA
     SGNRAIVQVF EGTSGVDVKK TKVEFAGHSL KLGVSEDMLG RIFDGSGRAI DKGPKVLAED
     YLDINGQPIN PYTRVYPEEM ISTGISAIDT MNSIARGQKI PIFSAAGLPH NEIASAIARQ
     ASLVRPTKDV HDGHEENFSI VFAAMGVNME TARFFTPNDP TIERIITPRL ALTTAEYYAY
     QLEKHVLVIM TDLSAYCDAL REVSAAREEV PGRRGYPGYM YTDLASIYER AGRVEGRNGS
     ITQIPILTMP NDGMGSPLLI FDFEGQIFID RQLANKGIYP PINVLPSLSR LMKSAIGEGR
     TRKDHSDVSN QLYAKYAIGR DAAAMKAVVG EEALSAEDKL SLEFLEKFER TFISQPSHES
     RSIYESLDIA WNLLRIYPRE LLNRVPKRTL DEFYARSARK VASKDTRDNS GEEQDTTAQQ
     NTNLIDA
//
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