ID D8QW38_SELML Unreviewed; 451 AA.
AC D8QW38;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN ORFNames=SELMODRAFT_141399 {ECO:0000313|EMBL:EFJ36565.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ36565.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377567; EFJ36565.1; -; Genomic_DNA.
DR RefSeq; XP_002963102.1; XM_002963056.1.
DR AlphaFoldDB; D8QW38; -.
DR STRING; 88036.D8QW38; -.
DR EnsemblPlants; EFJ36565; EFJ36565; SELMODRAFT_141399.
DR GeneID; 9661599; -.
DR Gramene; EFJ36565; EFJ36565; SELMODRAFT_141399.
DR KEGG; smo:SELMODRAFT_141399; -.
DR eggNOG; KOG2759; Eukaryota.
DR HOGENOM; CLU_025709_3_0_1; -.
DR InParanoid; D8QW38; -.
DR OMA; FRWMTFQ; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; IPR000225; Armadillo.
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 InterPro; IPR018506; Cyt_B5_heme-BS.
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 SMART; SM00185; ARM; 4.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 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:UP000001514};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 328..441
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 451 AA; 51929 MW; 4AF862CAA7DA4552 CRC64;
MDPPMDLTRD QVLTRDIPWE NYLNAKLISS TDLQLLRRYD HKPEDAQIAM LEENGVAYVR
VFLRLLDNIT KEETVEYVVA LVDEMLSVDP IKHAALFHDE EFSPEEIYRP FLSLLSRKNW
FLQEKACKIL TVLISARPRQ QAVEVSQKPG PSKNVLQDVL QKLVSWLCIQ LRHPSHPSRA
IPTAVSSLAT LLRDHGVKSM FVQLEGVKLL TPLISPATTQ QYIQLLYEAT LCMWLLSFYS
LAVDAIAATR ALPRLVEVAR TSSKEKVVRV VILTLRNLLT KGTFARDMVE LGMPKIIQNL
KMQAWSDEDL TEALNFMEET LKKNLKLLSS FEKYKQEVLS GNLDWTPMHK DPLFWKENIK
KFEENDFQVL RILVTILDNS RDPRTQAVAC QDIAQFIQFH PAGRGIVLDM RAKDRVMRLM
NHDNSEVRKE ALICVQKLLL NAKYASFMQN K
//
