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Conserved domains on  [gi|1711026063|gb|TVR78711|]
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M28 family peptidase [Saprospirales bacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 45-313 1.15e-111

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


The actual alignment was detected with superfamily member cd05663:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 266  Bit Score: 328.64  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  45 VEFLASDELKGRETGTEGEQRAAAYIADRLESLGLLPAGDHGTFYQQFEGTQLphpharpeegeviEGINVLGFIDNAAD 124
Cdd:cd05663     1 VGYLTSDELEGRLTGTKGEKLAADYIAQRFEELGLEPGLDNGTYFQPFEFTTG-------------TGRNVIGVLPGKGD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 125 H---TVVIGAHYDHIGLGVRGSLHTGDPA-IHPGADDNASGVALMLYLAERLRDVHTG----NNYLFIAFSGEEKGLWGS 196
Cdd:cd05663    68 VadeTVVVGAHYDHLGYGGEGSLARGDESlIHNGADDNASGVAAMLELAAKLVDSDTSlalsRNLVFIAFSGEELGLLGS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 197 GHWTKNPTVvEIENLNYMLNLDMVGRLNeDRTLMINGTGTSSVWERRLERANRA-NLNLRFTQSGVGGSDHTSFYLVEVP 275
Cdd:cd05663   148 KHFVKNPPF-PIKNTVYMINMDMVGRLR-DNKLIVQGTGTSPGWEQLVQARNKAtGFKLILDPTGYGPSDHTSFYLDDVP 225

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1711026063 276 AIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLI 313
Cdd:cd05663   226 VLHFFTGAHSDYHRPSDDSDKLNYDGMADIADFAVRII 263
cpPDZ_Deg_HtrA-like super family cl49614
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 335-420 2.16e-15

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


The actual alignment was detected with superfamily member cd06781:

Pssm-ID: 483954 [Multi-domain]  Cd Length: 98  Bit Score: 71.51  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 335 APRYSVSLGVIPDYLfsGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGEL 414
Cdd:cd06781    14 VPEYEQQSLKLPSNV--NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYRDGKE 91


                  ....*.
gi 1711026063 415 RTTTVK 420
Cdd:cd06781    92 KTLNIK 97
 
Name Accession Description Interval E-value
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 45-313 1.15e-111

M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 328.64  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  45 VEFLASDELKGRETGTEGEQRAAAYIADRLESLGLLPAGDHGTFYQQFEGTQLphpharpeegeviEGINVLGFIDNAAD 124
Cdd:cd05663     1 VGYLTSDELEGRLTGTKGEKLAADYIAQRFEELGLEPGLDNGTYFQPFEFTTG-------------TGRNVIGVLPGKGD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 125 H---TVVIGAHYDHIGLGVRGSLHTGDPA-IHPGADDNASGVALMLYLAERLRDVHTG----NNYLFIAFSGEEKGLWGS 196
Cdd:cd05663    68 VadeTVVVGAHYDHLGYGGEGSLARGDESlIHNGADDNASGVAAMLELAAKLVDSDTSlalsRNLVFIAFSGEELGLLGS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 197 GHWTKNPTVvEIENLNYMLNLDMVGRLNeDRTLMINGTGTSSVWERRLERANRA-NLNLRFTQSGVGGSDHTSFYLVEVP 275
Cdd:cd05663   148 KHFVKNPPF-PIKNTVYMINMDMVGRLR-DNKLIVQGTGTSPGWEQLVQARNKAtGFKLILDPTGYGPSDHTSFYLDDVP 225

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1711026063 276 AIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLI 313
Cdd:cd05663   226 VLHFFTGAHSDYHRPSDDSDKLNYDGMADIADFAVRII 263
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 94-323 1.41e-60

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 197.28  E-value: 1.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  94 GTQLPHPHARPEEGEVIEGINVLGFID--NAADHTVVIGAHYDHIGlgvrgslhtgdpAIHPGADDNASGVALMLYLAER 171
Cdd:COG2234    28 GLALLKLKGLLLEAAGGDSRNVIAEIPgtDPPDEVVVLGAHYDSVG------------SIGPGADDNASGVAALLELARA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 172 LRDVHTGNNY--LFIAFSGEEKGLWGSGHWTKNPTVvEIENLNYMLNLDMVGRLNEDRTLMINGTGTSSVWERRLERANR 249
Cdd:COG2234    96 LAALGPKPKRtiRFVAFGAEEQGLLGSRYYAENLKA-PLEKIVAVLNLDMIGRGGPRNYLYVDGDGGSPELADLLEAAAK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 250 A-----NLNLRFTQSGVGGSDHTSFYLVEVPAIHFFTGT---HEDYHRPSDTPDKINYQGMAEIGSFAFNLIGLLDWEDK 321
Cdd:COG2234   175 AylpglGVDPPEETGGYGRSDHAPFAKAGIPALFLFTGAedyHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELANADE 254


                  ..
gi 1711026063 322 LV 323
Cdd:COG2234   255 RW 256
Peptidase_M28 pfam04389
Peptidase family M28;
114-306 3.15e-38

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 136.65  E-value: 3.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 114 NVLGFID-NAADHTVVIGAHYDHIGLGvrgslhtgdpaihPGADDNASGVALMLYLAERLRDVHTGNNYL-FIAFSGEEK 191
Cdd:pfam04389   1 NVIAKLPgKAPDEVVLLSAHYDSVGTG-------------PGADDNASGVAALLELARVLAAGQRPKRSVrFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 192 GLWGSGHW-TKNPtvvEIENLNYMLNLDMVGRLNEDRtLMINGTGTSSVWERRLERANRAN-----LNLRFTQSGVGGSD 265
Cdd:pfam04389  68 GLLGSHHFaKSHP---PLKKIRAVINLDMIGSGGPAL-LFQSGPKGSSLLEKYLKAAAKPYgvtlaEDPFQERGGPGRSD 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1711026063 266 HTSFYLVEVPAIHF-FTGTHEDYHRPSDTPDKINYQGMAEIG 306
Cdd:pfam04389 144 HAPFIKAGIPGLDLaFTDFGYRYHTPADTIDNIDPGTLQRIG 185
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 335-420 2.16e-15

