ID   F2TTG8_AJEDA            Unreviewed;      1494 AA.
AC   F2TTG8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 2.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Pectate lyase superfamily protein domain-containing protein {ECO:0000259|Pfam:PF12708};
GN   ORFNames=BDDG_09476 {ECO:0000313|EMBL:EGE86531.2};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE86531.2};
RN   [1] {ECO:0000313|EMBL:EGE86531.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE86531.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; GG749561; EGE86531.2; -; Genomic_DNA.
DR   HOGENOM; CLU_004874_0_0_1; -.
DR   Proteomes; UP000007802; 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:0004650; F:polygalacturonase 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   InterPro; IPR039279; QRT3-like.
DR   PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 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   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   TRANSMEM        1474..1493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          195..425
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
FT   DOMAIN          565..623
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   1494 AA;  165085 MW;  0914A224030F113B CRC64;
     MATCHHGLLQ SILIWALLSL QVMASFIYPA VTDPLRSAHK HEMGDVVLET QLRLNMAIPS
     RVANATRSDI DKARRIVNAA IEKASVLNKA RLDHPVRNHY PWKPGFKASR RDASSGDAPP
     PLLKISSEIA AASALLAEVE AVAEARDLSK TKRDYSYIDV LYNRTAEKQA STFWMEDIER
     KGAWPFGNDP SFQVFRNVKD YGAYGDGVHD DTDAIKRAMA DAGTCGERCN GATTKNFILY
     FPSGTYLVSS TIETYFGSQL IGDANDRPII KAASSFVGLG VLSTNHYVEG GGAGPDGNPK
     EWYVTTANFY RQIRNFRIDI TATNQGAYVA ALHYQIAQAT SLSNVDFIVS TEPGTTQQAI
     FTENGSGGVM SDLTFTGGNF GIYGGNQQFT AQRLKFTNCK TAVQLIWDWG WMWKNIEITG
     SATGFKLMSE DSVPRTGSIM VIDSIFRDTD TALLTFPATA EKGRGTTGIT LDNVAFEEVR
     NAVADNEGKV YLAGSVLSVD TWAIGPVYFD ISQRDYTLGM DFTTKRESTL LADQSTSLPK
     APFFERQKPQ YEAIPASKFV HMKDHAKGDG VTDDTAAFQS VLSQYASSDN IIFVDAGSYI
     LTDTITIPVG AKIVGEGWSQ LVAFGPNFQD ERNPRPLVRV GNDGDHGDVE IQDLLFTTKG
     PTAGAVLVEW NIKATCSGCA GMWDSHVRIG GATGTELTST ECPAITSGVN DDGCKSGSLM
     MHITRSASAY MENVWLWTAD HDIDDPDLQD DNNTLVQTSV YSARGLLVES TEATWLYGTS
     SEHAVYYQYN FYKAQKVFAG MIQTESPYYQ PTPMPPAPFE SAVGIFSGDP NYERCPYGSP
     GCDASWALRI IESSEIYIAG AGLYSWFTTY TQECIATRSC QNSMIQLEGN NGRVRIHNLI
     SIGATNMIIS DGTQVTSEAN LAVDYHPYWS QITVVDPIHN TGAQRLIKQG LHTRNEDKCS
     VPPDVRVPGG RNPTDLPLVD IGGEADHGYF TLVNGSPYNW ILTYNHSYQM DQWKWHDVPA
     GESVQCEWQF AESFNRFDDK GEAFYTLEGT NKTFQIWARY YQDDPDNEFH LHVLYDGLET
     KDVPKGTSLD YPSRGGIGDM RAINWVLTGS ETEGFWSSHK PPIAWMSSIL HIIGDRKLKH
     VCMPGSHDAG MSKLDGHTQF SNEGNTLTQY LNVYDQLRRG SRYFDVRPAI GNGGKYLTGH
     YGYIDILEIG WQGGNGESIQ EIVDGINRFT AENPELIIIN LDLTLDTDNG YKPFNDEQWS
     KTFDLFEGVT HRRGGLQGDL SEKKMNEYIG NGQACVIIIA SGGPTRPDNG IYSTRQFPRY
     DSYSNTDQID TMAADQIAKL KGNRNLVPND GERKDIFHVF SWTLTLTRVF ERTIADQSIE
     LAYDPLFWRG YHSFTPFSYP SVLYMDFIGS AEQDTKTLEK TTGEVTAMAM AVNMQIASQN
     CYVGGGSIEP KKPEPPVSHQ PTPGSASPPL RPCLISLISA TLLIPLVFFY SCIF
//