ID   A0A1S3ILQ0_LINUN        Unreviewed;       785 AA.
AC   A0A1S3ILQ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=molybdopterin molybdotransferase {ECO:0000256|ARBA:ARBA00013269};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269};
GN   Name=LOC106165239 {ECO:0000313|RefSeq:XP_013398821.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013398821.1};
RN   [1] {ECO:0000313|RefSeq:XP_013398821.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013398821.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00007589}.
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DR   RefSeq; XP_013398821.1; XM_013543367.2.
DR   AlphaFoldDB; A0A1S3ILQ0; -.
DR   STRING; 7574.A0A1S3ILQ0; -.
DR   EnsemblMetazoa; g7089.t1; g7089.t1; g7089.
DR   EnsemblMetazoa; XM_013543367.2; XP_013398821.1; LOC106165239.
DR   GeneID; 106165239; -.
DR   KEGG; lak:106165239; -.
DR   InParanoid; A0A1S3ILQ0; -.
DR   OMA; HYDEDIR; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR   PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          16..163
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          179..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  85938 MW;  57F23695C8811ECD CRC64;
     MATSSEMEHG TKIKIGILTA SDSCFEGKAE DKSSANLKIL IEDKKIIPGK VVVQSCVPDD
     IEQIKEKLTI WSDALKLDLI LTTGGTGFAP RDVTPEATKS ILHKEAPGMT IAMIKASLDV
     TPLAMLSRLV CGTRGSTLII NLPGSKKGSQ ECLEFVTPAI PHAVDLLQGN KENVVTTHTH
     LQAETTPEPP VKNRKATLRS SRNQQTQLQE KQLPKTTDEQ VASASVIPQR LTRQQQTIVY
     LTNMTSDGEI TVVPQYPSGK NPKSKEGAQS GSDSNPVVAL HDKDQQKSHL DQNSDLNVSS
     EISPPSRKST RLSLKKKVKQ RASFQETADN DETSSAQTDV YDFEEDGENS KSGSPKAGGS
     GNADILKAKR NKKLLEGAEI IEVPVGVELK NFLSTHEVLK DTHLVRGKRH VKRSLLHLQR
     QENAVDTGSW KRGSRVHERN RLDDYFTPTA EGLLKIEAIQ KKAIRDEYAV NWYLWCSGVG
     NCKRQCGGYG KCVDGCSGPR HKQDRHNCSL LLNLKIYLSN LSMWVIRISG RHVDDKVEWI
     PPPTSGGHYD EDIRDVLMTF SDQVSSPSQV HKILVQKKGH ADIPSKHKVE CFVTSLRRRR
     RAKDYDYASK IRKTEDVNSS IHNYSCNTQA TGSGISGHES GGVPTATQTL LQLENNQPGC
     TETVQYQDTS NLVPVAVVGQ YGNAVMCSAS NTQVAREVVI GGQSDIHTSE PSVVYGTTEG
     SVIQEFIHNG QTIRVIRNTL EPVAQSEVIV QTQQDPQSGT MGLYGSQSPG LSNVGALLSA
     AYQTQ
//