ID F0U7Q8_AJEC8 Unreviewed; 1382 AA.
AC F0U7Q8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=LysM domain-containing protein {ECO:0000313|EMBL:EGC41627.1};
GN ORFNames=HCEG_00989 {ECO:0000313|EMBL:EGC41627.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; DS990636; EGC41627.1; -; Genomic_DNA.
DR STRING; 544711.F0U7Q8; -.
DR VEuPathDB; FungiDB:I7I53_07414; -.
DR HOGENOM; CLU_004874_0_0_1; -.
DR OMA; YHAFTPF; -.
DR Proteomes; UP000008142; 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:UP000008142};
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..532
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; 153101 MW; 985786821E62FBC3 CRC64;
MATRHHGILQ SILIWMLLFL QAIASFISPI VREPLPIARK 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 TTGITLDNVA FEAVKNAVVD NQGKVYLSGS VRKVDTWALG PVSFDMSQRD
YTLGMSFSTK REPTLVTDGL TSLPKAPFFE RAKPQYEAIP VSKFVHMKDR AKGDGITDDT
ESFQSVLLQY AGSDNIIFVD AGSYILTETI TIPAGAKIVG EGWPQLVAFG PKFQDEKNPR
PLVRVGNRGD RGDVEIQDLL FTTKGPTAGA ILVEWNIKAA 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 IVANNAERKD
VFHVFSWTLT LTRVLERTIA DQSIELAYDP LFWRAYHAFT PFSYPSVLYM DFIGSAEKNT
KSFDQTTGEV TAMAMAVNMQ LASQNCYVGG GSIVVSKKPP LEHRSEAARP HLMSSKSTLS
ER
//