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Conserved domains on  [gi|2018288809|emb|CAG1975085|]
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unnamed protein product [Fusarium graminearum]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10330031)

M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; contains a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes

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 ...
 31-444 2.48e-86

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 cd03876:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 289  Bit Score: 266.85  E-value: 2.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  31 DIKKSKLRKTLVDLNNIGKKHGGNRAFGLPGYKASVDYIYKELKKHKKYlDTHIQPFNYTFeqtrdiqvrgpdgedvyvi 110
Cdd:cd03876     1 DITVDNLMAHLQQLQDIADANGGNRAFGSPGYNASVDYVKNELKAAGYY-DVTLQPFTSLY------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 111 tliynvgtpaggvtaplalvpiddtrgsgcfadqwegvdakdklvlvkrgscaisdklklakkagargvllvhnapgegi 190
Cdd:cd03876       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 191 tsatlsaenlelivpvgvipqevgnawrkrieggeslevtllvdsfyetRETWNIIAETKQGDPKNVVMMGAHLDSVQEG 270
Cdd:cd03876    61 -------------------------------------------------RTTYNVIAETKGGDPNNVVMLGAHLDSVSAG 91

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 271 PGINDDGSGTAGILEIAKSFTKYtGYKNKVRFAWWGAEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQYWV-- 348
Cdd:cd03876    92 PGINDNGSGSAALLEVALALAKF-KVKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERSKIRLYLNFDMIASPNYGYFIyd 170

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 349 -QASKPADRV--GGD----ILAAWLRKKGKTVEWEEFGESSDYAAFIALGIPSSGIFTGADAET---------------- 405
Cdd:cd03876   171 gDGSAFNLTGppGSAeierLFEAYFTSLGLPSTPTEFDGRSDYAPFIEAGIPAGGLFTGAEGIKteeqaalwggtagvay 250

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2018288809 406 DPCYHLACDTIDNIHWDALTLNTKTAGRAAAQFALSLKG 444
Cdd:cd03876   251 DPCYHQACDTIDNINRTALLRNADAIAHAVATYARSTEG 289
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
 107-231 1.44e-54

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


:

Pssm-ID: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 178.67  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 107 VYVITLIYNVGTPAGGVTAPLalVPIDDTRGSGCFADQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAP 186
Cdd:cd04816     1 VFVVSLSYSPSTPPGGVTAPL--VPLDPERPAGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2018288809 187 GeGITSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd04816    79 G-GGTAGTLGAPNIDLKVPVGVITKAAGAALRRRLGAGETLELDA 122
 
Name Accession Description Interval E-value
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 31-444 2.48e-86

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: 266.85  E-value: 2.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  31 DIKKSKLRKTLVDLNNIGKKHGGNRAFGLPGYKASVDYIYKELKKHKKYlDTHIQPFNYTFeqtrdiqvrgpdgedvyvi 110
Cdd:cd03876     1 DITVDNLMAHLQQLQDIADANGGNRAFGSPGYNASVDYVKNELKAAGYY-DVTLQPFTSLY------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 111 tliynvgtpaggvtaplalvpiddtrgsgcfadqwegvdakdklvlvkrgscaisdklklakkagargvllvhnapgegi 190
Cdd:cd03876       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 191 tsatlsaenlelivpvgvipqevgnawrkrieggeslevtllvdsfyetRETWNIIAETKQGDPKNVVMMGAHLDSVQEG 270
Cdd:cd03876    61 -------------------------------------------------RTTYNVIAETKGGDPNNVVMLGAHLDSVSAG 91

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 271 PGINDDGSGTAGILEIAKSFTKYtGYKNKVRFAWWGAEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQYWV-- 348
Cdd:cd03876    92 PGINDNGSGSAALLEVALALAKF-KVKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERSKIRLYLNFDMIASPNYGYFIyd 170

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 349 -QASKPADRV--GGD----ILAAWLRKKGKTVEWEEFGESSDYAAFIALGIPSSGIFTGADAET---------------- 405
Cdd:cd03876   171 gDGSAFNLTGppGSAeierLFEAYFTSLGLPSTPTEFDGRSDYAPFIEAGIPAGGLFTGAEGIKteeqaalwggtagvay 250

