ID A0A177C5Q4_9PLEO Unreviewed; 620 AA.
AC A0A177C5Q4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Concanavalin A-like lectin/glucanase {ECO:0000313|EMBL:OAG02481.1};
GN ORFNames=CC84DRAFT_1022988 {ECO:0000313|EMBL:OAG02481.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02481.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02481.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02481.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441556; OAG02481.1; -; Genomic_DNA.
DR RefSeq; XP_018032846.1; XM_018173395.1.
DR AlphaFoldDB; A0A177C5Q4; -.
DR STRING; 1460663.A0A177C5Q4; -.
DR GeneID; 28756881; -.
DR InParanoid; A0A177C5Q4; -.
DR OrthoDB; 337487at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR10963:SF72; GLYCOSIDASE-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 4: Predicted;
KW Lectin {ECO:0000313|EMBL:OAG02481.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008057787"
FT DOMAIN 16..232
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 261..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 64608 MW; 68407E253DAE1CD1 CRC64;
MRYILTASAF AAIANAQTWS LCNPMEKDCD NNPAIAKSFE SNFKDGEGAL KGWQQTAKGA
EFTDEGIVFS VKKTGDAPTI QSDGYLHFGY VEVTMKAARG AGIVSSIVLE SDDLDEVDWE
FIGSDATHAQ MNYFGKGNTT VYDRMIMADV PSIEEVHRYA LNWTSDALTW LIDDAPVRTL
NYADANGGKN FPQTPCNVRI GIWAGGDSKD KGTQDWAGGK VDYSQAPFNQ VVEKVKITNY
SPGKEYEWTD KSGSWESIKV IDGEGVSSGG SKDEPSTTEK PSEEGAAATS TPCTEEATMS
TPPPEETPCD CEVETVTVTG PPPSTETSDV PQPPQTTPPP PETSDSPPPP ESTTCTDSTT
ESVPPPPTTS DSPPPPESTS EVPPPPSSSE VPPPSTSDVP PESTPPPSPP TESTSEVPPP
PPESTSCTES TTESVPTPPA TSDSPPPPET TEESSTVPPS PPQTTPPTEE SSSAPPPEST
PCTESTETTP TPPATSDSPP PPATETTPAP ETSSSVPPPE ETPCTTTTTT EVPPPPPASS
DNCTTLVSVT VPPYPITPTG GIIVDTSAAP SVPYPTNPTG AIPSPPNGTS PPIQEFPGAA
STSTVSYLLA VAAGLMVFAL
//
