ID F2PM61_TRIEC Unreviewed; 2430 AA.
AC F2PM61;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Nonribosomal peptide synthetase {ECO:0000313|EMBL:EGE02979.1};
GN ORFNames=TEQG_02017 {ECO:0000313|EMBL:EGE02979.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS995724; EGE02979.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TEQG_02017; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_4_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05918; A_NRPS_SidN3_like; 2.
DR CDD; cd19542; CT_NRPS-like; 2.
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; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
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; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 775..851
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1865..1941
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2430 AA; 269419 MW; FA4DF53446FF3A2D CRC64;
MDSAQVHSFN CTSTETRDDS IGKFPLLTDG YSPTCSKFEL ETKRHNICVE EGLTPGNLSE
SIVISAWALT LSIYIGSSNV SFHVLLNDET RWRTSMFHID ACENQTQQQF VQKSQNLLQK
LKSKSISNEN IGDIELLEQP VNTAIVIGHV SSRSDLSALK FVKKFITLDA MGPAVGTCFH
LNYQNSLLSD KQAMNVGSTF AKILSGFRQV SDRPLDSLEY MSQLHISQLW KFNSGSPKEP
WMECFHTVVE RHARGNPRSQ AIDAWDGIFT YAELNNLSII LAKYLQSHGV GPGSVVPISF
ERSAWAIVAM LSVSKAGGAF VSIPPYLPSG RREAMVQMIS PSILLTTSNF CHLWTTGPKC
IPIEGGRINC LPTSEMPLIT RSKPEDTFYI IFTSGSTGAP KGCMVSHSSF LNGALRNAPQ
WKFGPDRRVL QMLSHTFDMS LLEICTSLGS GACVCVPRTE EIEDNLADAI NKYKVSLAVM
TPSLARRLEP KAVPGLQVLC LGGESFPKEL VTLWSERINL FQFYGPSECS INSSTNAITH
KNTDPLNIGV PNNAACWVVS PEDYNKLVPI GAIGELLVSG AIVGQGYYKN PVKTAESFVQ
NVGFLQGDPH YSGWRCYRTG DLVRWNSDGT LVFCGRLDSQ VKLNGQRLEL GEVEYHLTLE
EEVGHAMAIV PGAGRCKDNL MGIISLKSSP PIDSKDKISV LPGALVDQNT QFIRKRLQNS
LPRYMVPTIW AYILRMPMSA SGKIDRVRVR RWVEEMSEST FREITGGIQQ PEDRKPLNKM
EQLIQGIWSA VLDLSTQDVG LHQSFIQLGG SSILAQEVVA KCRKEGIGLT MTDILTCNGI
AGAASLATAL GNNESQKRLL DSTSTQAWRK LQEKYDLSRL GVSHIEEVED VYPCTPMQIG
MFLGQIRKPG SYHLRFFYKP IVKGGKLPEL GRIKSAWHKV VSHHPSLRTV FVDDLGVGAE
YHSVVLRNTS VDVCIDEVPV NLSPSGAMDT FTKSIKPFAK RSTFHRISLC VCGDKVTYLM
IEISHALADG AAMENLMRDF ATAFDDGQLL YQPQSHRDFV EYVASQNNEA SAKYWTSYLK
DCPPCMIPIS KQMMFDDLPT RFLRKDFVYE RSSDFLAKCK EKQITVASAV RVAWALVLRA
YIGSSDVCFT YVAAGRDVPV KDVHKMVGLC LSIQPCRAQL YSGSTFVALA ERMQQDYIES
MPYQHYPLTE LKARLYPKGS EAMFNTAVSM EWTARTNPFY NTSIAFEEIR EQDDPTEYDI
VANVEIVDNI MKLGFLYWPS FSGIDVIHIA NAFKKALDCL LDSADKSAET ISLDGEHEFH
AMKTSDQESL DHTETCVFDA IEKQAMAQLN TQAVVSWDGE YSYGQLTEYY TTYAKYLVEQ
GINSGDIVVV CLDKSCWSVI TILAILKAGA VFVATNPLHS QQRLENIVNH CHAKLIIVEP
RYSSLFETVD TSTIVVNKET VERALLSTTL PAIHDSDIAT IVYTSGTTGL PKGIIIDHGS
LSTSILQGHG KRYGFDNQTR ALQFAAFTFD ACLQEIITVL SHGGCVCVPS EDERLSDLAG
CITQMHVNLA LFTPTVARLI RPQDVPCLKR IILCGEPMSR QDLEVWAGKV TLYNGYGPAE
ATICVSISGP LHVSDDPSNI GYAVEGTRLW ITEAADYNRL APAGCIGELV IESRQVSRGY
LHDVEKTTAM FINPAWLPGC RVYKTGDLAK RNPDGSLTYC GRKDTQVKLR GQRVELGEVE
YHVRECWTNA SGVVAEVICP TGEEKATLAV FVCTGDAQKN ALSDLDGLEE PKNEVSPVWV
SKEFIEKLED RLPCYMVPSI FFTVPSIPLT LSGKTDRQQL RGIGSNFTSE QLARVSDHQK
NSKRTPSGAR ERKLQQLWSS VLNVDKSQIS LDDSFFRLGG DSVSAMRLVT NARKSGINLT
VADVFRHPHI DEQARIASSS SKNILKTLIA KPFAHIQRKD LERVVSLVGL GPYAEIASDI
EDILPATDVQ SFYVSRAAES SRDALNYFYL RFDNTPDIAR LRHSCQGIVD QFPILRTIFI
STQGRTYQVV IRRLQVPFEI HNGVKNLSKA SDIFCLQDLE NKIVSGSLLL SFTLIRHLIS
GSQLIIRMSH AQYDGMSWPL ILRCFQESYA GVPRSPTQSF SSFISYTIGK VNESRKYWTN
LLQGSHMAQI SDKFRTETTL QRLEKTHVEK TVELPIPPKG ITVASLVSSA WSLVLRQITG
KRDVVYGFVV AGRNIGMPQI QEVVGPCMNT VPVRICFNSM RTTIDLQCHA MNQYLAMGDA
DSLGFQDIVE NCTQWPSSTK LDTLLQYHDI DETPVVTLSA GPGSEPCSAQ LDWFRKPYAA
PTNIEVSARP NGNALGITLS SDGSLLSIDS AMAILTMFER SIRILSNGRA LPLDSINLLA
VTGRRNQSKI PDLCPPAYLT FQLLSLMFGS
//
