ID A0A423VL27_9PEZI Unreviewed; 2116 AA.
AC A0A423VL27;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=VPNG_09946 {ECO:0000313|EMBL:ROV91725.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROV91725.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROV91725.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROV91725.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROV91725.1}.
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DR EMBL; LKEB01000089; ROV91725.1; -; Genomic_DNA.
DR STRING; 1230097.A0A423VL27; -.
DR InParanoid; A0A423VL27; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19542; CT_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146}.
FT DOMAIN 780..853
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1585..1661
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2116 AA; 231232 MW; 7630CCEA56825C2E CRC64;
MVIRHLDDSQ GQDRREGQLD VYTQITGQAS GDGFTSYHVA GLAPDQSVTP TTGMRDEILL
ASWLIVLLRT REDGQVQHDW AYRGRATAAK EVEPANTLST SEVMPSLQSS IQQTSEAILR
HITKAVSSQY TAISSPASLL LSTGSLSRTS EGTRDEGVIH LEVRYGNDLL EIRPVWHSDN
VLPYTVTRHV ETLVDTVRIC LSSPEASVED CLGPTAYDVD SIWSWNHLLP PTYDFCMHEM
IAERARRSPE KVAIHSWDGE LTYGQIEQYS TSLAHSLRDL GVQLHDFLPV CFEKSKWTIV
AVLAVMKAGA TIVLMDPTLP LARLQNMAIQ VGAKTMLASR MQHDLSVSIL PQGQLVDVGP
DTFTSLPDLQ ALPPLPAVPA TALMYIIFTS GSTGTPKGVK IAHRDYTSSA IPRAKAVGYN
EDSRVLDFAS YAFDVSIDSM LLTLGNGGCL CIPSDEDRLG DINGVIRNMR INYAGLTPSV
ARILDPDVIT SLSALGLGGE AASPRDVNLW GRDTRIVIGY GPCECTIGCT VNSSAATGRD
YISIGPGNGA AMWITNADDH NTLMPVGAVG ELLVEGPIVG RGYLNDPEKT AAAFIEDPPW
LLAGHKGHAG RRGRLYKTGD LGRYDPDGSG GIVFVGRKDT QVKLRGQRVE LGEIESQLKA
RLPSDINVIA EVIVPQGPGG QSTLVAFFAP QSTKGIQQKE LETVQLSDEL RSALSAADAD
VAKVLPRYMV PTAYVPVNYI PTLISGKTDR KRLRALGATV DLRQLDRERG ASSTVARELT
DLEQRLREAW AVTLKLDADG IRPDDNFFAL GGDSLAAMRL VSVCRERGLE LTVTGTFSHP
TLAGMAEGVL ICDVEAQKET PAFSMISQCA DSARVEASQL CGVDSAAIED IYPCTPTQES
LFTFSLKSTE PYVAQRVARI PSHISLDAWK QAWESVVAAS PILRSRLVQL QDPGLQQVVL
KEGIHWRQST DLQQYLQDDQ NEQMHFGQSL ARYAIVDHPT ESKQYMVWTI HHVVYDGWSE
PMILEQIRDA LQNAGQGTEI QPQAHVQTQM RDFVRFVRDT DEAAMHDYWR RELEGAVGPQ
FPRLPSRDFM PTPDGFVEHL ISFETNSGLP FTPATLIRGA WALVASQYTG SDDVVFGETL
TGRDIALPGV ESILGPLVAT VPIRVHVDRA SSVASYLQTV QQAILDRTPY QHMGWQNIRK
VSRDAQYASE AGTGLVIQPD AEHVGTELGF DQGDPVREAL HFNPYPLMVA CGLRKGGFRV
CASFDSSLIE VSQMKRILAQ LERACQELTR GFSQGRVGDI SCLPEAELDL IWRWNRNAPL
PLDKTLKRLR ADASITKGST YPQAAVPWVC DPRNASLLSP VGCAGELWLE GAFLQGQTVD
SPAWLVAGTP AYAGREGRLQ STGDIVQLRE DGSLIFVGRK DSVVPVQGHA VDIAELEAHF
AKILSVSTRA AAAVFQSSSG SAPQAQELVA FIEQQPSEGT SVEIMPAKHE VKADAADLRP
FKTTICSKIP ISLAVALKRL DKSIENTLSS YMVPSAYIVV DKLPTEAKQV DHNLLNHLAS
RIPPGVLGQL REGLKVAWKK SSAEANLAAP ETILRSSWAK ILGVPPEQID IDDNFFRLGG
DSVLAMKLVS SLRAQGHGLT VADIFQHMRL GDLAKVLKVG QVATSRKAQP YKPYSTLGSL
NVTLFLEEVI RPRLADPTWT IQDVLPVTDS QALDVPGTTQ VPRTSIQYTM LYFDEGIEQE
RLLQACNDLV KTHDILRTVF IEHGSTFFQI VLQELDAPVI KQVADKDLEQ FVTELCTADI
ESEFKLGAPF LRIFHVEGEE GQHCLVLGLS HAQYDGMSLP RLLQDLETLY KGEKVADFEP
FSSYITQVGD ERAQAKAVSY WSDLLKGSSL SVLDGTSTQP GDKAVFQTSL VDVAQPLEGI
TTANLLTAAW ALVVARSVKN TDVTFGSITS GRAIDLTNVE NVIGPCYQFT PVRVPFKSQW
TAQDLLLFVQ RQSAESAAHD FLGFERISQK CTQWSSSSTA EVRFFDSIVH HQDFEDFDTM
PFAGRTPRVE ILNPHGDAAY PLKAVSFVQS GKLHVGVVGS ERDAAFVGSI LAKLAAAVQE
LAEPASQQPL LDAQMF
//
