CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012434
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Molybdenum cofactor sulfurase 
Protein Synonyms/Alias
 MCS; MOS; MoCo sulfurase; Molybdenum cofactor sulfurtransferase 
Gene Name
 Mocos 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
287HVAPLLRKGYFGGGTubiquitination[1]
684NVSRWLSKFLGRLCHubiquitination[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
 Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form (By similarity). 
Sequence Annotation
 DOMAIN 704 855 MOSC.
 ACT_SITE 424 424 By similarity.
 MOD_RES 264 264 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 517 517 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Molybdenum cofactor biosynthesis; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 862 AA 
Protein Sequence
MACGAAERGP EPPAFQRHLE ASTQRLAHGY GLRSMSELRD QEFGRLAGTV YLDHAGATLF 60
PQSQLTNFTK DLMENVYGNP HSQNITSKLT HDTVEQVRYR ILTHFHTTPE DYIVIFTAGS 120
TAALRLVAEA FPWVSRSPEN SGSHFCYLTD NHTSVVGMRK VAAAMSVTSI PVKPEDMWSA 180
EGKDAGACDP DCQLPHLFCY PAQSNFSGTR YPLSWVEEVK SGRRSPVNAP GKWFVLLDAA 240
SYVSTSPLDL SAHQADFIPI SFYKIFGLPT GLGALLVNKH VAPLLRKGYF GGGTAAAYLA 300
GEDFYVPRSS VAERFEDGTI SFLDVIALKH GFDALEHLTG GMVNIQQHTF ALVQYTHSAL 360
SSLRYLNGAP VVRIYSDSEF SSPDVQGPII NFNVLDDGGK IIGYSQVDKM ASLYNIHLRT 420
GCFCNLGACQ RHLGLSDEMV KKHFQAGHVC GDDVDIIDGR PTGSVRISFG YMSTLEDAQA 480
FLRFISTIYL RSPSDQPVPQ ASISDAGALT SKSDCHSPQE GSCTDPSVCN GSYPDTNIMD 540
LHPSLSKASS AQQTPQDKAA GILNGDPGSH IVTNIYLYPI KSCAAFEVTK WPVGSQGLLY 600
DRSWMVVNHN GICMSQKQEP RLCLIQPFID LQQRIMVIKA EGMEPIQVPL EEDGEQTQIC 660
QSRVCADRVN TYDCGENVSR WLSKFLGRLC HLIKQSPHFQ RNARKTPKKG QPPGTTVALS 720
LVNEAQYLLV NTSSILELQR QLNASDEHGK EESFSMKDLI SRFRANIITK GARAFEEEKW 780
DEISIGSLHF QVLGPCHRCQ MICINQQTGQ RNQDVFQTLS ESRGRKVNFG VYLMHSYLDL 840
SSPCFLSVGS EVLPVLKDCG VS 862 
Gene Ontology
 GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:UniProtKB.
 GO:0030151; F:molybdenum ion binding; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
 GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB. 
Interpro
 IPR000192; Aminotrans_V/Cys_dSase.
 IPR005302; MoCF_Sase_C.
 IPR005303; MOSC_N.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00266; Aminotran_5
 PF03473; MOSC
 PF03476; MOSC_N 
SMART
  
PROSITE
 PS00595; AA_TRANSFER_CLASS_5
 PS51340; MOSC 
PRINTS