ID A0A068RRH5_9FUNG Unreviewed; 839 AA.
AC A0A068RRH5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:CDH52589.1};
GN ORFNames=LCOR_04046.1 {ECO:0000313|EMBL:CDH52589.1};
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:CDH52589.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH52589.1, 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 M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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:CDH52589.1}.
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DR EMBL; CBTN010000014; CDH52589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RRH5; -.
DR STRING; 1263082.A0A068RRH5; -.
DR VEuPathDB; FungiDB:LCOR_04046.1; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CDH52589.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CDH52589.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CDH52589.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..310
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 430..623
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 690..821
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 696..723
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 839 AA; 93509 MW; ADBCB35B0B71A106 CRC64;
MAPKYSAINH PPDNDNERHQ SHHHIDLPAL LNEAAETAHT IAKYAWLYKL LRFANEYTPL
LDRHGIPDRH AIKRLLTRVV SCCCFLFILI IVIVSLVVYF FVHRGNDAPH KQPLTDPEKL
VIEIPSSSFV KDFLHTYTAE PHLAGTDADR RYAEWTRDKM VEFGIEDTTI QSYYPLLTSP
VQQRLAIVSG PPEFIYEAKL KEDPIPEDTT SSHPNITSTF HAYSKNGTAT GRVVYANYGS
RQDFEYLLRR GVELRGTIAL MRSGGGVAAG IKVQGAERHG CVGALIYTDP ADDGAVDKQG
YPYTHPDKEY PDGPWRSANS VRRDSVEYIS MMAGDPSTPG WGATTEQGGN GKEQQQRLDR
DSSPCMSKIP SLPISYGDAL PLLRATQNIG VCDGEGWQGG LAQVVYCSGP SVGEAELINH
VEDKVTPIWN VIGRIPGEQE PDHAVILGTH RDAWVFGAAD ASSGSATMLE LARTLGILLS
KGWRPRRTII LASWDAHEYG MVGSTEWVED NQDWLTEQAV GYLNVGGVAG QYFAASAAPS
FHQLLYQVTS SIVTPGTEGT KTVYETWSEY TNSTEVESKP LPTIHNLGAG ADATAFFHHA
GITSVDLGMV GDYGVAHSAY DSFHWMEKFG DPTFEYHATF VKICGLLTVR LSDDRLLPMY
PQDYSFAIRQ YMDDLPLYET NGMLLGSIYK PLFKSVKKLK KKTRRFERRR ARLDERLKEF
DNNVKDAELP SVIAKRLAKT NKRIMYFERG FIQDDENNEM GRPWFKHVIY APSLDQGVSA
TTLPAMTEAL AESNNGDTEE GLVHAIQRTS RGLYAAIEAL KTDYDDDDDD DIDDDDNDD
//
