ID A0A1C1D149_9EURO Unreviewed; 713 AA.
AC A0A1C1D149;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=N-acetylated-alpha-linked acidic dipeptidase 2 {ECO:0000313|EMBL:OCT54446.1};
GN Name=NAALAD2 {ECO:0000313|EMBL:OCT54446.1};
GN ORFNames=CLCR_00787 {ECO:0000313|EMBL:OCT54446.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT54446.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT54446.1}.
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DR EMBL; LGRB01000004; OCT54446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1D149; -.
DR STRING; 86049.A0A1C1D149; -.
DR VEuPathDB; FungiDB:CLCR_00787; -.
DR VEuPathDB; FungiDB:G647_01707; -.
DR eggNOG; KOG2195; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..713
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008651201"
FT DOMAIN 165..235
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 348..538
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 602..711
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 713 AA; 77602 MW; DCFD62762E439A30 CRC64;
MKVNKALPLL VLQATSVLAH TGEHFHPRVF DPRQALSKRQ EAPFPPILEP NEAILLNSFD
NATIEGWSYY YTHGLHLAGT NKSQAQWTAD RWSEFGFTSG LASYYVYLNY PVSHSLTATF
ANGSAYTPQL EEEVLAEDEV TSYPNRVPIF NGYSPSGNAS AEYVYVGRGQ KVDFERLRAL
GVPLEGKIAL SRYGGPFRGL KVKNAQDYGM IGVILFTDTA DDGNITEANG YAAYPHGPAR
NPTYVQRGSV EFVSTYSGDP DTPGYASKLD SPRADRSVVI PQIPSLPISW KTAQPLLQAL
DGHGVDGKTV NRTNWVGKLN ATYSTGPAPG VTISFSNVAR DEITWIWNSI GIINGTNQDE
VVILGNHRDA WIVGGGSDPN SGSAVLIELA KAFGALLKTG WKPKRTIILA SWDAEEYASV
GSTEWVEEYI PWLKDSAIAY LNVDQAVAGP DPALSATPEL HDVVAESLKK VVYPYHGYSN
LTLYDVWYGL SDGEFEVLGA GSDYVAFLHN GIASLDTGAG QGPNDPIYHY HSSYDTFHWM
KTFGDPYFTT HKAVGQHLAI LVYHLANDDI IPFNVENYGI HLTSYLNDLR DLVESENATS
AVDLSPLEDA IATFNASAAA ITAFIQTSTT EADFKIINSK LRDFSRGFVS QGGLPTREFY
KHVAFAPGLD TGYAPVTWPG VTEAVQDGNL TLASSWVLKS ARAVEVAAAI LAP
//