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Database: UniProt
Entry: A0A261SNK7_9BORD
LinkDB: A0A261SNK7_9BORD
Original site: A0A261SNK7_9BORD 
ID   A0A261SNK7_9BORD        Unreviewed;       778 AA.
AC   A0A261SNK7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000313|EMBL:OZI38627.1};
GN   ORFNames=CAL29_05170 {ECO:0000313|EMBL:OZI38627.1};
OS   Bordetella genomosp. 10.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI38627.1, ECO:0000313|Proteomes:UP000216020};
RN   [1] {ECO:0000313|EMBL:OZI38627.1, ECO:0000313|Proteomes:UP000216020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU16122 {ECO:0000313|EMBL:OZI38627.1,
RC   ECO:0000313|Proteomes:UP000216020};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:OZI38627.1}.
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DR   EMBL; NEVM01000001; OZI38627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SNK7; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000216020; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR041460; Molybdopterin_N.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF18364; Molybdopterin_N; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000313|EMBL:OZI38627.1}.
FT   DOMAIN          9..49
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          53..505
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          626..740
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          747..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  85784 MW;  B9F950EC6CA9A3A7 CRC64;
     MSAVTRHPTL SHWGAYTALV QDGRLIACEP FPHDPAPSSL IHAMPAMVHS PLRVRRPAVR
     EGWLRNRDTA GRGSDRYVET SWDQALRLVH EELQRVRAEH GPHGVFGGSY GWASAGRVHS
     AITQTHRFLY AGGGCVEQAG NYSWGAAQFL LPHVIGTYKP LTGRVTDWNS VSRHTDLLLA
     FGGMPLRNAQ MIAGGAGAHT TEHWLRRTAE RGARFVIVSP TRGDVPPWLD AEWIPIRPNT
     DVAMMIAMAH TLLAESRHDA AFLHTHCEGY AAYAAYLRGD GDGQPKDAEW AQAICGVPAA
     TIRGLARNAA GCRTLINCTW SLQRAHRGEQ PYWASIALAA ILGQIGLPGG GFSFGTGSIN
     SASNPRPDVA GPEMPELRNP APRNIPVARI ADMLLAPGAE YQFNGRTGIY PDVRLVYWAG
     GNPFHHHQDL NRLARAWRKP ETIVVHESWW TPTARRADIV LPATTTLERN DIGGSTRDRY
     VFAMHQALPP QGESRSDFDI YRELAALGGF EAAFTEGRGE MDWIRHVYAR MGERWRKGPI
     PMPSPPPFEA FWERGYLELP ESERDFILFE DFRRDPAAHP LQTPSGRIEL YSSKVAGFGY
     EDCPPHPCWL PPAEWLGAPA AQRWPLHLIT SQPADRLHSQ LDPAPQSRRH KIQGREPIRI
     HPDDAARRGI KDGMLVRVFN ARGACLAGAM LDIGVSPGVL VMSTGAWFDP GKELERHGNP
     NVLTLDIGTS QLTQGTSAQS ALVEIEPWTG PAPEMRAYES PLARDAGDED GQTPISRE
//
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