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2018288809 406 DPCYHLACDTIDNIHWDALTLNTKTAGRAAAQFALSLKG 444
Cdd:cd03876   251 DPCYHQACDTIDNINRTALLRNADAIAHAVATYARSTEG 289
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 215-439 1.32e-54

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: 183.41  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 215 NAWRKRIEGGESLEVTLLVDSFYETRETWNIIAETKQGDPKN-VVMMGAHLDSV-QEGPGINDDGSGTAGILEIAKSFTK 292
Cdd:COG2234    19 AAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDeVVVLGAHYDSVgSIGPGADDNASGVAALLELARALAA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 293 YtGYKNK--VRFAWWGAEESGLAGSYFYGEQLTEkEADSIRFYFNYDMIGSPKP--QYWVQASKPADRvGGDILAAWLRK 368
Cdd:COG2234    99 L-GPKPKrtIRFVAFGAEEQGLLGSRYYAENLKA-PLEKIVAVLNLDMIGRGGPrnYLYVDGDGGSPE-LADLLEAAAKA 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018288809 369 -----KGKTVEWEEFGESSDYAAFIALGIPSSGIFTGADaETDPCYHLACDTIDNIHWDALTLNTKTAGRAAAQFA 439
Cdd:COG2234   176 ylpglGVDPPEETGGYGRSDHAPFAKAGIPALFLFTGAE-DYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELA 250
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
 107-231 1.44e-54

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 178.67  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 107 VYVITLIYNVGTPAGGVTAPLalVPIDDTRGSGCFADQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAP 186
Cdd:cd04816     1 VFVVSLSYSPSTPPGGVTAPL--VPLDPERPAGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2018288809 187 GeGITSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd04816    79 G-GGTAGTLGAPNIDLKVPVGVITKAAGAALRRRLGAGETLELDA 122
Peptidase_M28 pfam04389
Peptidase family M28;
244-439 4.00e-51

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 172.08  E-value: 4.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKYTGYKNKVRFAWWGAEESGLAGSYFYGEQlt 323
Cdd:pfam04389   1 NVIAKLPGKAPDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQRPKRSVRFLFFDAEEAGLLGSHHFAKS-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 324 EKEADSIRFYFNYDMIGSPKPQYWVQASKPADRVGGDILAAWLRKKGKTVEWEEFGES-----SDYAAFIALGIPSSGIf 398
Cdd:pfam04389  79 HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERggpgrSDHAPFIKAGIPGLDL- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2018288809 399 tgADAETDPCYHLACDTIDNIHWDALtlntKTAGRAAAQFA 439
Cdd:pfam04389 158 --AFTDFGYRYHTPADTIDNIDPGTL----QRIGDLVLALV 192
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 124-217 8.51e-11

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 58.29  E-value: 8.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 124 TAPLALVPiddtrgsGCFADQW--EGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGITSATLSAENLE 201
Cdd:pfam02225   1 TGPLVLAP-------GCYAGDGipADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYP 73

                          90
                  ....*....|....*...
gi 2018288809 202 LI--VPVGVIPQEVGNAW 217
Cdd:pfam02225  74 DGiyIPAVGVSRADGEAL 91
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 119-234 1.96e-10

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 63.52  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 119 PAGGVTAPLALVPIDDTRGS-GCFAdQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGITSaTLSA 197
Cdd:NF038113  436 PDAPITGDLALATDSSPDPNdGCDP-ILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGEPIVM-GGGD 513

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018288809 198 ENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTLLVD 234
Cdd:NF038113  514 TGPPITIPSIMISQADGEAIITALNNGETVNVTLKDD 550
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 113-232 8.98e-10

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 61.60  E-value: 8.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  113 IYNVGTPAGG-----VTAPLALVPIDDTRGS-GC--F--ADQWEGvdakdKLVLVKRGSCAISDKLKLAKKAGARGVLLV 182
Cdd:NF038112   502 VYEAGSASFGpqafdVTGDVVLAPDGTGSDTdGCtpFtnAAEVAG-----KIALIDRGTCDFTVKALNAQNAGAIGVIIA 576

