CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018503
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonylcarbamoyladenosine tRNA methylthiotransferase 
Protein Synonyms/Alias
 CDK5 regulatory subunit-associated protein 1-like 1; tRNA-t(6)A37 methylthiotransferase 
Gene Name
 Cdkal1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
515GEVSGLTKEFRNRLGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine (By similarity). 
Sequence Annotation
 DOMAIN 63 171 MTTase N-terminal.
 DOMAIN 430 492 TRAM.
 METAL 72 72 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 108 108 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 137 137 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 213 213 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 217 217 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 METAL 220 220 Iron-sulfur (4Fe-4S-S-AdoMet) (By
 MOD_RES 498 498 Phosphothreonine (By similarity).  
Keyword
 4Fe-4S; Alternative splicing; Complete proteome; Endoplasmic reticulum; Iron; Iron-sulfur; Membrane; Metal-binding; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 578 AA 
Protein Sequence
MPSASCDVLL DDIEDIISQE DSKPQDRQFS RKHVFPKVRR RNTQKYLQEE PRPPSDSTIP 60
GIQKIWIRTW GCSHNNSDGE YMAGQLAAYG YKITENASDA DLWLLNSCTV KNPAEDHFRN 120
SIKKAQEENK KVVLAGCVPQ AQPRQDYLKG LSIIGVQQID RVVEVVEETI KGHSVRLLGQ 180
KKDNGKRLGG ARLDLPKIRK NPLIEIISIN TGCLNACTYC KTKHARGNLA SYPIDELVER 240
AKQSFQEGVC EIWLTSEDTG AYGRDIGTDL PTLLWKLVEV IPEGAMLRLG MTNPPYILEH 300
LEEMAKILNH PRVYAFLHIP VQSASDSVLM DMKREYCVAD FKRVVDFLKE KVPGITIATD 360
IICGFPGETD QDFQETVKLV EEYKFPSLFI NQFYPRPGTP AAKAEQVPAH VKKQRTKDLS 420
RVFHSYNPYD HKIGERQQVL VTEESFDSKF YVAHNRFYEQ VLVPKNPAFM GKMVEVDIYE 480
SGKHFLKGQP VSETRVYTPS ISKPLAKGEV SGLTKEFRNR LGNHPNGTSD TCPATQHGSA 540
YSRMVLQMSQ YDCALKVATG LALLALLLHF WPDSLLTM 578 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0009451; P:RNA modification; IEA:InterPro.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR006638; Elp3/MiaB/NifB.
 IPR023970; MeThioTfrase/rSAM.
 IPR005839; Methylthiotransferase.
 IPR020612; Methylthiotransferase_CS.
 IPR013848; Methylthiotransferase_N.
 IPR006466; MiaB-like_B.
 IPR007197; rSAM.
 IPR023404; rSAM_horseshoe.
 IPR002792; TRAM_dom. 
Pfam
 PF04055; Radical_SAM
 PF01938; TRAM
 PF00919; UPF0004 
SMART
 SM00729; Elp3 
PROSITE
 PS51449; MTTASE_N
 PS01278; MTTASE_RADICAL
 PS50926; TRAM 
PRINTS