GenomeNet

Database: UniProt
Entry: A0A151NFN0_ALLMI
LinkDB: A0A151NFN0_ALLMI
Original site: A0A151NFN0_ALLMI 
ID   A0A151NFN0_ALLMI        Unreviewed;       922 AA.
AC   A0A151NFN0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-NOV-2023, entry version 29.
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:KYO35459.1};
GN   ORFNames=Y1Q_0008030 {ECO:0000313|EMBL:KYO35459.1};
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:KYO35459.1};
RN   [1] {ECO:0000313|EMBL:KYO35459.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO35459.1};
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:KYO35459.1}.
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; AKHW03003201; KYO35459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151NFN0; -.
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        900..920
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          406..514
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51449"
FT   DOMAIN          542..773
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          773..835
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          30..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  103242 MW;  5FDF5204CECD956C CRC64;
     MKVPAVRKIC LPRAVKARAK RRLELGEGGH QYLAEGLKTP KGKGRAATRS PDSPKTPKSP
     SEKTRYDTSL GLLTKKFIQL LSQSPDGVLD LNRAAEVLKV QKRRIYDITN VLEGIHLIKK
     KSKNNIQWMG CSLSDDGGML AQCQGLSKEV TELNQEEKKL DELIQSCTLD LKLLTEDSEN
     QRLAYVTYQD IRKISGLKDQ TVIVVKAPPE TRLEVPDPVE SALIHLSSTQ GPIEVYLCPE
     ENDALSPMKM YSQDHNGNIS KNISKDLASG NSGQGDNSVN MTNLSPLASP TNLLQQTEDQ
     IPSNFEGPFV NLLPPLLQED YLLSLGEEEG ISDLFDAYDF EKLPSLPERR ECGRFINQED
     LKEHLLERLL KDACCLIVPK VRKRNSQKNV QADDDPPSDS IIPGIQKIWI RTWGCSHNNS
     DGEYMAGQLA AYGYKITENS TEADLWLLNS CTVKSPAEDH FRNSIKKAQE ENKKVVLAGC
     VPQAQPRQDY LKGLSIIGVQ QIDRVVEVVE ETIKGHSVRL LGQKKDNGKR LGGARLDLPK
     IRKNPLIEII SINTGCLNSC TYCKTKHARG DLASYPVEEL VGRAKQSFQE GVCEIWLTSE
     DTGAYGRDIG TELPTLLWKL VEVIPEGAML RLGMTNPPYI LEHLEEMAKI LNHPRVYAFL
     HIPVQSASDS VLMDMKREYC VADFKRVVDF LKEKVPGITI ATDIICGFPG ETDEDFQETM
     KLVEEYRFPS LFINQFYPRP GTPAAKVHQV PALVKKQRTK DLSQLFHSYS PYDHKVGERQ
     RVLVTEESFD SKFYVAHNRF YEQVLVPKDP GFIGKMVEVD IYEAGKHFMK GQPVSDAKVY
     TPSLTKPFAK GEVSGVTEEL RHALKNGTNL KTCPSVGIQE KTSLCCRMVM QIPWQQRGRG
     LKILSVSLAL LAVLVTFYYG GV
//
DBGET integrated database retrieval system