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018288809  183 HNAPGegiTSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGeSLEVTLL 232
Cdd:NF038112   577 NNAAG---AAPGLGGTDPAVTIPALSITQADGNAWKAALANG-PVTVRLR 622
 
Name Accession Description Interval E-value
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 31-444 2.48e-86

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: 266.85  E-value: 2.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  31 DIKKSKLRKTLVDLNNIGKKHGGNRAFGLPGYKASVDYIYKELKKHKKYlDTHIQPFNYTFeqtrdiqvrgpdgedvyvi 110
Cdd:cd03876     1 DITVDNLMAHLQQLQDIADANGGNRAFGSPGYNASVDYVKNELKAAGYY-DVTLQPFTSLY------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 111 tliynvgtpaggvtaplalvpiddtrgsgcfadqwegvdakdklvlvkrgscaisdklklakkagargvllvhnapgegi 190
Cdd:cd03876       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 191 tsatlsaenlelivpvgvipqevgnawrkrieggeslevtllvdsfyetRETWNIIAETKQGDPKNVVMMGAHLDSVQEG 270
Cdd:cd03876    61 -------------------------------------------------RTTYNVIAETKGGDPNNVVMLGAHLDSVSAG 91

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 271 PGINDDGSGTAGILEIAKSFTKYtGYKNKVRFAWWGAEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQYWV-- 348
Cdd:cd03876    92 PGINDNGSGSAALLEVALALAKF-KVKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERSKIRLYLNFDMIASPNYGYFIyd 170

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 349 -QASKPADRV--GGD----ILAAWLRKKGKTVEWEEFGESSDYAAFIALGIPSSGIFTGADAET---------------- 405
Cdd:cd03876   171 gDGSAFNLTGppGSAeierLFEAYFTSLGLPSTPTEFDGRSDYAPFIEAGIPAGGLFTGAEGIKteeqaalwggtagvay 250

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2018288809 406 DPCYHLACDTIDNIHWDALTLNTKTAGRAAAQFALSLKG 444
Cdd:cd03876   251 DPCYHQACDTIDNINRTALLRNADAIAHAVATYARSTEG 289
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 215-439 1.32e-54

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: 183.41  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 215 NAWRKRIEGGESLEVTLLVDSFYETRETWNIIAETKQGDPKN-VVMMGAHLDSV-QEGPGINDDGSGTAGILEIAKSFTK 292
Cdd:COG2234    19 AAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDeVVVLGAHYDSVgSIGPGADDNASGVAALLELARALAA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 293 YtGYKNK--VRFAWWGAEESGLAGSYFYGEQLTEkEADSIRFYFNYDMIGSPKP--QYWVQASKPADRvGGDILAAWLRK 368
Cdd:COG2234    99 L-GPKPKrtIRFVAFGAEEQGLLGSRYYAENLKA-PLEKIVAVLNLDMIGRGGPrnYLYVDGDGGSPE-LADLLEAAAKA 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018288809 369 -----KGKTVEWEEFGESSDYAAFIALGIPSSGIFTGADaETDPCYHLACDTIDNIHWDALTLNTKTAGRAAAQFA 439
Cdd:COG2234   176 ylpglGVDPPEETGGYGRSDHAPFAKAGIPALFLFTGAE-DYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELA 250
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
 107-231 1.44e-54

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 178.67  E-value: 1.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 107 VYVITLIYNVGTPAGGVTAPLalVPIDDTRGSGCFADQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAP 186
Cdd:cd04816     1 VFVVSLSYSPSTPPGGVTAPL--VPLDPERPAGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2018288809 187 GeGITSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd04816    79 G-GGTAGTLGAPNIDLKVPVGVITKAAGAALRRRLGAGETLELDA 122
Peptidase_M28 pfam04389
Peptidase family M28;
244-439 4.00e-51

