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Database: UniProt
Entry: M2QNN6_CERS8
LinkDB: M2QNN6_CERS8
Original site: M2QNN6_CERS8 
ID   M2QNN6_CERS8            Unreviewed;       437 AA.
AC   M2QNN6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN   ORFNames=CERSUDRAFT_113838 {ECO:0000313|EMBL:EMD38663.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38663.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD38663.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD38663.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445795; EMD38663.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QNN6; -.
DR   STRING; 914234.M2QNN6; -.
DR   HOGENOM; CLU_025709_4_0_1; -.
DR   OrthoDB; 176803at2759; -.
DR   Proteomes; UP000016930; 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:UP000016930};
KW   Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT   DOMAIN          319..434
FT                   /note="ATPase V1 complex subunit H C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11698"
SQ   SEQUENCE   437 AA;  49461 MW;  82EF65DC3240CA7C CRC64;
     MSIALVTNSY LDDYSAKIRA KPVPWEGYQR AGLVTSEELS LIKKVDRQPK AKIESLLLSD
     GQSYTLLFLR LLKKLQRVDT QQFILVLIAD ALADHEERIP LFTRSSQVDP ELPYGPLLRI
     LDSQDDFVQL KTIQILTILL STETSPQPPQ RLQPYLNVIS ALVARPSPQT RDIAVQCLEA
     VLTRPEVRKA VWANASLIAG LVDILKHNPG PQMCYQVGFC LWLLTFEQEV AEQINKKFDI
     IPLLVDVAQS AVKEKVIRVI VATFRNLVTK APSQNLPAML VAHLLPFAKN LATRKWSDED
     VLEDVQFLRD ELNARFESLT TYDEYSSELT SGHLSWSPVH ESELFWKENA TKLNDKDYEQ
     VKTLVRLLKE SSDPVVLAVA AHDIGQYVKH YERGKKVISD LSGKTRVMEL MSHGNSDVRY
     QALVCVQRLV SHPWAAV
//
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