ID A0A166IUM0_9AGAM Unreviewed; 434 AA.
AC A0A166IUM0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=SISSUDRAFT_1057087 {ECO:0000313|EMBL:KZT44089.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT44089.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT44089.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT44089.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments. {ECO:0000256|PIRNR:PIRNR032184}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex. {ECO:0000256|PIRNR:PIRNR032184}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC {ECO:0000256|ARBA:ARBA00008613, ECO:0000256|PIRNR:PIRNR032184}.
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DR EMBL; KV428005; KZT44089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166IUM0; -.
DR STRING; 1314776.A0A166IUM0; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.25.40.150; V-type ATPase, subunit H, C-terminal domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR PANTHER; PTHR10698:SF0; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 316..431
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 434 AA; 48824 MW; 39052A59F081B75F CRC64;
MAALLSNAYL DDQSSKIRSK VVPWEGYQRA GHITSDELAL IRKVDRQPRS KTDSIFLTDG
PTYALLYLGL LKKLARVDTM QYILVLIGDA LSERVRFFLK ASESDSELPY GPLVHALDTS
DEFVQLKTAQ ILTIFLSASP TINPSILKPF LQFLSTTLQG SPVNQKKRDV TVQSLEALLP
QPAVRYAVWN NPALIQGLVA ILKDKPSPQL SYQAVFCFWL LTFEKDIAEQ INSKYDIIPV
LTEIAQEAAK EKVIRVVIAT FRNLVSKAPS QNLPSMLVAK LLPFIRSLSS RKFSDEEIVD
DITYLKSELS ENFESLTTYD EYTSELASGH LSWSPVHESD TFWKENAAKL NDRDYEQLKS
LIKLLNESTD PLVLAVAAHD VGQYVKYYER GKKVVSDLGA KTRVMELMGH SSSDVRYQAL
ISVQRLISNP WVTV
//