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 71.51  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 335 APRYSVSLGVIPDYLfsGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGEL 414
Cdd:cd06781    14 VPEYEQQSLKLPSNV--NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYRDGKE 91


                  ....*.
gi 1711026063 415 RTTTVK 420
Cdd:cd06781    92 KTLNIK 97
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 349-420 1.90e-11

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 64.01  E-value: 1.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1711026063 349 LFSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVK 420
Cdd:COG0265   197 LPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVT 268
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 55-218 4.16e-11

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 63.99  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  55 GRETGTEGEQRAAAYIADRLESLG------------LLPAGDHGTFYQQFEGTQLPHPHarpeEGEVIEGINVLGFIDNA 122
Cdd:PRK10199   46 GRMTGSPAEMLSADYLRQQFQQMGyqsdirtfnsryIYTARDNRKNWHNVTGSTVIAAH----EGKAPQQIIIMAHLDTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 123 ADHTvviGAHYDHI--GLGVRGslhtgdpaihpgADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGLWGSGHWT 200
Cdd:PRK10199  122 APQS---DADVDANlgGLTLQG------------MDDNAAGLGVMLELAERLKNVPTEYGIRFVATSGEEEGKLGAENLL 186

                         170
                  ....*....|....*...
gi 1711026063 201 KNPTVVEIENLNYMLNLD 218
Cdd:PRK10199  187 KRMSDTEKKNTLLVINLD 204
PDZ_2 pfam13180
PDZ domain;
353-421 4.12e-10

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 55.74  E-value: 4.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1711026063 353 GGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVKF 421
Cdd:pfam13180   6 GGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 357-421 3.34e-06

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 49.14  E-value: 3.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1711026063 357 IEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVKF 421
Cdd:TIGR02037 261 VAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTL 325
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 337-391 1.27e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 37.74  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1711026063  337 RYSVSLGV-IPDYLFSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDY 391
Cdd:smart00228   9 KGGGGLGFsLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHL 64
 
Name Accession Description Interval E-value
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 45-313 1.15e-111

M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 328.64  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  45 VEFLASDELKGRETGTEGEQRAAAYIADRLESLGLLPAGDHGTFYQQFEGTQLphpharpeegeviEGINVLGFIDNAAD 124
Cdd:cd05663     1 VGYLTSDELEGRLTGTKGEKLAADYIAQRFEELGLEPGLDNGTYFQPFEFTTG-------------TGRNVIGVLPGKGD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 125 H---TVVIGAHYDHIGLGVRGSLHTGDPA-IHPGADDNASGVALMLYLAERLRDVHTG----NNYLFIAFSGEEKGLWGS 196
Cdd:cd05663    68 VadeTVVVGAHYDHLGYGGEGSLARGDESlIHNGADDNASGVAAMLELAAKLVDSDTSlalsRNLVFIAFSGEELGLLGS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 197 GHWTKNPTVvEIENLNYMLNLDMVGRLNeDRTLMINGTGTSSVWERRLERANRA-NLNLRFTQSGVGGSDHTSFYLVEVP 275
Cdd:cd05663   148 KHFVKNPPF-PIKNTVYMINMDMVGRLR-DNKLIVQGTGTSPGWEQLVQARNKAtGFKLILDPTGYGPSDHTSFYLDDVP 225

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1711026063 276 AIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLI 313
Cdd:cd05663   226 VLHFFTGAHSDYHRPSDDSDKLNYDGMADIADFAVRII 263
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 112-313 3.56e-69

M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349874 [Multi-domain]  Cd Length: 206  Bit Score: 217.50  E-value: 3.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 112 GINVLGFIDNA--ADHTVVIGAHYDHIGLGVRGSlhtgDPAIHPGADDNASGVALMLYLAERLRDVHTGN-NYLFIAFSG 188
Cdd:cd03877     1 GHNVVGVLEGSdlPDETIVIGAHYDHLGIGGGDS----GDKIYNGADDNASGVAAVLELARYFAKQKTPKrSIVFAAFTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 189 EEKGLWGSGHWTKNPTVvEIENLNYMLNLDMVGRLNEDRTLMINGTGTSSvWERRLERANRAN----LNLRFTQSGVGGS 264
Cdd:cd03877    77 EEKGLLGSKYFAENPKF-PLDKIVAMLNLDMIGRLGRSKDVYLIGSGSSE-LENLLKKANKAAgrvlSKDPLPEWGFFRS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1711026063 265 DHTSFYLVEVPAIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLI 313
Cdd:cd03877   155 DHYPFAKAGVPALYFFTGLHDDYHKPSDDYEKIDYEGMARVVNLIYQLL 203
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 94-323 1.41e-60

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 197.28  E-value: 1.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  94 GTQLPHPHARPEEGEVIEGINVLGFID--NAADHTVVIGAHYDHIGlgvrgslhtgdpAIHPGADDNASGVALMLYLAER 171
Cdd:COG2234    28 GLALLKLKGLLLEAAGGDSRNVIAEIPgtDPPDEVVVLGAHYDSVG------------SIGPGADDNASGVAALLELARA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 172 LRDVHTGNNY--LFIAFSGEEKGLWGSGHWTKNPTVvEIENLNYMLNLDMVGRLNEDRTLMINGTGTSSVWERRLERANR 249
Cdd:COG2234    96 LAALGPKPKRtiRFVAFGAEEQGLLGSRYYAENLKA-PLEKIVAVLNLDMIGRGGPRNYLYVDGDGGSPELADLLEAAAK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 250 A-----NLNLRFTQSGVGGSDHTSFYLVEVPAIHFFTGT---HEDYHRPSDTPDKINYQGMAEIGSFAFNLIGLLDWEDK 321
Cdd:COG2234   175 AylpglGVDPPEETGGYGRSDHAPFAKAGIPALFLFTGAedyHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELANADE 254


                  ..
gi 1711026063 322 LV 323
Cdd:COG2234   255 RW 256
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 45-305 1.70e-60

