ID A0A1V9Z630_9STRA Unreviewed; 521 AA.
AC A0A1V9Z630;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=ACHHYP_02523 {ECO:0000313|EMBL:OQR93455.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR93455.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR93455.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR93455.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR93455.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNBR01000409; OQR93455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z630; -.
DR STRING; 1202772.A0A1V9Z630; -.
DR OrthoDB; 75535at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR006970; PT.
DR PANTHER; PTHR36234; LYSYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR36234:SF5; LYSYL ENDOPEPTIDASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF04886; PT; 2.
DR Pfam; PF13365; Trypsin_2; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..521
FT /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012438662"
FT DOMAIN 477..513
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 365..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 55948 MW; 04D65C72D3CA83D0 CRC64;
MHSIAQLAVC LGLFASSAMG QYCFQAVEKI GADQSYNASL SAAETTKTVQ HDKATYIAVH
FSQLDLPAGA SITVSSPNGE SKATYTGKHT DFYAEYIQGD SAVVTYHAPK HGGAEPVISI
DRYASGFPEN KRLNNLESIC GKDDSEASIC YKDKEPTQYK KAQAVARLFM NGSGLCTGWL
FGSEGHMITN NHCIGDAAAA KNVQVEMGAE CTTCNDPNNT KQLGCKGKVV ASSVEFIHTN
KALDYTLVKI NSKDLASYGY LTARASGPVL GEEIYIPQHP GGKPTRIAVK LDDGKPGTIE
DMGHPACVDD EVGYMVDTEP GASGSPVLSA KDNTVIALHN CGGCLNGAIK IDKIVKELQS
LNKLPKNALD GNDDKPTYKP TDEPTDMPTD EPTDMPTDEP TDMPTNEPTD MPTDKPTFMP
TDEPTDKPTD KPTTKPTFKP KPTGKPTAKP TNRPRPSTPR PVTKKPSAKP TSRPSSGAKK
IWEQCGGKDY TGSTSCADQL TCVRMDDWYS QCVPGLGFKW N
//