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 172.08  E-value: 4.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKYTGYKNKVRFAWWGAEESGLAGSYFYGEQlt 323
Cdd:pfam04389   1 NVIAKLPGKAPDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQRPKRSVRFLFFDAEEAGLLGSHHFAKS-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 324 EKEADSIRFYFNYDMIGSPKPQYWVQASKPADRVGGDILAAWLRKKGKTVEWEEFGES-----SDYAAFIALGIPSSGIf 398
Cdd:pfam04389  79 HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERggpgrSDHAPFIKAGIPGLDL- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2018288809 399 tgADAETDPCYHLACDTIDNIHWDALtlntKTAGRAAAQFA 439
Cdd:pfam04389 158 --AFTDFGYRYHTPADTIDNIDPGTL----QRIGDLVLALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 244-432 1.11e-37

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: 136.70  E-value: 1.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAE-TKQGDPKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTK-YTGYKNKVRFAWWGAEESGLAGSYFYGEQ 321
Cdd:cd02690     3 NVIATiKGSDKPDEVILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKlQLKPKRSIRFAFWDAEELGLLGSKYYAEQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 322 LtEKEADSIRFYFNYDMIGSPKPQYWVQASKPADRVgGDILAAWLRKKGKTVEWEEFGES------SDYAAFIALGIPsS 395
Cdd:cd02690    83 L-LSSLKNIRAALNLDMIGGAGPDLYLQTAPGNDAL-VEKLLRALAHELENVVYTVVYKEdggtggSDHRPFLARGIP-A 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2018288809 396 GIFTGADAETDPCYHLACDTIDNIHWDALTLNTKTAG 432
Cdd:cd02690   160 ASLIQSESYNFPYYHTTQDTLENIDKDTLKRAGDILA 196
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 244-419 5.26e-30

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: 117.67  E-value: 5.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKN---VVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKYTGYKnKVRFAWWGAEESGLAGSYFYGE 320
Cdd:cd05661    62 NVIATKKPDNNKNnndIIIVTSHYDSVVKAPGANDNASGTAVTLELARVFKKVKTDK-ELRFIAFGAEENGLLGSKYYVA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 321 QLTEKEADSIRFYFNYDMIGSP--------------KPQYWVQASKPADRVGGDILAawlrkkgktvewEEFGESSDYAA 386
Cdd:cd05661   141 SLSEDEIKRTIGVFNLDMVGTSdakagdlyaytidgKPNLVTDSGAAASKRLSGVLP------------LVQQGSSDHVP 208

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2018288809 387 FIALGIPSSgIF---TGADAETDPCYHLACDTIDNI 419
Cdd:cd05661   209 FHEAGIPAA-LFihmDPETEPVEPWYHTPNDTVENI 243
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 244-435 3.96e-28

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: 110.80  E-value: 3.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKN-VVMMGAHLDSVQEG---------PGINDDGSGTAGILEIAKSFTKYTGYKNKVRFAWWGAEESGLA 313
Cdd:cd03877     3 NVVGVLEGSDLPDeTIVIGAHYDHLGIGggdsgdkiyNGADDNASGVAAVLELARYFAKQKTPKRSIVFAAFTAEEKGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 314 GSYFYGEQLTEKEaDSIRFYFNYDMIGSPKP-----------QYWVQASKPADRVGGDILaawlrKKGKTVEWEEFgeSS 382
Cdd:cd03877    83 GSKYFAENPKFPL-DKIVAMLNLDMIGRLGRskdvyligsgsSELENLLKKANKAAGRVL-----SKDPLPEWGFF--RS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2018288809 383 DYAAFIALGIPSSGIFTGadaeTDPCYHLACDTIDNIHWDALTLNTKTAGRAA 435
Cdd:cd03877   155 DHYPFAKAGVPALYFFTG----LHDDYHKPSDDYEKIDYEGMARVVNLIYQLL 203
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 106-231 1.74e-20

