ID A0A2B7Y547_9EURO Unreviewed; 671 AA.
AC A0A2B7Y547;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|ARBA:ARBA00020007, ECO:0000256|RuleBase:RU003470};
DE EC=3.1.1.96 {ECO:0000256|RuleBase:RU003470};
GN ORFNames=AJ79_01713 {ECO:0000313|EMBL:PGH16606.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH16606.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH16606.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH16606.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333;
CC Evidence={ECO:0000256|RuleBase:RU003470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522;
CC Evidence={ECO:0000256|RuleBase:RU003470};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003470}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|RuleBase:RU003470}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000256|ARBA:ARBA00010898}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH16606.1}.
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DR EMBL; PDNB01000016; PGH16606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Y547; -.
DR STRING; 1447875.A0A2B7Y547; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000223968; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00256; D-aminoacyl-tRNA deacylase; 1.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF69500; DTD-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU003470};
KW Hydrolase {ECO:0000256|RuleBase:RU003470};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PGH16606.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000223968};
KW RNA-binding {ECO:0000256|RuleBase:RU003470};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW tRNA-binding {ECO:0000256|RuleBase:RU003470}.
FT DOMAIN 307..469
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 608..641
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 158..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 73877 MW; AFB8D88FC0796836 CRC64;
MKAVLQRVAS ASVTVDKKLV SSIGRGLLVF AAVGPEDTKQ DADSLATKVL KLKMWPDEAG
KTWKKSVQDI QGEVLCVSQF TLLAEVKKGN KPDFHNAAEV SKAKELYDYF YNKVRDLYNA
DRVKNGVFQA MMEVGLVNDG PVGVDYRSED EAVTIQIDTT LKKEKKNGNG NGNKNGNGKG
NEDKNGDGKS KDKGPEGDDE GKVFDGGVCS VCLMEASTSS SFCLLKEHHQ QLYFNIHLSP
NSLSLLSLLL TVFPYSLLTT PLLPVSLLSI SIMAETTGTL PLTPPPQLPT RHTANSWHFF
PGRPRVYFDI QIGNKFEGRI AFELVIVPKT AENFRALCTG EKGEGKAGKP LSYKGSIFHR
VIKQFMIQGG DFTAFNGTGG ESIYGEKFPD ENFELKHDRP FLLSMANSGP GTNGSQFFIT
TVPTPHLDGK HVVFGEVLNG KGLVRKIEKA PTDSGDKPLA EVKVIDCGQL SGEGYEAATQ
TAVDETGDKY EDYPEDAGQE LAGTEYYKIA SDLKEFGNKA FKSNNLDLGI EKYQKGLRYL
NEYPDTQESD PPELESQMST LRFTLHSNSA LLANKLKRYQ DGRTWAGYAL DTLNAKDSKA
KVDDKDKAKA YFRRAVALAG LKDEDKALVD LEEAAKLSPA DAAIPQEIAR VKKVINEQKR
KEKEVLKKFF Q
//
