ID   PELF2_ASPTN             Reviewed;         480 AA.
AC   Q0CZD4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Probable pectin lyase F-2;
DE            Short=PLF-2;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF-2; ORFNames=ATEG_00950;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CH476594; EAU39596.1; -; Genomic_DNA.
DR   RefSeq; XP_001211036.1; XM_001211036.1.
DR   AlphaFoldDB; Q0CZD4; -.
DR   SMR; Q0CZD4; -.
DR   EnsemblFungi; EAU39596; EAU39596; ATEG_00950.
DR   GeneID; 4355713; -.
DR   VEuPathDB; FungiDB:ATEG_00950; -.
DR   eggNOG; ENOG502QXM6; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; DWCGSYP; -.
DR   OrthoDB; 1267775at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0047490; F:pectin lyase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..480
FT                   /note="Probable pectin lyase F-2"
FT                   /id="PRO_0000394361"
FT   REGION          386..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  49721 MW;  9DB26533B27B4B46 CRC64;
     MTLIRTVLMA AALLGASAHA QGVVGKPFGF AAGTTGGGNA APAAPSDIKE LAQWLSDDTP
     RVILIDKEFD FTGSEGTCAD CACCVPSSNT CGSSGQNAIE TSFGWCGSSP NVTCTYDKAG
     TKGMDVGSDK SIVGVGSAGV IRGKGLRLTG GASNVIIQNI HITDINPEYI WGGDAISLDG
     TDKIWIDHVK ISLVGRQMFV TGYESSGSVT ISNSEFDGRT SWSASCDGHH YWTLLGLGKN
     EQITFARNYI HHTSGRSPKL GESSYWHSYN NYWSDNSGHA FDVESAGKSL IEGNVFSNVK
     TPLTKENLDG VFAVSADDES TCSGSLGRSC IPNVLTSSGE LSSAGDGVFS GWLSDEGDLT
     LMPASQVASY VKAHAGVGKL GAGDYSSSAI PSSTPAPSSS ALAKRHGGHD RHGLGHIPHL
     TEGGPGAWHT PGPAPSWSWR TIGVRSTALP TPSPSSSSCA IGKPTAGPPR FPIFGDLGIF