ID A0A068S7Q4_9FUNG Unreviewed; 410 AA.
AC A0A068S7Q4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=LCOR_09184.1 {ECO:0000313|EMBL:CDH58319.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH58319.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH58319.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH58319.1}.
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DR EMBL; CBTN010000055; CDH58319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S7Q4; -.
DR STRING; 1263082.A0A068S7Q4; -.
DR VEuPathDB; FungiDB:LCOR_09184.1; -.
DR OrthoDB; 1359987at2759; -.
DR Proteomes; UP000027586; 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; 1.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..335
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 410 AA; 46157 MW; 498159541219C1A8 CRC64;
MTNPVNASYE NAKTRSSWEG YATGQLIRLQ DKQHRVFARV DAITHNDQYL TSQCPQNHGH
WGLAYPALQT RPNDVYFNQD YQRTPSLQTL FDAMRQQLNI PNAFSYQLCP KHRVDVSAAK
GLQSVSKQQR HEGKSICQNR VGHFWLGGYN AEAMNKQVTW VPLISNQYHY ELHVDQFLVN
GKRVPMHDIN HPRTIIDTGT KDIVLSKQNL QNLLFSFKES GLVWFDPAFV SSEYEQAFWF
NRTRLTLPSK AVKLNDGSNV AISLSGQKID LHIENLLDVV LIDHDDETQP WINISLTGLS
SHNDDNQVAG TILGNTFMRG KTTIWDRDQG LIGFTSSGYD DDTCCQPGSA TDIKALLTAV
STAEQGKHEG HSHIQPLFVI LIACATLGAT THIALFVLQY CLSQQKRSTA
//
