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Database: UniProt
Entry: E0ST57_IGNAA
LinkDB: E0ST57_IGNAA
Original site: E0ST57_IGNAA 
ID   E0ST57_IGNAA            Unreviewed;       660 AA.
AC   E0ST57;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Molybdenum cofactor synthesis domain protein {ECO:0000313|EMBL:ADM28718.1};
GN   OrderedLocusNames=Igag_1925 {ECO:0000313|EMBL:ADM28718.1};
OS   Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignisphaera.
OX   NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM28718.1, ECO:0000313|Proteomes:UP000001304};
RN   [1] {ECO:0000313|EMBL:ADM28718.1, ECO:0000313|Proteomes:UP000001304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC   {ECO:0000313|Proteomes:UP000001304};
RX   PubMed=21304693; DOI=10.4056/sigs.1072907;
RA   Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL   Stand. Genomic Sci. 3:66-75(2010).
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046}.
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DR   EMBL; CP002098; ADM28718.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0ST57; -.
DR   STRING; 583356.Igag_1925; -.
DR   KEGG; iag:Igag_1925; -.
DR   HOGENOM; CLU_010186_3_0_2; -.
DR   BioCyc; IAGG583356:GHAH-1914-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001304; Chromosome.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00887; MoeA; 1.
DR   CDD; cd05466; PBP2_LTTR_substrate; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   InterPro; IPR024370; PBP_domain.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   Pfam; PF12727; PBP_like; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   4: Predicted;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001304}.
FT   DOMAIN          195..333
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   660 AA;  72990 MW;  ADBC45D741692FB6 CRC64;
     MDPNAVDRRI FHRLVSLEEA IHILESEGIL KPIDIDEVDL LESYGRILAE DIYAPIDYPP
     FDRSEVDGYG VMVKSVEGAD ELNPIELTVK GSVKVGESPS IAIDLGEAVE IATGAMIPRG
     VEGVVMEEYT ERIDNRKVVV YRSVYAGENI AYAGSDIAIG ELVIPRGTTL TYSEIAVLAA
     LGIRRVKVFK SPKVFVISTG NELIEPGKSL DIGKIYDSNG YLITSLLKML NIDVKFYGIV
     KDDEEELYKV IVDALKEYDI VVTSGGTSAG LEDVVYRVFS RVGRIVVHGL KLKPGKPTVI
     AVSNNGKLLI GLPGFPFSAV SNALLLLIPI IKKIMGSSDQ NIFVKAKIGN KIRKDIGRKW
     FVPVVLNKVA GEVYAIPFSY SSGNISVLIK ADGIALLPEN RDVIDEGEYI DVLPLSNRAI
     EGIIMGSHDI LLNEILNRSG LLNRFRVISI GSYNGVELIK KGYIDIAPIH IFDETEGLYN
     IPLFKKDEVL REKAFLVRGY ERRLVLAFRP GNPKNITSFE DILRKDIRFV NRNRGSGTRA
     YIDYILRKLA EKLGVSFSDL VRRINGYRYE VSTHSGVAAA IAQGRADIGV CIEYAAIIYN
     LNYIPLSWES YDFIVSKDSY KSKGVVKAFL NVLRSSSIKD IINSTKGYRA SEDIGEIICC
//
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