Variant position: 80 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 636 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human FLTDSFGRQHSYLRISLTEK CNLRCQYCMPEEGVPLTPKAN
Mouse FLTDSFGRQHSYLRISLTEK CNLRCQYCMPEEGVPLTPKAD
Bovine FLTDSFGRHHSYLRISLTER CNLRCQYCMPEEGVPLTPKAD
Caenorhabditis elegans F--DMFMREHTYLRISLTEK CNFRCLYCMPAEGVPLKPKDK
Drosophila -LTDSFGRHHTYLRISLTER CNLRCDYCMPAEGVPLQPKNK
Slime mold ILTDRFNRHHTYLRISLTER CNLRCKYCMPEEGVMLSQADK
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 636 Molybdenum cofactor biosynthesis protein 1
64 – 277 Radical SAM core
1 – 383 Molybdenum cofactor biosynthesis protein A
80 – 80 Iron-sulfur (4Fe-4S) 1; 4Fe-4S-S-AdoMet
84 – 84 Iron-sulfur (4Fe-4S) 1; 4Fe-4S-S-AdoMet
87 – 87 Iron-sulfur (4Fe-4S) 1; 4Fe-4S-S-AdoMet
73 – 73 GTP
86 – 86 S-adenosyl-L-methionine
64 – 64 Phosphoserine
1 – 87 Missing. In isoform 4 and isoform 7.
80 – 80 C -> S. Impairs precursor Z synthesis.
84 – 84 C -> S. Impairs precursor Z synthesis.
87 – 87 C -> S. Impairs precursor Z synthesis.
Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase.
Leimkuehler S.; Charcosset M.; Latour P.; Dorche C.; Kleppe S.; Scaglia F.; Szymczak I.; Schupp P.; Hahnewald R.; Reiss J.;
Hum. Genet. 117:565-570(2005)
Cited for: VARIANTS MOCODA TRP-67; GLY-80 AND PHE-84;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.