M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 198.35  E-value: 1.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  45 VEFLASDELKGRETGTEGEQRAAAYIADRLESLGLLPAGDHGTFYQqfegtqlPHPHARPEegEVIEGINVLGFIDNA-- 122
Cdd:cd05660     1 VKFLASDEFEGRAPGSEGEKKTVDYLAEQFKELGLKPAGSDGSYLQ-------AVPLVSKI--EYSTSHNVVAILPGSkl 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 123 ADHTVVIGAHYDHIGLGVrgslHTGDPAIHPGADDNASGVALMLYLAERLRDVHTG--NNYLFIAFSGEEKGLWGSGHWT 200
Cdd:cd05660    72 PDEYIVLSAHWDHLGIGP----PIGGDEIYNGAVDNASGVAAVLELARVFAAQDQRpkRSIVFLAVTAEEKGLLGSRYYA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 201 KNPTvVEIENLNYMLNLDMVGRLNEDRTLMINGTGTSSVwERRLERANRA-NLNLRFTQSGVGG----SDHTSFYLVEVP 275
Cdd:cd05660   148 ANPI-FPLDKIVANLNIDMIGRIGPTKDVLLIGSGSSEL-ENILKEAAKAvGRVVDYDPNPENGsfyrSDHYNFAKKGVP 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1711026063 276 AIHFFTG--------------THEDYHRPSDT-PDKINYQGMAEI 305
Cdd:cd05660   226 VLFFFGGydlgdggkklakayLHTDYHKPADDvTEKWDYEGAAED 270
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 43-317 3.69e-55

M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain.


Pssm-ID: 349912 [Multi-domain]  Cd Length: 268  Bit Score: 183.44  E-value: 3.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  43 ADVEFLASDELKGRETGTEGEQRAAAYIADRLESLGLLPAGDhgtfyqQFEgtqlpHPHARPEEGEVIEGINVLGFI--D 120
Cdd:cd05662     4 ADVKILSSDKFEGRKTGTKGAAKTRAYIIERFKQIGLLPWGD------RFE-----HPFSYTKRFSTRQGVNVLAVIkgS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 121 NAADHTVVIGAHYDHigLGVRGSlhtgdpAIHPGADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGLWGSGHWT 200
Cdd:cd05662    73 EPPTKWRVVSAHYDH--LGIRGG------KIYNGADDNASGVAALLALAEYFKKHPPKHNVIFAATDAEEPGLRGSYAFV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 201 KNPTVVEiENLNYMLNLDMVGRlNEDRTLMINGTGTSSVWERRLER----ANRANLNLRFTQSG-----VGGSDHTSFYL 271
Cdd:cd05662   145 EALKVPR-AQIELNINLDMISR-PERNELYVEGASQFPQLTSILENvkgtCIKALHPKDTDGSIgsidwTRASDHYPFHK 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1711026063 272 VEVPAIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLIGLLD 317
Cdd:cd05662   223 AKIPWLYFGVEDHPDYHKPTDDFETIDQEFFAAVVESAVQLFKIDD 268
Peptidase_M28 pfam04389
Peptidase family M28;
114-306 3.15e-38

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 136.65  E-value: 3.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 114 NVLGFID-NAADHTVVIGAHYDHIGLGvrgslhtgdpaihPGADDNASGVALMLYLAERLRDVHTGNNYL-FIAFSGEEK 191
Cdd:pfam04389   1 NVIAKLPgKAPDEVVLLSAHYDSVGTG-------------PGADDNASGVAALLELARVLAAGQRPKRSVrFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 192 GLWGSGHW-TKNPtvvEIENLNYMLNLDMVGRLNEDRtLMINGTGTSSVWERRLERANRAN-----LNLRFTQSGVGGSD 265
Cdd:pfam04389  68 GLLGSHHFaKSHP---PLKKIRAVINLDMIGSGGPAL-LFQSGPKGSSLLEKYLKAAAKPYgvtlaEDPFQERGGPGRSD 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1711026063 266 HTSFYLVEVPAIHF-FTGTHEDYHRPSDTPDKINYQGMAEIG 306
Cdd:pfam04389 144 HAPFIKAGIPGLDLaFTDFGYRYHTPADTIDNIDPGTLQRIG 185
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 114-298 2.51e-26

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 105.12  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 114 NVLGFI--DNAADHTVVIGAHYDHIGLGvrgslhtgdpaihPGADDNASGVALMLYLAERLRDVHTGNN--YLFIAFSGE 189
Cdd:cd02690     3 NVIATIkgSDKPDEVILIGAHYDSVPLS-------------PGANDNASGVAVLLELARVLSKLQLKPKrsIRFAFWDAE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 190 EKGLWGSGHWTKNPTvVEIENLNYMLNLDMVGRLNeDRTLMINGTGTSSVWERRL-----ERANRANLNLRFTQSGVGGS 264
Cdd:cd02690    70 ELGLLGSKYYAEQLL-SSLKNIRAALNLDMIGGAG-PDLYLQTAPGNDALVEKLLralahELENVVYTVVYKEDGGTGGS 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1711026063 265 DHTSFYLVEVPAIHFFTGTHED---YHRPSDTPDKIN 298
Cdd:cd02690   148 DHRPFLARGIPAASLIQSESYNfpyYHTTQDTLENID 184
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 45-305 3.25e-26

M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349911 [Multi-domain]  Cd Length: 262  Bit Score: 106.50  E-value: 3.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  45 VEFLASDElkgRETGTEGEQRAAAYIADRLESLGLlpagdhGTFYQQF-----EGTQLPhpharpeegevieginvlgfi 119
Cdd:cd05661    20 IRFLSQAI---GVAGTPEELKAARYIEQQLKSLGY------EVEVQPFtshnvIATKKP--------------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 120 DNAADHT--VVIGAHYDhiglGVRGSlhtgdpaihPGADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGLWGSG 197
Cdd:cd05661    70 DNNKNNNdiIIVTSHYD----SVVKA---------PGANDNASGTAVTLELARVFKKVKTDKELRFIAFGAEENGLLGSK 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 198 HWTKNPTVVEIENLNYMLNLDMVG----RLNEDRTLMINGTgTSSVWERRLERANRANLNLRFTQSgvGGSDHTSFYLVE 273
Cdd:cd05661   137 YYVASLSEDEIKRTIGVFNLDMVGtsdaKAGDLYAYTIDGK-PNLVTDSGAAASKRLSGVLPLVQQ--GSSDHVPFHEAG 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1711026063 274 VPAIHFFTGTHED------YHRPSDTPDKIN---YQGMAEI 305
Cdd:cd05661   214 IPAALFIHMDPETepvepwYHTPNDTVENISkerLDNALDI 254
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 65-305 9.34e-20

