ID A0A0E0F8Q2_9ORYZ Unreviewed; 522 AA.
AC A0A0E0F8Q2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amidase domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI11G19030.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI11G19030.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI11G19030.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI11G19030.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000256|ARBA:ARBA00007296}.
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DR AlphaFoldDB; A0A0E0F8Q2; -.
DR STRING; 40149.A0A0E0F8Q2; -.
DR EnsemblPlants; OMERI11G19030.2; OMERI11G19030.2; OMERI11G19030.
DR Gramene; OMERI11G19030.2; OMERI11G19030.2; OMERI11G19030.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_621716_0_0_1; -.
DR Proteomes; UP000008021; Chromosome 11.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18176; ATP-synt_Vo_c_ATP6C_rpt2; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 2.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR11895:SF67; AMIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 2.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 487..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..205
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 220..407
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 454..512
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT REGION 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 55749 MW; C030DC4A6BBEB854 CRC64;
MGPTCAATMF VNLFTACHTP LTLIRISKYI IWMKYQLPQA DYIKAVKQQL MGFIMDEIVN
SVGEFHDDGG LIPRDELSDG DGDGAGGTRW LGRARACAAD AAVVAQLRAC GAVLAGKTNM
HELGAGTSGI NPHHGSTRNP HNPGRVSGGS SSGSAAAVCA GLCPVALGVD GGGSVRMPAA
LCGVVGFKPT AGRLSNAGVL PLNWTPELNL PLLKSSLSIK NIKLAKYAKW FNDSSEDIRN
CCDKSLQMLH AHYGWETLDV TIPEIEEMRL AHYVTIGSEC TASLAKYLDK LRRSEIGWDV
RVALGVYGSF SSRAYLNSQR LRNRQMYFHK EIFKTADVIV SPMTGVTAYK LQDDALKSGE
LDYINGAALV RYSIAGNFLG LPAITVMVGY DKAGLPIGLQ FIGRPWRRAR STTRSLKCST
ISSRKIKPVG FIISTGINPK AKPYYLFDGY AHLSSGLACG LAGLAAGMAI GIVGDAGVRA
NAQQPKLFVG MILILIFAEA LALYGLIVGI ILSSRAGQSR AD
//
