ID A0A1Y3NFL1_PIRSE Unreviewed; 616 AA.
AC A0A1Y3NFL1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carbohydrate-binding module family 18 protein {ECO:0000313|EMBL:OUM64771.1};
GN ORFNames=PIROE2DRAFT_8385 {ECO:0000313|EMBL:OUM64771.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM64771.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM64771.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM64771.1,
RC ECO:0000313|Proteomes:UP000195826};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; KZ150852; OUM64771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NFL1; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd11618; ChtBD1_1; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..616
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012824907"
FT DOMAIN 574..616
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 101..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 461
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT DISULFID 590..604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 616 AA; 67666 MW; 4F7901A5D1274263 CRC64;
MKNNNKILFF LLNSILLINI IFAKSVNTSS DGGEIISKKG SKDQKYVIFV NNTFGEYNIF
SNPYNKKHVK RQEVQSYDFA VSLMDEIDEL INENRDTFKD QEKLEEIDNQ SKLRKRDSDD
KTGNYYDNSS FVHPVSSQGS SLLISAYLSE ELAKKIEKMD NVEAVVPDIE ITPDANYYNK
NDILKESEWK GLSVQGNADL HLSVISQGLY NNKLVGQYDE NYYYPSSAGK GIDIIVIDSG
FNFDYSEYSN TERTAKCSVV FNSDGKPTIP KNKKVCGSTQ YFHGHKVADI AAGLKRGIAK
SANIYGVAIP VKESEVFDVS YVVEALDYLL KNNMIRPNKT IINISLGGYS KKVNGNLSNL
NLKVQELVKT IINKGGVVVA SAGNNGKNVD KGSEVYVPCY IDNIICVGGI QSDEISSVTN
KYVKSAKSNY GKRVDIYAPY NVHAEFNENG KIKRIYGSGT SYSTPLTAGI IATIMSDNPN
TKFTKKSILN YLLNDGISFN VEGLTKKVIN NGKHIVYSSN GKYKGCGINA GNQPCSNSSN
SSKSSNSNSS KTSNSSKSSN SSKTSNTIPV STVKARCGPE YGRCANSNEC CSQYGWCDTT
SAHCGTGCQP KYGICK
//