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 88.66  E-value: 9.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  65 RAAAYIADRLESLGllpagdhgtfyQQFEgtqlphPHARPEEGEVieGINVLGFIDNAA--DHTVVIGAHYDhiglGVRG 142
Cdd:cd05640    24 AAAEYIAQELVGSG-----------YNVT------SHFFSHQEGV--YANLIADLPGSYsqDKLILIGAHYD----TVPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 143 SlhtgdpaihPGADDNASGVALMLYLAeRLRDVHTGNNYL-FIAFSGEEK-----GLWGSGHWTKNPTvVEIENLNYMLN 216
Cdd:cd05640    81 S---------PGADDNASGVAALLELA-RLLATLDPNHTLrFVAFDLEEYpffarGLMGSHAYAEDLL-RPLTPIVGMLS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 217 LDMVGRLNEDR-------TLM----------INGTGTSSVWE--RRLERANRAN-------LNLRFTQSGVGG---SDHT 267
Cdd:cd05640   150 LEMIGYYDPFPhsqaypaGFElhfyphmgdfIAVVGRLRSRKlvRAFKRAFRMLsdfpvesLNLPFNGPGVPPfrrSDHS 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1711026063 268 SFYLVEVPAI-----HFFTGTHedYHRPSDTPDKINYQGMAEI 305
Cdd:cd05640   230 SFWDHGYPAImvtdtAFYRNPQ--YHLPCDTPDTLNYKFLTRV 270
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 335-420 2.16e-15

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 71.51  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 335 APRYSVSLGVIPDYLfsGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGEL 414
Cdd:cd06781    14 VPEYEQQSLKLPSNV--NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYRDGKE 91


                  ....*.
gi 1711026063 415 RTTTVK 420
Cdd:cd06781    92 KTLNIK 97
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 56-298 3.27e-14

M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.


Pssm-ID: 349873 [Multi-domain]  Cd Length: 289  Bit Score: 72.71  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  56 RETGTEGEQRAAAYIADRLESlgllpAGDHGTFYQQFEGTqlphpharpeegeVIEGINVLgfidnA------ADHTVVI 129
Cdd:cd03876    25 RAFGSPGYNASVDYVKNELKA-----AGYYDVTLQPFTSL-------------YRTTYNVI-----AetkggdPNNVVML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 130 GAHYDHIGLGvrgslhtgdpaihPGADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGLWGSGHWTKNPTVVEIE 209
Cdd:cd03876    82 GAHLDSVSAG-------------PGINDNGSGSAALLEVALALAKFKVKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 210 NLNYMLNLDMVGRLN--------EDRTLMINGTGTSSVWERRLERANRAnLNLRFTQS-GVGGSDHTSFYLVEVPAIHFF 280
Cdd:cd03876   149 KIRLYLNFDMIASPNygyfiydgDGSAFNLTGPPGSAEIERLFEAYFTS-LGLPSTPTeFDGRSDYAPFIEAGIPAGGLF 227

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1711026063 281 TGTHE--------------------DYHRPSDTPDKIN 298
Cdd:cd03876   228 TGAEGikteeqaalwggtagvaydpCYHQACDTIDNIN 265
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 56-321 1.62e-12

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.


Pssm-ID: 349895 [Multi-domain]  Cd Length: 290  Bit Score: 67.43  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  56 RETGTEGEQRAAAYIADRLESLGLL------PAGDHGTFYQQFEGtqlphPHARPEEGEVIEGINVLGF-IDNAADHTVV 128
Cdd:cd05643    13 RVQGSRGYVKAAEEVKELLEELGLEaklisdIYDGGERILTPQSP-----ISWELIEGELNETLPILYAiIGKETPPEIA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 129 IGAHYDHiglgvrgslhtgdPaiHPGADDNASGVALMLYLAERLRDVHTGNNYLFIAFsgeekgLW-----GSGHW-TKN 202
Cdd:cd05643    88 FVAHLCH-------------P--KPGANDNASGSALLLEVARVLAKLILNRPKRGICF------LWvpeytGTAAYfAQH 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 203 PtvVEIENLNYMLNLDMVGrLNEDRT---LMINGT--------------GTSSVWERRLErANRANLNlRFTqsgvGGSD 265
Cdd:cd05643   147 P--DRLKKIIAVINLDMVG-EDQTKTgstLMLVPTplsfpsylneelaqKLSNFTGSSLP-AVRYGKE-PYE----GGSD 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1711026063 266 HTSFYLVEVPAIHFFTGTHEDYHRPSDTPDKINYQGMAEIGSFAFNLIGLLDWEDK 321
Cdd:cd05643   218 HDVFSDPGIPAVMFNTWPDRYYHTSDDTPDKLDPETLKNVGAAVLLTAYALANGEE 273
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 114-311 2.90e-12

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349894 [Multi-domain]  Cd Length: 347  Bit Score: 67.52  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 114 NVLGFIDNAAD--HTVVIGAHYDHIGLGVRGSlhTGDPaihPGADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEK 191
Cdd:cd05642    90 NVVATLKGSEDpdRVYVVSGHYDSRVSDVMDY--ESDA---PGANDDASGVAVSMELARIFAKHRPKATIVFTAVAGEEQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 192 GLWGS---GHWTKNPTVveieNLNYMLNLDMVGRLNEDRTLMINGT------GTSSVwERRLERANRANL---------N 253
Cdd:cd05642   165 GLYGStflAQTYRNNSV----NVEGMLNNDIVGSSTGDDGTKDPHTirlfaqGTPAV-ESSEQAESRLSIggendsparN 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 254 L-RFTqSGVG--------------------GSDHTSFYLVEVPAIHfFTGTHEDY---HRPSDTPDKINYQGMAEIGSFA 309
Cdd:cd05642   240 LgRFI-AEVAsnaftdmkvaliyrldrylrGGDHRPFLEAGYPAVR-FTEPNENYahqHQDVRTEDGTVYGDLIEFVDFD 317


                  ..
gi 1711026063 310 FN 311
Cdd:cd05642   318 YI 319
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 120-296 1.45e-11

