ID A0A151NF90_ALLMI Unreviewed; 928 AA.
AC A0A151NF90;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=E2F3 {ECO:0000313|EMBL:KYO35461.1};
GN ORFNames=Y1Q_0008030 {ECO:0000313|EMBL:KYO35461.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO35461.1};
RN [1] {ECO:0000313|EMBL:KYO35461.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO35461.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU003796}.
CC -!- SIMILARITY: Belongs to the E2F/DP family.
CC {ECO:0000256|ARBA:ARBA00010940, ECO:0000256|RuleBase:RU003796}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000256|ARBA:ARBA00008616}.
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:KYO35461.1}.
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DR EMBL; AKHW03003201; KYO35461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NF90; -.
DR STRING; 8496.A0A151NF90; -.
DR eggNOG; KOG4355; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd14660; E2F_DD; 1.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 6.10.250.540; -; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 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; SM01372; E2F_TDP; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF144074; E2F-DP heterodimerization region; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 DNA-binding {ECO:0000256|RuleBase:RU003796};
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 Nucleus {ECO:0000256|RuleBase:RU003796};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|RuleBase:RU003796};
KW Transcription regulation {ECO:0000256|RuleBase:RU003796};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 412..520
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 548..779
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 779..841
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 39..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 103747 MW; B92113065C712958 CRC64;
MFVVEVASYN VSHGTGLSCA VNEAKRRLEL GEGGHQYLAE GLKTPKGKGR AATRSPDSPK
TPKSPSEKTR YDTSLGLLTK KFIQLLSQSP DGVLDLNRAA EVLKVQKRRI YDITNVLEGI
HLIKKKSKNN IQWMGCSLSD DGGMLAQCQG LSKEVTELNQ EEKKLDELIQ SCTLDLKLLT
EDSENQRLAY VTYQDIRKIS GLKDQTVIVV KAPPETRLEV PDPVEQSALI HLSSTQGPIE
VYLCPEENDA LSPMKMYSQD HNGNISKNIS KDLASGNSGQ GDNSVNMTNL SPLASPTNLL
QQTEDQIPSN FEGPFVNLLP PLLQEDYLLS LGEEEGISDL FDAYDFEKLP SLPERRECGR
FINQEDLKEH LLERLLKDAC CLIVPKVRKR NSQKNVQADD DPPSDSIIPG IQKIWIRTWG
CSHNNSDGEY MAGQLAAYGY KITENSTEAD LWLLNSCTVK SPAEDHFRNS IKKAQEENKK
VVLAGCVPQA QPRQDYLKGL SIIGVQQIDR VVEVVEETIK GHSVRLLGQK KDNGKRLGGA
RLDLPKIRKN PLIEIISINT GCLNSCTYCK TKHARGDLAS YPVEELVGRA KQSFQEGVCE
IWLTSEDTGA YGRDIGTELP TLLWKLVEVI PEGAMLRLGM TNPPYILEHL EEMAKILNHP
RVYAFLHIPV QSASDSVLMD MKREYCVADF KRVVDFLKEK VPGITIATDI ICGFPGETDE
DFQETMKLVE EYRFPSLFIN QFYPRPGTPA AKVHQVPALV KKQRTKDLSQ LFHSYSPYDH
KVGERQRVLV TEESFDSKFY VAHNRFYEQV LVPKDPGFIG KMVEVDIYEA GKHFMKGQPV
SDAKVYTPSL TKPFAKGEVS GVTEELRHAL KNGTNLKTCP SVGIQEKTSL CCRMVMQIPW
QQRGRGLKIL SVSLALLAVL VTFYYGGV
//
