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Database: UniProt
Entry: A0A4S8IYI3_MUSBA
LinkDB: A0A4S8IYI3_MUSBA
Original site: A0A4S8IYI3_MUSBA 
ID   A0A4S8IYI3_MUSBA        Unreviewed;      1324 AA.
AC   A0A4S8IYI3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=tRNA(adenine(34)) deaminase {ECO:0000256|ARBA:ARBA00012740};
DE            EC=3.5.4.33 {ECO:0000256|ARBA:ARBA00012740};
GN   ORFNames=C4D60_Mb10t10160 {ECO:0000313|EMBL:THU53032.1};
OS   Musa balbisiana (Banana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=52838 {ECO:0000313|EMBL:THU53032.1, ECO:0000313|Proteomes:UP000317650};
RN   [1] {ECO:0000313|EMBL:THU53032.1, ECO:0000313|Proteomes:UP000317650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC   TISSUE=Leaves {ECO:0000313|EMBL:THU53032.1};
RA   Yao X.;
RT   "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT   function divergence in polyploid bananas.";
RL   Nat. Plants 0:0-0(2019).
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:THU53032.1}.
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DR   EMBL; PYDT01000008; THU53032.1; -; Genomic_DNA.
DR   STRING; 52838.A0A4S8IYI3; -.
DR   Proteomes; UP000317650; Chromosome 10.
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:UP000317650};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          1122..1244
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   REGION          827..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..868
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1324 AA;  148719 MW;  2308935A831F54FC CRC64;
     MYGGHAAATF AVRAKSSVCH SRRLSLLDDG GGDEFALHGL SINRRFMLYG YYSRQSSLIY
     WSHLRTFLAG HGGHHYLRLS LRDVQPCAPR VPARRGGFRA CCCCRSPQPR FQMAGECCRE
     SFDDGMWEDD ADYVEFGDMT RHSKREVKIR PVDAEKVRSL RARKDASSSV CHSCGHENKM
     SGGLSSGGKK CYTGKKVNAA VREVRKGWKM DDDVDYDSRE ESDYRDRNYN VRDLTSARVS
     NRKTEGRAAK LIASAYQEKE DHHFKVEDKV KKRDSREGSR KFANIVKVDD NVDVANSFID
     MADLKKVDRD KRVVEQDKQE VEQRGASCSF LAHGRRDEYY LGRQNIIGRE SREGSQKSVI
     ASDVHEDDMM MTSRPKRHVD ERKVDMAESS LKQHGQVDKR VVRRAESRTE VGDEYVNNEN
     QVAVLRESIE GSQRSRRIPE VHEDNAERIA SAESMLDTRK VDKEHSSTSI MKKHTAVGQQ
     AVRSYESREQ LQNFRQIEEV HNSNIKKVSN KEKRHEEVLV KNRDDKSISV HMARDNRGHI
     GQQIIDKMEL GKQYENQVDV SRPHVRGTES ASSSQSLLQS RINDRVDYST SIMNPIHQVE
     KHQTQSENQY TYQYSPKRES GKAMCTSELP RKDSGKVSTA QVMYNADIQN ELNNCQYSSR
     RECETDARMS EYAVTDIQRN FNLQNISNMR IGNGKERSSL LMVQDDKKKL GTLTGESSQP
     INQEITSLGA FDGDSSFLDT HMQQPDDPAC GDENYLVKSD TLDSASRLES SSAMYVGEFV
     DKLRHESSTF ISSGTQTEKA HGKGIQATTS MQSDRLVATI TEKDEKYIQE GSGRSSRSGI
     RGPSDEMWDV RSLISQKDGR KEEQGEHGLS AGVIDSTTTT PTVENTIAGR SPKSLWAHIS
     DIMRMGWVHR AESHTSNQKS GKRSSSEGSE AWFSGQDASD DENDPNARSS EIKELLPVAV
     PVDRGHETHS SITQGCFQAP DVVVMQLGGG ASTSMTTAGG YASKGASANS RPEQTTLAEN
     EKGTKSIISR AVTVDKPSLM TGDASSVAID EGITYTGNLT VPVSGYTNFE EDLLREEPPE
     ADKTEGKDGE LKRRKLQRNK QVLKETFEEW EEAYRFESEQ RKIDEYFMRE ALVEAQKAAD
     IWEVPVGAVL VQNGKIIARG FNLVEERRDS TAHAEMICIR EASNLLRTWR LAETTLYVTL
     EPCPMCAGAI LQARVDTVVW GAPNKLLGAD GSWIRLFPGD NGGSSSLDPS SQMAGPVHPF
     HPNIRIRRGV LATECSDVLQ QFFQLRRKKK KKPESPPQSC LPVPNHPIKL FTRMHNIFSV
     MFCL
//
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