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Database: UniProt
Entry: S2K1V3_MUCC1
LinkDB: S2K1V3_MUCC1
Original site: S2K1V3_MUCC1 
ID   S2K1V3_MUCC1            Unreviewed;       509 AA.
AC   S2K1V3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE            Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE   AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN   ORFNames=HMPREF1544_07057 {ECO:0000313|EMBL:EPB86155.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB86155.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC       ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC       complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC       that translocates protons. V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments.
CC       {ECO:0000256|RuleBase:RU366021}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex attached to an integral membrane V0 proton pore
CC       complex. {ECO:0000256|RuleBase:RU366021}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR   EMBL; KE123995; EPB86155.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2K1V3; -.
DR   STRING; 1220926.S2K1V3; -.
DR   VEuPathDB; FungiDB:HMPREF1544_07057; -.
DR   eggNOG; KOG1351; Eukaryota.
DR   InParanoid; S2K1V3; -.
DR   OMA; GFKIKPR; -.
DR   OrthoDB; 5473721at2759; -.
DR   Proteomes; UP000014254; 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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
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; IPR005723; ATPase_V1-cplx_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
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   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 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   ECO:0000256|RuleBase:RU366021};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU366021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT   DOMAIN          33..99
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          156..385
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   509 AA;  56836 MW;  6AB3A355E0C6E887 CRC64;
     MAKTLSAREA FELHKSAVTR DFIAKPRLDY RTVTGVNGPL VILDNVKFPK FSEIVNLTLP
     DGSVRAGQVL EVQGKKAVVQ VFEGTSGIDA KQTHVTFTGQ TQHIPVSEDM LGRVFNGSGK
     PIDKGPKIFA EDYLDVNGSP INPFSRIYPE EMIQTGVSAI DTMNSIARGQ KIPIFSAAGL
     PHNEIAAQIC RQAGLVQKMA PTKGVHDGHE ENFSIVFGAM GVNMETARFF KQDFEENGSM
     ERVTLFLNLA NDPTIERIIT PRLALTTAEY YAYQLEKHVL VILTDMSSYA DALREVSAAR
     EEVPGRRGYP GYMYTDLSTI YERAGRVEGR NGSITQIPIL TMPNDDITHP IPDLTGYITE
     GQIFVDRQLH NRQIYPPINV LPSLSRLMKS AIGEGMTRKD HGDVSNQLYA KYAIGRDAAA
     MKAVVGEEAL NQEDKLSLEF LEKFEKTFIA QGAYESRTIY ESLDLAWSLL RIFPKELLNR
     IPQKVLAEFY QRERSKRSKG VFDTNDDEE
//
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