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 87.19  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 106 DVYVITLIYnvGTPAGGVTAPLALVPIDDTRGSGC--FADQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVH 183
Cdd:cd00538     1 DVILATTGY--AGSALLFNPPSSPVGVVAGPLVGCgyGTTDDSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYN 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2018288809 184 NAPGEGITSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd00538    79 NGDDPGPQMGSVGLESTDPSIPTVGISYADGEALLSLLEAGKTVTVDL 126
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 237-429 2.72e-19

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: 88.19  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 237 YETRETWNIIAeTKQGD--PKNVVMMGAHLD-----SVQEGPGIN----DDGSGTAGILEIAKSFTK-YTGYKNKVRFAW 304
Cdd:cd05660    54 IEYSTSHNVVA-ILPGSklPDEYIVLSAHWDhlgigPPIGGDEIYngavDNASGVAAVLELARVFAAqDQRPKRSIVFLA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 305 WGAEESGLAGSYFYGEQLTEKEADSIRFyFNYDMIGSPKPQYWVQASKPADRVGGDILAAWLRKKGKTVEWEEFGES--- 381
Cdd:cd05660   133 VTAEEKGLLGSRYYAANPIFPLDKIVAN-LNIDMIGRIGPTKDVLLIGSGSSELENILKEAAKAVGRVVDYDPNPENgsf 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018288809 382 --SDYAAFIALGIPSSGIFTGAD----------AETDPCYHLACDTI-DNIHWDALTLNTK 429
Cdd:cd05660   212 yrSDHYNFAKKGVPVLFFFGGYDlgdggkklakAYLHTDYHKPADDVtEKWDYEGAAEDTK 272
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 53-428 1.65e-18

M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.


Pssm-ID: 349879 [Multi-domain]  Cd Length: 425  Bit Score: 87.75  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  53 GNRAFGLPGYKASVDYIYKELKKHKkyLDT-HIQPFNYTfeqtrdIQVRG--------PDGEDVYVITLIYNVGTPAGGV 123
Cdd:cd03883    33 GPRLSGSENLEKAIDWLYAKLQNDG--FDKvHEEPVEVP------HWVRGeesatllePRPQKLAILGLGGSVGTPVEGI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 124 TAPLALV--------PIDDTRGS-GCFADQWEGVDAkdklVLVKRGSCAisdklKLAKKAGARGVLL------VHNAPGE 188
Cdd:cd03883   105 EAEVVVVfsfeelqaKADEVKGKiVVYNQPFKGYGE----TVKYRGQGA-----VEAAKYGAVAVLIrsitpfSIYSPHT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 189 GITS----------ATLSAENLELIvpvgvipqevgnaWRKRIEGgesLEVTLLVD---SFYETRETWNIIAETKqGD-- 253
Cdd:cd03883   176 GIMRyqdgvtkipaAAITVEDAEML-------------SRMAARG---QKIVIELKmeaKTYPDATSRNVIAEIT-GSky 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 254 PKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFtKYTGYKNK--VRFAWWGAEESGLAGSYFYGEqLTEKEADSIR 331
Cdd:cd03883   239 PDEVVLVGGHLDSWDVGTGAMDDGGGVAISWEALKLI-KDLGLKPKrtIRVVLWTGEEQGLVGAKAYAE-AHKDELENHV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 332 FYFNYDmIGSPKPQYWVQASKPADRVGGDILAAWLRKKGKTVEWEEFGESSDYAAFIALGIPSSGIFTgadaETDPCY-- 409
Cdd:cd03883   317 FAMESD-IGTFTPYGLQFTGSDTARAIVKEVMKLLSPLGITQVLPKAGVGPDISFLKAAGVPGASLIQ----DNSDYFdy 391

                         410       420
                  ....*....|....*....|
gi 2018288809 410 -HLACDTIDNIHWDALTLNT 428
Cdd:cd03883   392 hHTAGDTMDVMDPKQLDQNV 411
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 239-431 2.24e-18

