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Database: UniProt
Entry: A0A285IS66_9RHOB
LinkDB: A0A285IS66_9RHOB
Original site: A0A285IS66_9RHOB 
ID   A0A285IS66_9RHOB        Unreviewed;       349 AA.
AC   A0A285IS66;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Molybdopterin or thiamine biosynthesis adenylyltransferase {ECO:0000313|EMBL:SNY50673.1};
GN   ORFNames=SAMN06297129_1916 {ECO:0000313|EMBL:SNY50673.1};
OS   Pseudooceanicola antarcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1247613 {ECO:0000313|EMBL:SNY50673.1, ECO:0000313|Proteomes:UP000231655};
RN   [1] {ECO:0000313|EMBL:SNY50673.1, ECO:0000313|Proteomes:UP000231655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12662 {ECO:0000313|EMBL:SNY50673.1,
RC   ECO:0000313|Proteomes:UP000231655};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OBEA01000003; SNY50673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285IS66; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000231655; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:SNY50673.1};
KW   Transferase {ECO:0000313|EMBL:SNY50673.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..340
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   349 AA;  36610 MW;  3FEC9D8E4EFD0539 CRC64;
     MGWLLLLGVL IWLAGGWLDV SRGRRGAVLA ALWALITGAL ALLPPGHVLA QAWGPLSAWL
     ILGGVVLLVL GYMRGLALLK TRVREEPAPD GPQPLFSDAE LARYARHIVL RELGGPGQKK
     LKEASVLVIG AGGLGAPALL YLAAAGVGRI GIVDDDEVSL SNLQRQVVHG DADVGDAKVF
     SATRRLKALN PHVEIRPYKR RFDDAIAAEL LADYDLILDG SDNFDTRYLS NRTAVAAGKP
     LVSGALSQWE GQLSVFHPAS GAPCYACIFP EAPAEGLAPS CAEAGVVAPL PGVVGAMMAG
     EAVKLITGAG AALRGEMMIY DALWGETRKI ALKRRPGCPV CGATDEVTP
//
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