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 64.57  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 120 DNAADHTVVIGAHYDHIGLGVRGSLhtgdPAihPGADDNASGVALMLylaERLRdVHTGNNYL------FIAFSGEEKGL 193
Cdd:cd03879    84 SEKSDEIVVIGAHQDSINGSNPSNG----RA--PGADDDGSGTVTIL---EALR-VLLESGFQpkntieFHWYAAEEGGL 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 194 WGSGhwtknpTVV-----EIENLNYMLNLDMVG--RLNEDRTLMINGTGTSSVWERRLERANRANLNL--RFTQSGVGGS 264
Cdd:cd03879   154 LGSQ------AIAtqyksEGKNVKAMLQLDMTGyvKPGSAEDIGLITDYTDSNLTQFLKQLIDEYLPIpyGDTKCGYACS 227

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1711026063 265 DHTSFYLVEVPAIHFFTGTHEDY----HRPSDTPDK 296
Cdd:cd03879   228 DHASWTKAGYPAAFPFESAFEDYnpyiHTTNDTLDN 263
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 349-420 1.90e-11

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 64.01  E-value: 1.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1711026063 349 LFSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVK 420
Cdd:COG0265   197 LPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVT 268
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 55-218 4.16e-11

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 63.99  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  55 GRETGTEGEQRAAAYIADRLESLG------------LLPAGDHGTFYQQFEGTQLPHPHarpeEGEVIEGINVLGFIDNA 122
Cdd:PRK10199   46 GRMTGSPAEMLSADYLRQQFQQMGyqsdirtfnsryIYTARDNRKNWHNVTGSTVIAAH----EGKAPQQIIIMAHLDTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 123 ADHTvviGAHYDHI--GLGVRGslhtgdpaihpgADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGLWGSGHWT 200
Cdd:PRK10199  122 APQS---DADVDANlgGLTLQG------------MDDNAAGLGVMLELAERLKNVPTEYGIRFVATSGEEEGKLGAENLL 186

                         170
                  ....*....|....*...
gi 1711026063 201 KNPTVVEIENLNYMLNLD 218
Cdd:PRK10199  187 KRMSDTEKKNTLLVINLD 204
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
333-420 3.82e-10

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 61.76  E-value: 3.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 333 RSAPRYSVSLGVipDYLFSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIeTIYDYMEALSDYISGDETEVGFKRDG 412
Cdd:COG3975   476 EDAPSLKPSLGL--RVSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRV-TADNLDDALAAYKPGDPIELLVFRRD 552


                  ....*...
gi 1711026063 413 ELRTTTVK 420
Cdd:COG3975   553 ELRTVTVT 560
PDZ_2 pfam13180
PDZ domain;
353-421 4.12e-10

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 55.74  E-value: 4.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1711026063 353 GGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVKF 421
Cdd:pfam13180   6 GGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 356-420 4.14e-09

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 52.96  E-value: 4.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1711026063 356 KIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDyISGDETEVGFKRDGELRTTTVK 420
Cdd:cd23081     2 VVGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRE-NPGKPLTLKIERDGKILTVTVT 65
M28_nicalin_like cd03882
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ...
 126-226 4.93e-09

M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development.


Pssm-ID: 349878  Cd Length: 296  Bit Score: 56.99  E-value: 4.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 126 TVVIGAHYDHIGLGvrgslhtgdPAIHPGADDNASGVALMLYLAERLRDVHTGN------NYLFIAFSGEEKGLWGSGHW 199
Cdd:cd03882    91 TIVIVAHYDTFGVA---------PWLSSGADSNGSGVAALLELMRLFSRLYSNPrtrakyNLLFLLTGGGKLNYQGTKHW 161

                          90       100
                  ....*....|....*....|....*..
gi 1711026063 200 TKNPTVVEIENLNYMLNLDMVGRLNED 226
Cdd:cd03882   162 LESNLDHFLDNVEFVLCLDSIGSKDSD 188
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 32-278 8.13e-09

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 57.20  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  32 TEPLSPVEQFRAD-VEFLAsdELKGRETGTEGEQRAAAYIADRLESLGllpagdhgtfyqqFEGTQLPHPHARPeegevi 110
Cdd:COG0624     1 AAVLAAIDAHLDEaLELLR--ELVRIPSVSGEEAAAAELLAELLEALG-------------FEVERLEVPPGRP------ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 111 egiNVLGFID-NAADHTVVIGAHYDHIGLGvRGSLHTGDP--------AIH-PGADDNASGVALMLYLAERLRDVHTG-- 178
Cdd:COG0624    60 ---NLVARRPgDGGGPTLLLYGHLDVVPPG-DLELWTSDPfeptiedgRLYgRGAADMKGGLAAMLAALRALLAAGLRlp 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 179 NNYLFIAFSGEEKGLWGSGHWtknptvveIENLNYMLNLDMVgrlnedrtlmINGTGTSSVwerRLERANRANLNLRFTQ 258
Cdd:COG0624   136 GNVTLLFTGDEEVGSPGARAL--------VEELAEGLKADAA----------IVGEPTGVP---TIVTGHKGSLRFELTV 194

                         250       260
                  ....*....|....*....|
gi 1711026063 259 SGVGGsdHTSFYLVEVPAIH 278
Cdd:COG0624   195 RGKAA--HSSRPELGVNAIE 212
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 356-420 1.68e-08

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 55.86  E-value: 1.68e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1711026063 356 KIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYiSGDETEVGFKRDGELRTTTVK 420
Cdd:COG0750   131 VVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRAS-PGKPLTLTVERDGEELTLTVT 194
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 112-310 3.16e-08

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349937 [Multi-domain]  Cd Length: 218  Bit Score: 53.75  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 112 GINVLGFIDNA--ADHTVVIGAHYDhiglgvrgSLHTGDpaihpGADDNASGVALMLYLAERLRDVHTG--NNYLFIAFS 187
Cdd:cd08015     1 TYNVIAEIPGSdkKDEVVILGAHLD--------SWHGAT-----GATDNGAGTAVMMEAMRILKAIGSKpkRTIRVALWG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 188 GEEKGLWGS--------GHWTKNPTVVEIENLNYMLNLDM-VGRLnedRTLMING-TGTSSVWERRLERANRANLNlRFT 257
Cdd:cd08015    68 SEEQGLHGSrayvekhfGDPPTMQLQRDHKKISAYFNLDNgTGRI---RGIYLQGnLAAYPIFSAWLYPFHDLGAT-TVI 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1711026063 258 QSGVGGSDHTSFYLVEVPAIHF-------FTGTHedyHRPSDTPDKINY----QGMAEIGSFAF 310
Cdd:cd08015   144 ERNTGGTDHAAFDAVGIPAFQFiqdpwdyWTRTH---HTNRDTYDRLIPedlkQAAIITASFAY 204
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 351-419 6.92e-08