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: 84.83  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 239 TRETWNIIAETKQGDPKNVVMM-GAHLD--SVQEG---PGINDDGSGTAGILEIAKSFTKYtGYKNKVRFAWWGAEESGL 312
Cdd:cd05662    59 TRQGVNVLAVIKGSEPPTKWRVvSAHYDhlGIRGGkiyNGADDNASGVAALLALAEYFKKH-PPKHNVIFAATDAEEPGL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 313 AGSYFYGEQLTEKEAdSIRFYFNYDMIGSPK--------PQYWVQASKPADRVGGD-ILAAWLRKKGKTVEWEEFGESSD 383
Cdd:cd05662   138 RGSYAFVEALKVPRA-QIELNINLDMISRPErnelyvegASQFPQLTSILENVKGTcIKALHPKDTDGSIGSIDWTRASD 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2018288809 384 YAAFIALGIPSsgIFTGadAETDPCYHLACDTIDNIHWDALTLNTKTA 431
Cdd:cd05662   217 HYPFHKAKIPW--LYFG--VEDHPDYHKPTDDFETIDQEFFAAVVESA 260
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 231-436 5.74e-18

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: 84.04  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 231 LLVDSFYETRETW---------NIIAETK-QGDPKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKYTGyKNKV 300
Cdd:cd05640    32 ELVGSGYNVTSHFfshqegvyaNLIADLPgSYSQDKLILIGAHYDTVPGSPGADDNASGVAALLELARLLATLDP-NHTL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 301 RFAWWGAEE-----SGLAGSYFYGEQLTeKEADSIRFYFNYDMIGSPKPQYWVQASKP-------ADRvgGDILAAWLRK 368
Cdd:cd05640   111 RFVAFDLEEypffaRGLMGSHAYAEDLL-RPLTPIVGMLSLEMIGYYDPFPHSQAYPAgfelhfyPHM--GDFIAVVGRL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 369 KGKT----------------VEW---EEFGES------SDYAAFIALGIPSSGIFTGADAETdPCYHLACDTIDNIHWDA 423
Cdd:cd05640   188 RSRKlvrafkrafrmlsdfpVESlnlPFNGPGvppfrrSDHSSFWDHGYPAIMVTDTAFYRN-PQYHLPCDTPDTLNYKF 266

                         250
                  ....*....|...
gi 2018288809 424 LTLNTKTAGRAAA 436
Cdd:cd05640   267 LTRVTAGLAAGLA 279
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 242-394 2.49e-17

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: 80.72  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 242 TWNIIAETKQGDPKN-VVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKYtGYKNK--VRFAWWGAEESGLAGS--- 315
Cdd:cd08015     1 TYNVIAEIPGSDKKDeVVILGAHLDSWHGATGATDNGAGTAVMMEAMRILKAI-GSKPKrtIRVALWGSEEQGLHGSray 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 316 ---YFYGEQLTEKEADSIRF--YFNYDMIGSPKPQYWVQASKPAdrvgGDILAAWLRK----KGKTVEWEEFGeSSDYAA 386
Cdd:cd08015    80 vekHFGDPPTMQLQRDHKKIsaYFNLDNGTGRIRGIYLQGNLAA----YPIFSAWLYPfhdlGATTVIERNTG-GTDHAA 154


                  ....*...
gi 2018288809 387 FIALGIPS 394
Cdd:cd08015   155 FDAVGIPA 162
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
 103-231 1.31e-16

PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239045 [Multi-domain]  Cd Length: 122  Bit Score: 75.76  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 103 DGEDVYVITLIYnvgTPAGGVTAPLALVPiddtrGSGCFADQWEgVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLV 182
Cdd:cd02130     5 NGEAIPTTAFTY---SPAGEVTGPLVVVP-----NLGCDAADYP-ASVAGNIALIERGECPFGDKSALAGAAGAAAAIIY 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2018288809 183 HNAPGEGItSATLSAENLELiVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd02130    76 NNVPAGGL-SGTLGEPSGPY-VPTVGISQEDGKALVAALANGGEVSANL 122
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 244-438 4.39e-16

