ID A0A094G047_9PEZI Unreviewed; 1004 AA.
AC A0A094G047;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=MoaB/Mog domain-containing protein {ECO:0000259|SMART:SM00852};
GN ORFNames=V498_02665 {ECO:0000313|EMBL:KFY96489.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY96489.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY96489.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY96489.1}.
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DR EMBL; JPKA01000426; KFY96489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094G047; -.
DR HOGENOM; CLU_010186_2_0_1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
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; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SMART; SM00320; WD40; 4.
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; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 260..294
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 340..488
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 764..914
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 514..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..545
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 106561 MW; 3610D3F31E111222 CRC64;
MSLATQFEIS TPPADVISAV KFAPESPNRL LVSSWDKYLH LYEVQGGENA SGTLVNKFEH
RAPVLDTCFG AGNDEAFTAG VDWQVKRIDL STGEQTVLST HEAPANRVVY SKEHSLLISS
SWDSTLHFHF LSDPSRGPTT ITLPAKPFSL SLSPTRLVVA MASRLVNIYD LKSTALLSSQ
AVDGKSEVEP WQKRESSLKF MTRAVACMPN DAGYATSSIE GRVAVEWFDP SDSSQARKYA
FKCHRQPDSS GDGSDIVYPV NALTFHPIHG TFASGGGDGV VALWDAVAKR RIRQYQKYAT
SVAALSFSAD GKYLAIGVSP GYEDGKEFNP DGLVKVFIRE LVSTTAVEDP STDKSCDILK
DVFREEAGGQ WAWDVVETKI VGDVVEDIQE AIKNWAGQEN PVNVIVTTGG TGFAVADNTP
EAVSPLLHRQ APGLVYGMLS SSAAITPFAL MSRPVAGIRN KSIIITLPGS PKGAKENLQS
VLKLLPHACL QAAGADSRSL HAGGIKKLES EAGISSTGAH AGHHHHGHSH SHGHSHSHKH
DHGHATPVRH TTATDSPQSN DPSAGPSRRH RSSPYPTLEV SRALELIKNE TPTPQIISAK
VDGSLVGFVL AEDVTATEAV PAYRASIVDG YAVIAPEGGE SSAGVFPVAS ISHAAPGEIK
PLLKGQIARI TTGAPLPPGA TSVIMVEDTV LKSTSEDGTE EKEVEILATN VKSGENIREV
GSDIQSGSVI LRKGDQISAT GGELGLLVSV GRTEVNVYRR PVVGVLSTGD EIVQHDRPGP
LRLGEVRDCN RPTIMAAIRG WGFEARDLGI ASDTPGSLEE TLRATLRQVD VIITSGGVSM
GELDLLKPTI ERQLGGTIHF GRVAMKPGKP STFATVPVKS NDGVPVKKLI FSLPGNPASA
IVTLHLFVLP SLHFACGVQP AGLPSVPVLL GHEIRLDKQR KEYHRAVVSV GRNGRLVAAS
TGAQRSSMVG SLKSANALLC LPIGDKIGKG EEVQALLLGN ISAP
//