ATP25_AJEDR
ID ATP25_AJEDR Reviewed; 724 AA.
AC C5GAC6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=ATPase synthesis protein 25, mitochondrial;
DE Flags: Precursor;
GN Name=ATP25; ORFNames=BDCG_01222;
OS Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER-3 / ATCC MYA-2586;
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- FUNCTION: Probable mitochondrial mRNA stabilization factor.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP25 family. {ECO:0000305}.
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DR EMBL; EQ999973; EEQ84417.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GAC6; -.
DR SMR; C5GAC6; -.
DR STRING; 559297.C5GAC6; -.
DR EnsemblFungi; EEQ84417; EEQ84417; BDCG_01222.
DR VEuPathDB; FungiDB:BDCG_01222; -.
DR eggNOG; ENOG502RGZN; Eukaryota.
DR HOGENOM; CLU_016140_0_0_1; -.
DR OMA; IMIFGTA; -.
DR Proteomes; UP000002039; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140053; P:mitochondrial gene expression; IEA:InterPro.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR040152; Atp25.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR28087; PTHR28087; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..724
FT /note="ATPase synthesis protein 25, mitochondrial"
FT /id="PRO_0000404456"
FT REGION 36..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 81458 MW; BCD2BEF670F020F2 CRC64;
MRRALLTGIQ CHACRNNVVR SFVSVSGVTF MPLASGSWSA SQTRPPPLSR NFSSQHAKLF
SSHPSDNAEV AVDPMPEKDI TEETVKPPEE PEEHIPWYLQ EELEATTSHP LRKQQPLPPL
PENPPPILNG LLEHISIDLG LDDISLLDLR KLDPPPALGA NLIMIFGTAR GVKHLNVSAD
RLCRWLRTTY KLRPDADGLL GRNELKIKLR RKARRAKLAK SAKSTLTAPD DGITTGWICV
DVGTVEGGQF RKPEEEARKV GFVGFGTFVQ GTRIVVQLMT EEKREEVDLE GLWRRTLERN
SLENEGLPQP QAEEPPQEAG DIHKPSSVTP AHISHRVSHA AQISVNYEQR RGISTGSCQY
RDLEEDGLNY APINPDGTIK LPELISESTP LTSLTSRLRN ISPYEAIYHL GQDVNDTNST
TFLEQFYRKL SKAPDDLASA QRIKLICIAI MLHHPGYGKT DLFKVTQEHF ISNYGVTPPQ
FLEILDALLS FKPDLTSDPP NLLLPAADME LALQTIDHVG LRGIDLLNST VWMKLFVGAS
FRVPVCPVRD LMNAPVIGNR TPVSLDTYET VNRVQTRLLK VKTAAKIELS ANEYLSLLRV
LFDHEWYSMF WDTWEEIALA GMPRDKSLYV FLFQLHAESD GWEGWKSTLL NCIPMMEREN
PPVYMDRELA EVIARCLAIA HPEIMDRVER NEPSPLVRLW HRCRITIEKE VPLRGAQNPP
STMS