ID   C6H3K7_AJECH            Unreviewed;      1382 AA.
AC   C6H3K7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=LysM domain-containing protein {ECO:0000313|EMBL:EER45681.1};
GN   ORFNames=HCDG_01260 {ECO:0000313|EMBL:EER45681.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER45681.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; GG692419; EER45681.1; -; Genomic_DNA.
DR   STRING; 544712.C6H3K7; -.
DR   VEuPathDB; FungiDB:HCDG_01260; -.
DR   eggNOG; ENOG502SINF; Eukaryota.
DR   HOGENOM; CLU_004874_0_0_1; -.
DR   OMA; YHAFTPF; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd08621; PI-PLCXDc_like_2; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR13593:SF148; SI:DKEY-152B24.6-RELATED; 1.
DR   PANTHER; PTHR13593; UNCHARACTERIZED; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 2.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..288
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
FT   DOMAIN          471..533
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
FT   REGION          1359..1382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1382 AA;  153153 MW;  C1DF65BEB8B275B8 CRC64;
     MATRHHGILQ SILIWMLLFL QAIASFISPI VREQLPIARK HDIQNAAPGK QMIIPLLVAK
     AAQSDIDEAR RLVDAAIKKA SVLNKARLDH PMRNRYSSTR AAKASRRDAS SRDALLPPLL
     KITNEIAAAA ALLAEVEAVA EAKDLSKPKR DYSYIDALYN RTAEKQAQPF WMEDIERKGA
     WPFGNDPSFK ANDRPVIKAA SSFIGLGVLS TNRYVENGGA GPDGNAKEWY VTTGNFYRQI
     RNFRIDITAT SRDAYVAALH YQVAQATSLT NVDFIASTDP GTTQQAIYGG NQQFTAQRLK
     FNNCKTAVQI IWDWGWIWKN IEVTGSTTGF QLMSEDSVPR TGSILVLDSI FRNTETALLT
     FPASQEKGKG TTGITFDNVA FEAVKNAVVD NQGKVYLSGS VRKVDTWALG PVSFDMSQRD
     YTLGMSFSTK REPTLVTDGL TSLPKAPFFE RAKPQYEAIP VSKFVHMKDR AKGDGITDDT
     ESFQSVLLQY AGSDNIIFVD AGSYILTETI TIPAGAKIVG EGWPQLVAFG PKFQDEKNPR
     PLVRVGNRGD RGDVEIQDLL FTTKGPTAGA VLVEWNIKAA CSGCASMWDS HVRIGGATGS
     ELTSTECPAI TSGVNGDGCK SGSLMMHITD SSSAYMENVW LWTADHDIDD LDWQDNNNTL
     VQTSIYTARG LLVESTEATW LYGTSSEHAL YYQYNFYKAQ NVFAGMIQTE SPYYQPTPNP
     PAPFESAVGI FNGDPAYQNC HCGSPGNDAA WALRIIESSE IYIAGAGLYS WFSTYTQECI
     KTRSCQNSLI QLEGNGGGVR IFNLITIGAT NMITSDGNQF TSQDNLAVDY HPYWSQITII
     DPIQKTGPQR LIKQGLHARN EDKCPPVLPE AILPEGKYPT NLSIIDIGGH SDHGYFTLVN
     GSPYNWILTS SHSYQMDQWK WHNVPAGESV QCEWQFAQSF NRYDDKGEAY YKIEGTDKTF
     QIMARYQDDP NNNFHLRVLY DGLETKDVPK GTSLDFPSRG GLGDMRAMNW VLAGSEEQGY
     WSSHKPPIAW MSSILTIIGE RKLKHVCMPG SHDAGMSKLN GHTEFSNEGN TLTQYLNIYD
     QLRRGSRYFD VRPAIGDGGK FLTGHYSDID ILDIGWQGGN GESIQDIVDG INRFTAENPE
     LIIINLDLTL DTENGYKPFN DEQWSKTFDL FEGVTHLRGG LEGDLSEKKM NDYIGNGQAS
     VIILSSGGAT RPDKGIYSTR QFPRFDSYSN TDVVSTMADD QIAKLKGNRN IVANDAERKD
     VFHVFSWTLT LTRVLERTIA DQSIELAYDP LFWRAYHAFT PFSYPSVLYM DFIGSAEKNT
     KSFDQTTGEV TAMAMAVNMQ LASQNCYVGG GSIVVSKKPP LEHRSEAARP HLMSSKSTLS
     ER
//