ID A6VYF6_MARMS Unreviewed; 1083 AA.
AC A6VYF6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Amino acid adenylation domain {ECO:0000313|EMBL:ABR71485.1};
GN OrderedLocusNames=Mmwyl1_2568 {ECO:0000313|EMBL:ABR71485.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71485.1};
RN [1] {ECO:0000313|EMBL:ABR71485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71485.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000749; ABR71485.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VYF6; -.
DR STRING; 400668.Mmwyl1_2568; -.
DR KEGG; mmw:Mmwyl1_2568; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_10_6; -.
DR OrthoDB; 9757559at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
FT DOMAIN 531..606
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1083 AA; 123699 MW; 52D88A17F15ACAF9 CRC64;
MIDTECKENK NDFRYQFPKN VCVHQLFEQQ VERSPEKTAL VFGDEELSYG ALNASANCLA
RRLLTSGVGS ENLVGLYVDR SFEMIIGLLA ILKAGAAYVP LDPEYPAARI EQMLEDCLPS
KILVSGLNNQ HLSEEIETIS IPAVLDEYAQ SSNVKREELT KPITQSNLAY VIYTSGSTGK
PKGVLIEHEG LVNLVQYQRD EFLADDTCRV LQFTSISFDA AVFEWTLALC NGGTLFLVSR
DATTNPRELE RIIKEYDITH TNLVPSVLRN ISPSCFSRTA YVISAGEALP EDVRSKFAKQ
CNFYNGYGPT EVTVASSYCR IDDDNRSVSI GKPLSNKIVY VVDESRKLVE SGEVGELLIG
GVGISRGYLG REDLTKEKFI SDPFNERGGR VYCSGDLVKW LPDGNLQFIG RADEQVKIRG
FRIELGEIEK VIRKQADVKD VIVTTIEGIN GRKHLKAYVV TDTVFCEGGE SRRRILVENC
KVQLEKVLPE HMIPGLWSLL SGWPLLINGK IDRKKLQELE LIDVRKVNYL APSNEIERRL
CEIFSSVLKV ESVGINDNFF YLGGDSITAG IILHEIGREY GVEIKLNKFF ENPEVSELTL
LIKNKSQNNQ SPGIVPRPNQ YRNKIAPSSF QKQILFMFEI NNDDKPYHAK SAINFYGKVD
LERLDASIRK VVKKHEIYRT GFHNENDDYV QKIVPEIEFD IPVFNLLNFS LGEKRLFVED
ILNLKSIEAF DIERAPLTRW VVLKLSEELT SLLYIEHHLV HDGWSYNIFL QDLFREYNDG
SLCLPSLQYG DFVLSHEMWM YSEQSEDQLK FWEENLKDSP QQTTLPSDWR RQEAGSEGKT
LRIAMNRKAW QRLDQLSIDV GVTKFNILLT AMYILIFSHT KAKDLLLGTG AANRSWKDSN
NIIGMFVNSI VIRNQLDEDC TVEELIKKVS HSCLEAFDND KVAFESVVER INPLRAPKVN
PFFQIMLAFH DSVFPDINTQ DAKVRVIEAL ENGGAKFDMT VVVIPRKGQY LEKDPVHFVW
NYNTGLYRES TVKEYIEQYF SILQNLVEMR SERVIDLQRK EIDINKIKES FEYLPESFLE
WCM
//