ID A0A1Y2AW71_9FUNG Unreviewed; 408 AA.
AC A0A1Y2AW71;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pectin lyase-like protein {ECO:0000313|EMBL:ORY26841.1};
GN ORFNames=LY90DRAFT_513655 {ECO:0000313|EMBL:ORY26841.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY26841.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY26841.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY26841.1,
RC ECO:0000313|Proteomes:UP000193920};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|ARBA:ARBA00010980, ECO:0000256|RuleBase:RU361173}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY26841.1}.
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DR EMBL; MCOG01000198; ORY26841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2AW71; -.
DR STRING; 1754190.A0A1Y2AW71; -.
DR OrthoDB; 1331663at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PECTATE LYASE 18-RELATED; 1.
DR PANTHER; PTHR31683:SF187; PECTATE LYASE 18-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR SMART; SM00656; Amb_all; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Secreted {ECO:0000256|RuleBase:RU361173};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012598536"
FT DOMAIN 20..56
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 43807 MW; D7A335D9C8C3D12B CRC64;
MKSFIIITSL FNFASVFAAN CASPFGQCGG STWNGVTCCS SGYACKPMNQ WYSQCVPSNE
VSPSNANNSN VNNSNVNNSN VNNSGNNKAP INNASIPQNN SYAPNVQYAT SNASASSGVI
GYASMNGGTN GGNGGQTITV SNQSQLETAL KGNNAKIIKV NGIIKLDADV TVNSNTSLIG
ANKNSGITGA GLKIKNAKNI IIQNLKFSYC LGSNKDCINA QKSTNIWVDH CEFFNDRNHG
KDYYDGLIDF THASDYITIS WNYVHDHYKA SLIGHSDSNA SEDTGKLHIT YHHNYFKNVG
SRLPSLRFGT GHVFNNVYEN IEASSVNIRM GAKALVEGNV FRNANKPIST NLDSKQEGSV
IQRNNDFGST ANSNSITRTD GLTSVPYQYS AENVNNVYNS VVKSAGPQ
//