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
//