ID A0A498JA70_MALDO Unreviewed; 1968 AA.
AC A0A498JA70;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000256|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_03053};
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000256|HAMAP-Rule:MF_03053};
GN Name=NCS6 {ECO:0000256|HAMAP-Rule:MF_03053};
GN Synonyms=CTU1 {ECO:0000256|HAMAP-Rule:MF_03053};
GN ORFNames=DVH24_020057 {ECO:0000313|EMBL:RXH91034.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH91034.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH91034.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH91034.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC intermediate required for 2-thiolation. It is unclear whether it acts
CC as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC onto the uridine of tRNAs at wobble position. {ECO:0000256|HAMAP-
CC Rule:MF_03053}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:RXH91034.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RDQH01000334; RXH91034.1; -; Genomic_DNA.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000290289; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR CDD; cd01993; Alpha_ANH_like_II; 1.
DR CDD; cd13846; CuRO_1_AAO_like_1; 1.
DR CDD; cd13872; CuRO_2_AAO_like_1; 1.
DR CDD; cd13894; CuRO_3_AAO_like_1; 1.
DR CDD; cd17039; Ubl_ubiquitin_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_03053; CTU1; 1.
DR InterPro; IPR032442; CTU1_C.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034273; CuRO_1_AAO-like.
DR InterPro; IPR034271; CuRO_2_AO-like.
DR InterPro; IPR034275; CuRO_3_AO-like.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR15204; LARGE PROLINE-RICH PROTEIN BAG6; 1.
DR PANTHER; PTHR15204:SF5; UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03053};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03053}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03053};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_03053}.
FT DOMAIN 24..99
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 96..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1392..1423
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 96..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1968 AA; 212777 MW; 9FC4B0AFAE3CBD08 CRC64;
MADQHSNEGT SSGNVAGADC DSNLEINIKT LDSQMYSFQV DKNMRVSLFK EKIADQTGVP
VGQQRLIFRG RVLKDDHPLS EYHLENGHTL HLVIRQPSQP QPSSGTSSGE AHANSGNDPS
GVPRGRIGQI SHSVVLGTFN VGDQGEGAVP DLNRVIGAVL NSIGIGTQAT TNGTGNPQFT
TSVSNLNTPG QPPNGNEAEG SRNVNRGGHQ AQYGQAFPTQ PFQTFPQAVQ PPHAAAAFPM
PSSNMPIPHS LNTLSEFMNR MEQGLSQNGY QPNTSATNTG EPPRVNLPST AEGMPTPEAL
GIVLRHAERL LSNHAVSALS HIAGRLEQEG VSPDPSVRGQ IQTESIQLGL AMQHLGSLLL
ELGRTIWTLR MGQSPGEAVV NSGPAVYISP AGPNPIMVQP FPLQTSSLFG GSVPQPNPTS
FGPVGIGSAP RNVNIHIHAV GARGSNGEGI PSGSRDSGGR VLPVRNVVGA TIPSSQTGVA
VSAASQPGPG GSVSQPPSGS PLSSIVAELN SHIGNAQPDD TAQSGQEVST GPYVDSRNYA
GSERPSTDYV DVAGQSSVSL PGCTSESEGL KDLASGSTLK NDSRSPAGGP LSSSSGQNTV
VREDEKRSAP QSSEKQAEDV KAVPLGLGLG VLERKRQARQ PKPSTKNGDG GTTSAPINQN
QQVIGGQQVL QSLASRGSAA SRMNLNDAPE RQTAPAVGQV RDGRTLGGQG PIGQVDMGSM
MSQVLQSPAL NGLLAGVSDQ TGVGSPDVLR NMLQSFTQNP QMRSAVNQIA EQVDGQDLGN
LFGGGQGGGI DLSRMFQQMM PIVTRALGAG SPPVRPSSAL APESHPPHNE RSLGRDDNIP
NSEINLEEVV QRIENLNAPG EVFHALVENS VQLSGRGSGS QELVDELCRD ESLSSEYVEI
LSRDIRRRLE GDSGKDKIGA LICFALLWMY HLILSFDRVS SRSMESSTDG KQKKAAGRQC
CICHERRAAL KRPKTLEQIC RECFYKVFEE EIHQVIVENQ LFKPGERIAL GASGGKDSTV
LAYVLSELNR RHNYGLDLFL LSVDEGITGY RDDSLETVKR NEIQYGLPLK IVSYKDLYGW
TMDEIVKMIG LKNNCTFCGV FRRQALDRGA ALLKVDKLAT GHNADDIAET VLLNILRGDI
ARLSRCTSIV TGEDGPIPRC KPFKYTYEKE IRLDYFSTEC IYSPNAYRGF AREFIKDLER
IRPRAILDII KSGENFRIST STKMPEQGTC ERCGYISSQK WCKACVLLEG LNKGLPKLGI
GRTRGLNNDD KKDAKERNGT KSIESKQCGR KETTHVILWD RILSGTYLSG SSGSSRKTHS
SHSRSGSALC NRVSVVMASS VPPSSSAGVQ NSKKSLGFIA NAVKRKDSFI QFFAMTGILL
LSVRSLGQKY RLHNLQEDTT ALKEEQEALA ERTRNIKRDL LHEASLEPTA GGAISALLCL
AALFSIAVAE DPYRFFEWNV TYGDIYPLGV RQKGILINGQ FPGPDIHSVT NDNLIINVFN
SLDEPFLLSW NGIQQRRNSF VDGVYGTTCP IPPGRNFTYI LQVKDQIGSF YYFPSLDFHK
AAGGFGGIRI LSRPRIPVPF PDPDGDYTVL IGDWYKSNHT TLKAHLDSGK KLPSPDGILI
NGRGPGGFSL NFEQGKTYRL RISNVGLQNS LNFRIQNHKM KLVEVEGTHT LQTTYSSLDV
HVGQSYSVLV TADQPGQDYY IVASSRFTSP ILTTTGTVHY ANSAGAVSGP PPGGPTIQVD
WSLNQARSIR TNLTASGPRP NPQGSYHYGL INLTKTYVLE NSAGQVNGKQ RYGVNSVSFV
PADTPLKLAD YFKIGGVFRV GSISDKPTGG GLYLDTSVLG ADYRTFVEIV FQNNEDIIQS
WHLDGYSFFV VGMDGGQWTT ASRDAYNLRD AVSRCTTQVY PKSWTAIHIA LDNVGMWNLR
TEFWARQYLG QQLYLRVYTS STSLRDEFPI PRNARLCGRA SGQRTRPL
//