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 49.98  E-value: 6.92e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1711026063 351 SGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd06779    23 VNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTILRDGKTLTVTV 91
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 56-306 3.82e-07

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349943 [Multi-domain]  Cd Length: 287  Bit Score: 51.37  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  56 RETGTEGEQRAAAYIADRLESLGllpagdhGTFYQQfegtqlpHPHARPEEGEVIEGINVLGFIDNAADHTVVIGAHYDh 135
Cdd:cd08656    17 RVPNTAAHKACGEYLAGKLEAFG-------AKVYNQ-------YADLIAYDGTILKARNIIGAYNPESKKRVLLCAHWD- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 136 iglgVRG-SLHTGDPAIHP----GADDNASGVALMLYLAERLRDVHTGNNYLFIAFSGEEKGL------------W--GS 196
Cdd:cd08656    82 ----SRPyADNDADPKKHHtpilGANDGASGVGALLEIARQIQQQAPAIGIDIIFFDAEDYGTpefyegkyksdtWclGS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 197 GHWTKNPtVVEIENLNYMLNLDMVGRLN-----EDRTLMINGTGTSSVWerrlERANRANLNLRFTQSGVGG--SDHTSF 269
Cdd:cd08656   158 QYWARNP-HVQGYNARYGILLD*VGGKNatflkEQYSLRTARDIVKKIW----KTAKRLGYGKYFVPEAGGTitDDHLYV 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1711026063 270 Y-LVEVPAIHFF-------TGTHEDYHRPSDTPDKINYQGMAEIG 306
Cdd:cd08656   233 NqLARIPTIDIInydperpTGFPSYWHTIQDN*ENIDKETLKAVG 277
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
354-420 7.07e-07

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 50.96  E-value: 7.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1711026063 354 GLKIEGVTSGRPAEnaGLIR-GDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVK 420
Cdd:COG3480   139 GVYVASVLEGSPAD--GVLQpGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVT 204
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 39-218 1.50e-06

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 49.51  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  39 EQFRADVEFLASdeLKGRETGTEGEQRAAAYIADRLESLGLLPAGDHGTFY-QQFEGTQLPHPHARPEEGEVIEGINVLG 117
Cdd:cd03875     7 ERAWEDLQVLIS--IGPHPYGSHNNDKVRDYLLARVEEIKERANANGLEVEvQDDTGSGSFNFLSSGMTLVYFEVTNIVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 118 FI---DNAADHTVVIGAHYDhiglgvrgSLHTGdpaihPGADDNASGVALMLYLAERLRDVHTGNNYLFIA-FSG-EEKG 192
Cdd:cd03875    85 RIsgkNSNSLPALLLNAHFD--------SVPTS-----PGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFlFNGaEENG 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1711026063 193 LWGS-----GHWTKNptvveieNLNYMLNLD 218
Cdd:cd03875   152 LLGAhafitQHPWAK-------NVRAFINLE 175
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 353-419 1.58e-06

circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Escherichia coli DegS and related domains. DegS (also known as Site-1 protease DegS, S1P protease DegS, and Site-1-type intramembrane protease) participates in the activation of the sigma(E) extracytoplasmic stress response. Initially, there is an accumulation of misfolded membrane proteins (OMPs) in the periplasm which bind by their YXF motif to the DegS PDZ domain, activating DegS-catalyzed cleavage of the RseA periplasmic domain and making RseA a substrate for cleavage by another membrane protease RseP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegS family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467620 [Multi-domain]  Cd Length: 93  Bit Score: 46.23  E-value: 1.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1711026063 353 GGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd06777    25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEIRPGTVIPVVVLRDGKQLTLEV 91
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 357-421 3.34e-06

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 49.14  E-value: 3.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1711026063 357 IEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVKF 421
Cdd:TIGR02037 261 VAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTL 325
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 360-419 8.19e-06

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 44.01  E-value: 8.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 360 VTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd10839    32 VLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKILRDGKEKTLTV 91
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 313-419 1.16e-05

circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana putative protease DEGP14 and related domains. DEGP14 is a putative protease belonging to the HtrA family of housekeeping proteases. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP14-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467632 [Multi-domain]  Cd Length: 101  Bit Score: 43.99  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 313 IGLLDWE-DKLVFSEtVQEESRSAPRysVSLGVIpdylfsggglkIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDY 391
Cdd:cd23085     4 LGMKMLElNEHIIAQ-LKERDPMFPD--VKAGVL-----------VPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQI 69

                          90       100
                  ....*....|....*....|....*...
gi 1711026063 392 MEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd23085    70 IDALGDKVGKPFKVVVKRANKVQVTLTV 97
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 41-199 1.65e-05

M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor (TfR) and prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase or GCP-II) subfamily. TfR and PSMA are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. While related in sequence to peptidase M28 GCP-II, TfR lacks the metal ion coordination centers and protease activity.


