ID A0A2Y9P5U8_DELLE Unreviewed; 612 AA.
AC A0A2Y9P5U8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase {ECO:0000256|ARBA:ARBA00018810};
DE EC=2.8.4.5 {ECO:0000256|ARBA:ARBA00013273};
DE AltName: Full=CDK5 regulatory subunit-associated protein 1-like 1 {ECO:0000256|ARBA:ARBA00029733};
DE AltName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|ARBA:ARBA00031213};
GN Name=CDKAL1 {ECO:0000313|RefSeq:XP_022442469.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022442469.1};
RN [1] {ECO:0000313|RefSeq:XP_022442469.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022442469.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-
CC methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in
CC tRNAs that read codons beginning with adenine.
CC {ECO:0000256|ARBA:ARBA00002399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-L-
CC threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine =
CC 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-
CC deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:37075, Rhea:RHEA-COMP:10163,
CC Rhea:RHEA-COMP:11092, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:74420; EC=2.8.4.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000730};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000256|ARBA:ARBA00008616}.
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DR RefSeq; XP_022442469.1; XM_022586761.1.
DR AlphaFoldDB; A0A2Y9P5U8; -.
DR STRING; 9749.A0A2Y9P5U8; -.
DR KEGG; dle:111181408; -.
DR InParanoid; A0A2Y9P5U8; -.
DR OrthoDB; 1122at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006466; MiaB-like_arc_euk.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR NCBIfam; TIGR01578; MiaB-like-B; 1.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..205
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 233..464
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 464..526
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 612 AA; 69157 MW; BEA3E8B8BC4C8A0A CRC64;
MCHGELHLKS LQFPESGVLI FQEDLRLIAN NQEKMPSASC DTLLDDIEDI VSQEDSKPQD
RHFARKHVVP KVRRRNTQKY LQDENSPPSD STIPGIQKIW IRTWGCSHNN SDGEYMAGQL
AAYGYKITEN ASEADLWLLN SCTVKNPAED HFRNSIKKAQ EENKKIVLAG CVPQAQPRQD
YLKGLSIIGV QQIDRVVEVV EETIKGHSVR LLGQKKDNGK RLGGARLDLP KIRKNPLIEI
ISINTGCLNA CTYCKTKHAR GNLASYPVDE LVDRAKQSFQ EGVCEIWLTS EDTGAYGRDI
GTSLPALLWK LVEVIPEGAM LRLGMTNPPY ILEHLEEMAK ILNHPRVYAF LHIPVQSASD
TVLMEMKREY CVADFKRVVD FLKDKVPGIT IATDIICGFP GETDQDFQET VKLVEEYKFP
SLFINQFYPR PGTPAAKMEQ VPAQVKKQRT KDLSQVFHSY NPYDHKIGER QKVLVTEESF
DSKFYVAHNR FYEQVLVPKN PTFMGKMVEV NVYESGKHFM KGQPVSDAKV YAPSISKPLA
KGEISGLTEE FRNRLGNHLN SVSHTLGATQ QDSASSRMAL QLQRLHQDCT LRMSVVLALF
AFLFAFLIKV CN
//