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: 78.26  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIA--ETKQGDPKNVVMMGAHLDSVQEG--------------PGINDDGSGTAGILEIA---KSFTKYTGYKNKVRFAW 304
Cdd:cd05663    57 NVIGvlPGKGDVADETVVVGAHYDHLGYGgegslargdeslihNGADDNASGVAAMLELAaklVDSDTSLALSRNLVFIA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 305 WGAEESGLAGSYFYGEQLTeKEADSIRFYFNYDMIGSPK-PQYWVQASKPADRVGGDILAAWLRKKGKTVEWEEFGESSD 383
Cdd:cd05663   137 FSGEELGLLGSKHFVKNPP-FPIKNTVYMINMDMVGRLRdNKLIVQGTGTSPGWEQLVQARNKATGFKLILDPTGYGPSD 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2018288809 384 YAAFIALGIPSSGIFTGADAEtdpcYHLACDTIDNIHWDALTLNTKTAGRAAAQF 438
Cdd:cd05663   216 HTSFYLDDVPVLHFFTGAHSD----YHRPSDDSDKLNYDGMADIADFAVRIISAL 266
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 243-421 1.05e-14

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: 74.57  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 243 WNIIAETK-QGDPKNVVMMGAHLDSvqEGPGINDDGSGTAGILEIAKSFTKYT--GYKNKvR---FAWWGAEESGLAGSY 316
Cdd:cd08022    61 WNVIGTIRgSEEPDEYIILGNHRDA--WVFGAGDPNSGTAVLLEVARALGTLLkkGWRPR-RtiiFASWDAEEYGLIGST 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 317 FYGEQLTEKEADSIRFYFNYDMIGSpKPQYWVQASKPADRVGGDILA----------------AWLRKKGktvEWEEFGE 380
Cdd:cd08022   138 EWVEENADWLQERAVAYLNVDVAVS-GSTLRAAGSPLLQNLLREAAKevqdpdegatlkylpsWWDDTGG---EIGNLGS 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2018288809 381 SSDYAAFIA-LGIPSSGI-FTGADAETDPCYHlacdTI-DNIHW 421
Cdd:cd08022   214 GSDYTPFLDhLGIASIDFgFSGGPTDPYPHYH----SNyDSFEW 253
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
 145-234 1.42e-14

PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239048 [Multi-domain]  Cd Length: 143  Bit Score: 70.78  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 145 WEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEgITSATlsaeNLELIVPVGVIPQEVGNAWRKRIEGG 224
Cdd:cd02133    41 FEGKDVKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNVDGL-IPGTL----GEAVFIPVVFISKEDGEALKAALESS 115

                          90
                  ....*....|
gi 2018288809 225 ESLEVTLLVD 234
Cdd:cd02133   116 KKLTFNTKKE 125
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 236-442 1.52e-13

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: 70.79  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 236 FYETRETWNIIAETK---QGDpKNVVMmGAHLDSVqeGPGINDDGSGTAGILEIAKSFTKYTgYKN------KVRFAWWG 306
Cdd:cd03874    51 LEEYSPITNVVGKIEgieQPD-RAIII-GAHRDSW--GYGAGYPNSGTAVLLEIARLFQQLK-KKFgwkplrTIYFISWD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 307 AEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQYWVQAS--------KPADRVGGDILAAWLRKKG-KTVewEE 377
Cdd:cd03874   126 GSEFGLAGSTELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHpllqslfrKASKKVKFPGNEDWWKHSPnAKV--SN 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018288809 378 FGESSDYAAFI-ALGIPSSGIFTGADAETDPCYHLACDTIDNIH--WDALTLNTKTAGRAAAQFALSL 442
Cdd:cd03874   204 LHQYGDWTPFLnHLGIPVAVFSFKNDRNASYPINSSYDTFEWLEkfLDPDFELHSTLAEFVGLLVLSL 271
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
 117-231 1.43e-12

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 64.27  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 117 GTPAGGVTAPLALV-PIDDTRGSGCFADQwEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGitSATL 195
Cdd:cd04818     6 GPALTNVTADVVLAgAAPASNTDGCTAFT-NAAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAGGA--PITM 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2018288809 196 SAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd04818    83 GGDDPDITIPAVMISQADGDALKAALAAGGTVTVTL 118
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 254-418 2.11e-12