Pssm-ID: 349871 [Multi-domain]  Cd Length: 278  Bit Score: 46.14  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  41 FRADVEFLASdelKGRETGTEGEQRAAAYIADRLESLGLLpagdhgtfyqqfegtqlphphaRPEEGEVIEGINVLGFID 120
Cdd:cd03874    11 IKEDLEYLSS---MPHMAGTKGDAALAKYIENSFKNNGLF----------------------EVELEEYSPITNVVGKIE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 121 NA--ADHTVVIGAHYDhiglgvrgslhtgdpAIHPGADDNASGVALMLYLAERLRDV--HTG----NNYLFIAFSGEEKG 192
Cdd:cd03874    66 GIeqPDRAIIIGAHRD---------------SWGYGAGYPNSGTAVLLEIARLFQQLkkKFGwkplRTIYFISWDGSEFG 130


                  ....*..
gi 1711026063 193 LWGSGHW 199
Cdd:cd03874   131 LAGSTEL 137
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 352-419 2.07e-05

circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana DEGP1 (also known as protease Do-like 1, chloroplastic, protein DEGRADATION OF PERIPLASMIC PROTEINS 1, DEGP PROTEASE 1 and DEG1), and related domains. DEGP1 is a serine protease that is required at high temperature and may be involved in the degradation of damaged proteins. This family also includes Arabidopsis protease DEGP8/Do-like 8 (chloroplastic), a probable serine protease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467618 [Multi-domain]  Cd Length: 102  Bit Score: 42.95  E-value: 2.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1711026063 352 GGGLKIEGVTSGRPAENAGLI---R--------GDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd00990    22 RSGVLVLDVPPGGPAAKAGLRgtkRdefgrivlGDVIVAVDGKPVKNESDLYRALDEYKVGDVVTLKVLRGGTKVDLKV 100
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 126-296 2.77e-05

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 44.72  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 126 TVVIGAHYDHIGLGVRGSLHT--------GDPAIHPGADDNASGVALMLYLAERLRDVHTGNNY--LFIAFSGEEKGlWG 195
Cdd:cd03873    14 SVALGAHLDVVPAGEGDNRDPpfaedteeEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGtiVVAFTADEEVG-SG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 196 SGHWTKNPTVVEIE-NLNYMLNLDMVGRLNEDRtlminGTGTSSVWERRLERANRANL-NLRFTQSGVGGSDHTSFYLVE 273
Cdd:cd03873    93 GGKGLLSKFLLAEDlKVDAAFVIDATAGPILQK-----GVVIRNPLVDALRKAAREVGgKPQRASVIGGGTDGRLFAELG 167

                         170       180
                  ....*....|....*....|...
gi 1711026063 274 VPAIHFFTGTHEDYHRPSDTPDK 296
Cdd:cd03873   168 IPGVTLGPPGDKGAHSPNEFLNL 190
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 350-419 3.81e-05

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 45.68  E-value: 3.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 350 FSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:TIGR02037 359 GDVKGVVVTKVVSGSPAARAGLQPGDVILSVNQQPVSSVAELRKVLARAKKGGRVALLILRGGATIFVTL 428
Peptidase_M50 pfam02163
Peptidase family M50;
356-419 6.06e-05

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 44.41  E-value: 6.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1711026063 356 KIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYIsGDETEVGFKRDGELRTTTV 419
Cdd:pfam02163  96 VIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKSP-GKPITLTVERGGQTLTVTI 158
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 354-420 7.14e-05

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 41.54  E-value: 7.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1711026063 354 GLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTVK 420
Cdd:cd10838    34 GVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAVK 100
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 352-420 1.41e-04

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 43.71  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1711026063 352 GGGLKIEGVTSGRPAENAGLIRGDIIIK-----MGEKEIETIYDYMEALsdyiSGDETEVGFKRDGELRTTTVK 420
Cdd:COG0793    70 DGKVVVVSVIPGSPAEKAGIKPGDIILAidgksVAGLTLDDAVKLLRGK----AGTKVTLTIKRPGEGEPITVT 139
M28_Nicastrin cd03881
M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, ...
 149-299 1.46e-04

M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, nicastrin subfamily. Nicastrin is a main component of the gamma-secretase complex, which also contains presenilin, Pen-2 and Aph-1. Its extracellular domain sequence resembles aminopeptidases, but certain catalytic residues are not conserved. It is mainly localized to the endoplasmic reticulum and Golgi. It is highly glycosylated (Mr 120 kDa) and is essential for substrate recognition of the N-terminus of gamma-secretase substrates derived from APP and Notch. Nicastrin facilitates substrate cleavage by the catalytic presenilin subunit in the gamma-secretase complex. One conserved glutamate is especially important, probably because this residue forms an ion pair with the amino terminus of the substrate. This substrate-binding domain is often called the DAP domain (named after DYIGS, the amino acid stretch that modulates amyloid precursor protein (APP) processing, and Peptidase homologous region). The sequence of the substrate N-terminus is apparently not critical for the interaction, but a free amino group is. Thus, nicastrin can be considered a kind of gatekeeper for the gamma-secretase complex: type I membrane proteins that have not shed their ectodomains cannot interact properly with nicastrin and do not gain access to the active site. Dysfunction of gamma-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).


Pssm-ID: 349877 [Multi-domain]  Cd Length: 519  Bit Score: 43.95  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 149 PAIHPGADDNASGVALMLYLAERLRDV----HTGNNYLFIAFSGEEKGLWGSG--------------HWTKNPTVVEI-- 208
Cdd:cd03881   226 RDVAPGADSSLSGFVALLAAAEALKKVdgkgSLKRNVVFAFFNGESWGYIGSSrfvydmengkfptyGSKDDLFFFPIsf 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 209 ENLNYMLNLDMVGRLnEDRTLMI---NGTGTSSVWERRLERANRANLNLRFT-------QSGVGGSDHTSFyLVEVPAI- 277
Cdd:cd03881   306 ENIDTILEVGQVGLA-LGAKLYAhtdGVSTNSSVTQQLLDALSNSLKSLAFTilsapasSPGLPPSSLMSF-LRADPNIp 383

                         170       180
                  ....*....|....*....|....*...
gi 1711026063 278 ------HFFTGTHEDYHRPSDTPDKINY 299
Cdd:cd03881   384 gvvltdHDKAFTNKYYHSIYDDAENVNV 411
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 351-419 1.91e-04

circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease MamE and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Magnetospirillum magneticum MamE (also known as magnetochrome MamE and magnetosome serine protease MamE), and related domains. MamE is a serine protease required to produce magnetite crystals in the magnetotactic bacterium M. magneticum. It is involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome, and likely cleaves at least itself, MamO and MamP. MamE-PDZ1 may bind MamB. Its autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains. Peptide binding to either the first or the second PDZ domain of MamE can activate proteolysis; activation through PDZ2 is much weaker. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This MamE-like PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467634 [Multi-domain]  Cd Length: 91  Bit Score: 40.24  E-value: 1.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1711026063 351 SGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:cd23087    23 AGRGVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEVSAIMAEMPNGRSVRLGVLRDGDVRNMSL 91
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 59-295 5.50e-04

