ID A0A2K3P6S4_TRIPR Unreviewed; 1356 AA.
AC A0A2K3P6S4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=tRNA(adenine(34)) deaminase {ECO:0000256|ARBA:ARBA00012740};
DE EC=3.5.4.33 {ECO:0000256|ARBA:ARBA00012740};
GN ORFNames=L195_g007576 {ECO:0000313|EMBL:PNY10979.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY10979.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNY10979.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY10979.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNY10979.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY10979.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000256|ARBA:ARBA00001103};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:PNY10979.1}.
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DR EMBL; ASHM01004215; PNY10979.1; -; Genomic_DNA.
DR STRING; 57577.A0A2K3P6S4; -.
DR Proteomes; UP000236291; Unassembled WGS sequence.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR CDD; cd01285; nucleoside_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR PANTHER; PTHR11079:SF179; CYTOSINE DEAMINASE; 1.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 1162..1284
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT REGION 164..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT UNSURE 258
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:PNY10979.1"
SQ SEQUENCE 1356 AA; 152453 MW; 1DB85CA2166D79F3 CRC64;
MHNAYFSSTI YGVRCKESFP LSFNGYSNQW YERFDRTSSQ CSSCRSCCDC CALSTCRVPV
KPCILNGLRQ STLLQLSASR KLVFRSEDLY VSRVPYGLVR GSYELKCSTN ERNVCNTSRR
SRIKERCVCS ASQKGRENSP SFASDDSELV LSFLIEEADK DATGVKSNNV SSSKRMEAEK
KRNNVSRERH LNLSEKIKTK KKGNLKKHEV SSIDLRRECE KSDTERKAFT KGENSRKQRD
MSSCSSYYTL SSGDFESDME EQHDMGLEEF SQAYENDEAN RVEGKVKEEF NRQRVEPKKV
HNVSNKERIV SGADIDWNIR KKSEKKLTEG TVQETQSTRH QDMHSKRSTI HDSGYGKASI
SQKQVHSEED NSSFVEHLDK KTNKAYIQTG NRRKHQSSYA QESGRDEIET TSLSRKKFSG
SEENLEISNT LFKETSDKHE KFVGSTSTTG MESLKSKKTF GGKEAKLEMS ETRLQETSDK
HKKFIGSNST TTNDVIERSS QKYIGNLKIE DTEKISDTRM KNTGEKKYSV LGSTQGVELQ
HHKEETIIAH DKDRRRKSQQ FSEVSQVHGS HVEDTSILKS KISVKNQEER SYLSSHARDT
RLQTDRRRTQ SVQHSKGYEH VSTLSEGCAS DEKQVSSSQI TSEKNRFIPK SKSASAVKTR
ESSSQTEERI FQFANDQQRH ITDETVAREK SSFRGSLNSV SETGKQVILA ESDERSSEIT
LIPSSQRGRV SGHIEHTEEF ASPDIYLETS ESGSSALYGH SGRSPAMFSG PHSQYGSDKS
YSEPSIVMTP EDVLGSANRL EESSKQFVDE FVERVRHEVT TSERQEMEVA RTQLAIDIED
NQMHSSRQQG TQKDSQSKSH DSSRSTGSLG AKGISDEMWD VKEPSVGHGR LAEEPEINET
AKPIVNRTGR SLWGVISDIV RLRWNSRASS STSAGRSGRN SPKKSDSEAW FSGQEHEETG
KSVLPQAMTF DKSKPDTRYT RSEGDVSDTE ILKHKGKRIE VGSSSPNKLE SEGDLSGTEI
LKDKGKHIKV GSSSPNKLES GSTSIGTTYA AGEEFFTPTA IEKDLQATTS GFHKIESPIP
SLSVRGQPIA GEIVNIGGSN ISRTESVVSI KEPVAPEKIE SSGSKRTDGE LKQRKLQRKG
QVLRDRFDDW EDAYKVEFEQ RRIDELFMKE ALLEARKAGD TWEVPVGAVL VQHGKIIARG
SNLVEELRDS TAHAEMICIR EASKLLNSWR LSETTLYITL EPCTMCAGAI FQARIDTVVW
GAPNKLLGAD GSWIRLFPDG EETSEASNLP PAPVHPFHPK IKIRRGVLAT ECADVMQQFF
QLRRRKKKDD LPVVTRRHHP SKLLNKLHDI FHVMCM
//
