ID A0A167A3V6_9PEZI Unreviewed; 620 AA.
AC A0A167A3V6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Aspartic proteinase {ECO:0000313|EMBL:KZL79687.1};
GN ORFNames=CI238_06342 {ECO:0000313|EMBL:KZL79687.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79687.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79687.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79687.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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:KZL79687.1}.
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DR EMBL; LFIW01002029; KZL79687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167A3V6; -.
DR STRING; 1573173.A0A167A3V6; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF73; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..620
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007883447"
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..439
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 482..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 67102 MW; E91D3E342A1268DC CRC64;
MRASSLLAAT ACAAVASAQI RLPFARQAYP STDNVKPRAS GDRRSIPVLD ILANDWNYLV
NVSVGTPMQE MSMRLTVQAD SSWVPDAQYC GNHETYYVDS AMGKYHDEYA SCRYGAFNAS
KSTTYVNPGT ESFSEKYTND YVNGDWVSDT LEIAGTRLPK LVMGFVRSAD TFIGVLGLGF
NVSSYSSSSA SSSPSSSDAV PTVPERLFKD GLINSTAYSV WLDDKSAKSG NLLLGAIDKS
KFEGPLIRFP TSSSLRTSTS YGIKMFDTII SSVNGSKSAT NELQPLGRGL LSEEDYLSDS
DKTNIRLAPD FSFSVLPSAL ALDIWALAGA SWNNNLYYAI IPCAAAETST GHIVMQLHGT
EGPVLNVSIA DLVISKEAWS HSEWSWDTES SAEYCLFGIQ SDNSTSTSYE SSSRYSLGGA
MLKQAYMVFD LANAEIAIAQ ATFGNTVAED IVPFASYGAK TPESTRARPS YCSRPGYSSY
VECSDDDSGP GGKSSGDDFD DDNYGNDGYG DYYDGSYTPF LSQSTKIGIG LGVGLFCLLV
LCLTIWAVRR CRRIRKAEKD LSEKQADAEQ VAERTGTRNG NDVTQEGSMP QQPPAAVTRE
PLTMDTVEEQ HNTENTASTR
//