ID A0A3L8RUM2_CHLGU Unreviewed; 349 AA.
AC A0A3L8RUM2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=ATPase F1/V1/A1 complex alpha/beta subunit nucleotide-binding domain-containing protein {ECO:0000259|Pfam:PF00006};
GN ORFNames=DV515_00016172 {ECO:0000313|EMBL:RLV84493.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV84493.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV84493.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV84493.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV84493.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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:RLV84493.1}.
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; QUSF01000265; RLV84493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RUM2; -.
DR STRING; 44316.ENSEGOP00005018593; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF1; V-TYPE PROTON ATPASE SUBUNIT B, KIDNEY ISOFORM; 1.
DR Pfam; PF00006; ATP-synt_ab; 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:UP000276834};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..231
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 349 AA; 39120 MW; A311B76FCEC21E90 CRC64;
MIQTGISPID VMNSIARGQK IPIFSAAGLP HNEIAAQICR QAGLVKKSKD VVDFHEDNFA
IVFAAMGVNM ETARFFKSDF EQNGSMENVC LFLNLANDPT IERIITPRLA LTTAEFLAYQ
CEKHVLVILT DMSSYAEALR EVSAAREEVP GRRGFPGYMY TDLATIYERA GRVEGRNGSI
TQIPILTMPN DDITHPIPDL TGFITEGQIY VDRQLHNRQI YPPINVLPSL SRLMKSAIGE
GMTRKDHGDV SNQLYACYAI GKDVQAMKAV VGEEALSADD LLYLEFLHKF EKNFISQGPY
ENRSIFESLD IGWQLLRIFP KQLLKRIPEN ILAEFYPREA KAPEQGTAL
//
