ID A0A2A9M9N2_9APIC Unreviewed; 1464 AA.
AC A0A2A9M9N2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN ORFNames=BESB_070660 {ECO:0000313|EMBL:PFH33914.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH33914.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH33914.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH33914.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC position. ATP is required to activate the C2 atom of the wobble base.
CC {ECO:0000256|ARBA:ARBA00003986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC EC=2.8.1.14; Evidence={ECO:0000256|ARBA:ARBA00000897};
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family.
CC {ECO:0000256|ARBA:ARBA00006191}.
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:PFH33914.1}.
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DR EMBL; NWUJ01000007; PFH33914.1; -; Genomic_DNA.
DR STRING; 94643.A0A2A9M9N2; -.
DR VEuPathDB; ToxoDB:BESB_070660; -.
DR OrthoDB; 231303at2759; -.
DR Proteomes; UP000224006; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 3.90.1010.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR PANTHER; PTHR43052; -; 1.
DR PANTHER; PTHR43052:SF1; TRNA-5-TAURINOMETHYLURIDINE 2-SULFURTRANSFERASE; 1.
DR Pfam; PF02657; SufE; 1.
DR Pfam; PF03054; tRNA_Me_trans; 3.
DR Pfam; PF20258; tRNA_Me_trans_C; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF82649; SufE/NifU; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW Transferase {ECO:0000313|EMBL:PFH33914.1}.
FT DOMAIN 469..519
FT /note="Fe-S metabolism associated"
FT /evidence="ECO:0000259|Pfam:PF02657"
FT DOMAIN 1414..1445
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 154699 MW; A001518B8171A701 CRC64;
MLSLNSMADV SHLEQRGCAR RTISAPAPTP FFSVSFEGAA GDRTQSCSSV PRSTAIHLEP
GLPSRVGTGP RVASLSVRDE DARPRAAGAG PACVKPRRGC PIELKFVSAC GRSTVPLLGG
REEGRLWRRS DGAIAFLVSP VRRIASTSVR GWERLSILDR FDIGYRERRA SSLRPAFPLL
LSVSPSPPRP SARPSSVAFR RPSSRVWLDF GDRFPSSALA ATPRSPSLVS APPPLCPSLS
NSPSPPPCTS PPPPRSLPPR LEALLSELKQ PADLQAVFDK LVAFASDLPA PSPARKVAAR
RAAERDSLRE SSPSSSPAFS SVNSAEERDS RPNATEMRHS RDEEGPRDAS AEGDDPPQSW
ERVQGCTALV RIKATLCRPS SPGRKSCQTK GLLPQRQDPR EDPPADLSLP SAASLLSSPA
AASPALTGSR GGLRTEGTED EGEPVTPLPA PRAAPADARG DAERRREGDK VYVHLRGWSD
SLLVRGWLAI LVRGLRNSTP EEILSLTLLD LLSAAGLKPS ERSRPSGPAS AEAAKAEHGG
GEGEKAENRE RREDRLPETR GGTRKKDAGE RRREEEKRRL LVPQGLDNML RSIQRQVRAE
LAGLEEEGEG DRTQANADTG EEEAGESGRV LFSLSSVERS EASALAAEEG GDSAAASSAS
SAEADARELE RRGMRVSLPA AGARQEVAVL LSGGVDSSVS LRLLQRQGLP VRAFFIKIWL
PEYLLMSRHL RRLQERSAGG GGGGGSQSAG EESLGETEGG RGAQGCGWQE DLKFAENVCR
QAGVALEVLP LQEAYWDGVV EHMLQEARAG LTPNPDWWCN CRVKFGAFLD LLDSRGGGAP
QADPLATRSD REAIAAAGGG VARLSPDLVS SAWAGDGDGL VASGHYARVL HWAGRGAGDE
EGGPRRHARL FRGRDPRKDQ SYFLSGLAQR QLRRLITPVG DFHKAEVRRL AASLALPTAS
RRDSQGLCFL GELPLSLFFQ HFLGSAPGPV LHFPSCLALG SHAGLWNFTL GQRKNVTPCL
DVARVRQLSS PQRPRAPAPT NKAQRGAAAG GVASGAEPHK GERSEPAEEA SASGKWQPDE
GGGSASEGRA RTRASTDLDA GKRDLKQAYA ARDSVSAPQG ADGELVQCAY TPGSERGASK
AANAPFQADA GRVQGDHRGE RGRSATGEES AEAEGEAGAG SRLLASPVLS PAGGCHASRV
PDKHFARGFL GPASLAGRWV VTGKHPPSNA LFVVSEKEMN EALSVAARVH YSLAALAAGA
GLAYPERRPE GGSHLLAFLL TLQQKFLLVE DLQWIAGGTP PPSVDSAEAV NAADAGEDAD
AFLQWAFGGV EATTQRDEVQ SHLSVQVRHA GGSACTAIHG AVRLRLLPPA PHPRPCRSLS
SATSFSLASS RARRGSGDGA AAESGRAEVG GWHAWIELAE PDHGLAPGQI AAIYQNDECL
GAGRISAQQG EIALEAAMKA AGLM
//