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 41.45  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  59 GTEGEQRAAAYIADRLESLGLLPAgdhgtfyqqfegtQLPHPHARpeegeviegI-NVLGFIDNAA--DHTVVIGAHYDh 135
Cdd:cd08022    28 GTEGNLELAQWTEDKWREFGLDDV-------------ELEEYDVP---------IwNVIGTIRGSEepDEYIILGNHRD- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 136 iglgvrgslhtgdpAIHPGADDNASGVALMLYLAERLRD-VHTG----NNYLFIAFSGEEKGLWGSGHWtknptvVEiEN 210
Cdd:cd08022    85 --------------AWVFGAGDPNSGTAVLLEVARALGTlLKKGwrprRTIIFASWDAEEYGLIGSTEW------VE-EN 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 211 LNYM-------LNLDMVG---RLNED-----RTLMINGT--------GTSSVWERRLERANRANL-NLRftqsgvGGSDH 266
Cdd:cd08022   144 ADWLqeravayLNVDVAVsgsTLRAAgspllQNLLREAAkevqdpdeGATLKYLPSWWDDTGGEIgNLG------SGSDY 217

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1711026063 267 TSFYL-VEVPAIHF-FTGTHED----YHRPSDTPD 295
Cdd:cd08022   218 TPFLDhLGIASIDFgFSGGPTDpyphYHSNYDSFE 252
Nicastrin pfam05450
Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, ...
 149-256 9.13e-04

Nicastrin; Nicastrin and presenilin are two major components of the gamma-secretase complex, which executes the intramembrane proteolysis of type I integral membrane proteins such as the amyloid precursor protein (APP) and Notch. Nicastrin is synthesized in fibroblasts and neurons as an endoglycosidase-H-sensitive glycosylated precursor protein (immature nicastrin) and is then modified by complex glycosylation in the Golgi apparatus and by sialylation in the trans-Golgi network (mature nicastrin). A region featured in this family has a fold similar to human transferrin receptor (TfR) and a bacterial aminopeptidase. It is implicated in the pathogenesis of Alzheimer's disease.


Pssm-ID: 310213 [Multi-domain]  Cd Length: 227  Bit Score: 40.61  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063 149 PAIHPGADDNASGVALMLYLAERLR----DVHTGN-NYLFIAFSGEEKGLWGSGHWT------KNPTV------VEIENL 211
Cdd:pfam05450  16 DGVSLGAMSSLSGFIVLLAAADALSkalpDISNLKrNVLFAFFNGESYDYIGSQRFVydmengKFPSDrththpISPDNI 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1711026063 212 NYMLNLDMVG-RLNEDRTLMINGTGTSSVWERRLERANRANLNLRF 256
Cdd:pfam05450  96 DYMLEIGQVGkATSRKFYLHVDAARNQSVKTQTLDLLDRIEKSLRS 141
PRK06133 PRK06133
glutamate carboxypeptidase; Reviewed
 20-175 1.07e-03

glutamate carboxypeptidase; Reviewed


Pssm-ID: 235710 [Multi-domain]  Cd Length: 410  Bit Score: 41.15  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  20 LAGCSSTAVIPTTEPLSPVEQFRADVefLAS-DELKGRETGT---EGEQRAAAYIADRLESLGllpagdhgtfyqqFEGT 95
Cdd:PRK06133   14 AAAAGAAAAAPDAELLAAAQQEQPAY--LDTlKELVSIESGSgdaEGLKQVAALLAERLKALG-------------AKVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  96 QLPhphARPEEGEviegiNVLGFIDNAADHTVVIGAHYDHIGLgvRGSLHT------GDPAIHPGADDNASGVALMLYLA 169
Cdd:PRK06133   79 RAP---TPPSAGD-----MVVATFKGTGKRRIMLIAHMDTVYL--PGMLAKqpfridGDRAYGPGIADDKGGVAVILHAL 148


                  ....*.
gi 1711026063 170 ERLRDV 175
Cdd:PRK06133  149 KILQQL 154
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 351-420 1.09e-03

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 37.85  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1711026063 351 SGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIE--TIYDymeaLSDYISGDE-TEV--GFKRDGELRTTTVK 420
Cdd:cd06782    12 DDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRgmSLDE----VVKLLRGPKgTKVklTIRRGGEGEPRDVT 82
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 354-419 1.24e-03

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 39.96  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1711026063 354 GLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSDYISGDETEVGFKRDGELRTTTV 419
Cdd:COG3031   152 GYRVNPGRPGSLFSKLGLQPGDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTLTY 217
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 337-391 1.27e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 37.74  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1711026063  337 RYSVSLGV-IPDYLFSGGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDY 391
Cdd:smart00228   9 KGGGGLGFsLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHL 64
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 352-397 1.76e-03

circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do), and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for the identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for the combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 2 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 37.22  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1711026063 352 GGGLKIEGVTSGRPAENAGLIRGDIIIKMGEKEIETIYDYMEALSD 397
Cdd:cd23084    17 GKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKS 62
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 357-406 2.20e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 35.97  E-value: 2.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1711026063 357 IEGVTSGRPAENAGLIRGDIIIKMGEKEIETiydyMEALSDYISGDETEV 406
Cdd:pfam17820   2 VTAVVPGSPAERAGLRVGDVILAVNGKPVRS----LEDVARLLQGSAGES 47
M28_QC_like cd03880
M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) ...
 53-190 6.85e-03

M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease.


Pssm-ID: 349876 [Multi-domain]  Cd Length: 305  Bit Score: 38.37  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711026063  53 LKGRETGTEGEQRAAAYIADRLESLGllpAGDHGTFyQQFEGTQlphPHARpeegevIEGINVLGFIDNAADHTVVIGAH 132
Cdd:cd03880    24 LIPRVPGSPGHREVRNFIIDFLKSLL---AGWTVEL-DNFTEKT---PIGE------VTFTNIIATLNPPAKRYLVLACH 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1711026063 133 YDhiglgvrgSLhtgdpaIHP-----GADDNASGVALMLYLAERLRDVHTGNNYL---------FIAFSGEE 190
Cdd:cd03880    91 YD--------SK------YFPegefiGATDSAVPCAMLLYLARSLDAALTRKWPKskksdlglqLIFFDGEE 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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