ID A0A093UV02_TALMA Unreviewed; 1065 AA.
AC A0A093UV02;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Linear gramicidin synthase subunit D {ECO:0000313|EMBL:KFX41529.1};
GN ORFNames=GQ26_0580300 {ECO:0000313|EMBL:KFX41529.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX41529.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX41529.1}.
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DR EMBL; JPOX01000058; KFX41529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UV02; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_002220_2_1_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
FT DOMAIN 576..656
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1065 AA; 118000 MW; A94A02198A82F71A CRC64;
MTVNELGTAF TWPKLSLLEG EGDARSLPEL IDFQARVNPH RRFCIQAQKS TDAPLLDVTY
AQLKHAVSCC QDWLGKNVPE IQLENGTKDR PVGLLMDSDL TLVIYLFALM GLGIPTVLLS
TRLSAEAVKH LVQKTRTSAI LVSARLDGTA NEALSSWDAS DSSPPSKYCP AAYRDFMTEN
TTSSTAFTES NVGRKNHFVS ESDCNVLILH SSGTTGLPKP IYTSHRHYLS FALCHEFKNA
EEMLSPALST SPLFHGFGLL PPCLSLGMGK PFCLPEAGTI FTGPSTAQLL RNSGAKSLLT
VPSVLEEIAL LPDDEGIHVL QELHFIVFGG GLPKETIGDK LTAAGVKLLN HYGATETGPL
APLYVPQRGY DWHYFKLRTD IQDALQVSLE PIVEENQESE SRWKLSLQPV GWTERFPLQD
ILVPRPSSDS DNEYTVLGRS DDLIRLATGE KVRPTIVESM LAQSEAVKAA VAFGDGQFEI
GVLIEPTFKI SSAEEEDALK SSLWPIIQLA GEKMDAHARI SSSQAIVVVQ AGSLPRSDKG
TVLRREVNQR FEKEIAEVYR KLDGVIDYSI PPLRLNSLEA DLRKLINDNL KWTNNSEWTD
ERDFFELGMD SLQSTILRRL LVSSLRDGLS KVSIGRDFVY QHPSVAELAK AVREGCGNQA
ASSVDGSLLD VFIDMYSLQR QQKSNGYGEN DTATVLLTGG TGSLGSHLLA HLVQKSVVRH
VVCMNRPSTG KQDPYDRQAA ALKSKGLSIS PEEWSKVIVF ETNTGSPKLG LSGADYTWLC
ERITHIVHNA WPMNFKMHVS SYKSQFRVLQ HLLLLARDAH AHQQPTRRTR VLFISSISTV
GWYGKFTAET IVPETPIQDF RTALDLGYAQ AKLVCEKIIE RARNDFGTEI EVGYIRIGQI
AGAQGGFWNT DEHFASLVAS SEALGHLPDI RGPRAYGTVY HLENPVRQPW NEVLDILASE
LDVDKHNRIP MAEWLEDIMK RRPDDGNPVA ALADFFQEDF EWMSGGSIVL STETSRRHSP
TLRRAGPVHD ETIRRYVQYW RGIGLIRGLK NQALPVDSSS LLSFS
//