ID A0A197JR79_9FUNG Unreviewed; 545 AA.
AC A0A197JR79;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN ORFNames=K457DRAFT_139212 {ECO:0000313|EMBL:OAQ27787.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ27787.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ27787.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ27787.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; KV442054; OAQ27787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JR79; -.
DR STRING; 1314771.A0A197JR79; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..545
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008276180"
FT DOMAIN 229..526
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 545 AA; 62089 MW; 69E7C8FF31B99EE3 CRC64;
MKKFLSISVV LSFALLATQS APQVLSVTGD LTFTSEGGVS ESAQVVFGGR CQRESGPQRI
SHCDEDDIFG IKQVNYPREL KNHALVRFNA RKHHDITFPV PAGFALEDVS PLSSSTFQEQ
EEPMETMLQH LDVWSRSSAS DEVLAHFTAS QFERFERAMH LKGIPEGGDD WQVIERDLQR
VADEDAENIY MTSLRVRVEE EISLWKNKHH GNKDKKKSRV DFETWFKNYH RHDEIKDFYL
QIADDYPELV TYIPSIGQTV EGRDIFAIKL TAKEHDGSIK EKPQIWWQGL QHAREWAGGS
TVQFLTHHLT SNYGKNDNIT AILRDTEFVI VPIMNIDGYD YTWNNNRLWR KNRRQNGLGA
YGVDLNRNWD DHFAEGGSSG FPWSETYHGP SAASEPEVQA LQKFFSEQKR IVGAIDFHCY
SQLVLRPEGW TTKLSPHEKE HKFVGDRIVS IIKNVHGKTY ISEPSVALYK TTGAASDWFY
GDQATAANNG QHVYSYTIEL RPSDTNPGGR SGFILPPEEI IPLGEEIAQA MEFFVDYVVK
NPLKN
//