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: 67.65  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 254 PKNVVMMGAHLDSVQEG-------PGINDDGSGTAGILEIAKSFTKYtGY--KNKVRFAWWGAEESGLAGSYFYGEQLTE 324
Cdd:cd03879    87 SDEIVVIGAHQDSINGSnpsngraPGADDDGSGTVTILEALRVLLES-GFqpKNTIEFHWYAAEEGGLLGSQAIATQYKS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 325 KEADsIRFYFNYDMIGspkpqyWVQASKPA------DRVGGDiLAAWLRKKGKTVEWEEFGES------SDYAAFIALGI 392
Cdd:cd03879   166 EGKN-VKAMLQLDMTG------YVKPGSAEdiglitDYTDSN-LTQFLKQLIDEYLPIPYGDTkcgyacSDHASWTKAGY 237

                         170       180
                  ....*....|....*....|....*.
gi 2018288809 393 PSSGIFTGADAETDPCYHLACDTIDN 418
Cdd:cd03879   238 PAAFPFESAFEDYNPYIHTTNDTLDN 263
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 244-321 1.48e-11

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: 65.30  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIA--ETKQGDPKNVVMMGAHLDSVQEGPGINDDGSGTAGILEIAKSFTKY-TGYKNKVRFAWWGAEESGLAGSYFYGE 320
Cdd:cd03875    81 NIVVriSGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSgHQPKRDIIFLFNGAEENGLLGAHAFIT 160


                  .
gi 2018288809 321 Q 321
Cdd:cd03875   161 Q 161
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 124-217 8.51e-11

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 58.29  E-value: 8.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 124 TAPLALVPiddtrgsGCFADQW--EGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGITSATLSAENLE 201
Cdd:pfam02225   1 TGPLVLAP-------GCYAGDGipADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYP 73

                          90
                  ....*....|....*...
gi 2018288809 202 LI--VPVGVIPQEVGNAW 217
Cdd:pfam02225  74 DGiyIPAVGVSRADGEAL 91
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 119-234 1.96e-10

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 63.52  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 119 PAGGVTAPLALVPIDDTRGS-GCFAdQWEGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGITSaTLSA 197
Cdd:NF038113  436 PDAPITGDLALATDSSPDPNdGCDP-ILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGEPIVM-GGGD 513

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018288809 198 ENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTLLVD 234
Cdd:NF038113  514 TGPPITIPSIMISQADGEAIITALNNGETVNVTLKDD 550
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 238-442 4.74e-10

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: 60.50  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 238 ETRETWNIIAETKQGDPKNVVMMGAHLdsvQEG-PGINDDGSGTAGILEIAKSFTKYTGYKNKVRFAW-WGAEESGLAgS 315
Cdd:cd05643    66 ELNETLPILYAIIGKETPPEIAFVAHL---CHPkPGANDNASGSALLLEVARVLAKLILNRPKRGICFlWVPEYTGTA-A 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 316 YFYGEQLTEKEadsIRFYFNYDMIGSPKPQ---YWVQASKPADRV--GGDILAAWLRKKGKTVE------WEEFGESSDY 384
Cdd:cd05643   142 YFAQHPDRLKK---IIAVINLDMVGEDQTKtgsTLMLVPTPLSFPsyLNEELAQKLSNFTGSSLpavrygKEPYEGGSDH 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2018288809 385 AAFIALGIPSSGIFTGadaeTDPCYHLACDTIDNIhwDALTL-NTKTAGRAAAQFALSL 442
Cdd:cd05643   219 DVFSDPGIPAVMFNTW----PDRYYHTSDDTPDKL--DPETLkNVGAAVLLTAYALANG 271
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 113-232 8.98e-10

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 61.60  E-value: 8.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809  113 IYNVGTPAGG-----VTAPLALVPIDDTRGS-GC--F--ADQWEGvdakdKLVLVKRGSCAISDKLKLAKKAGARGVLLV 182
Cdd:NF038112   502 VYEAGSASFGpqafdVTGDVVLAPDGTGSDTdGCtpFtnAAEVAG-----KIALIDRGTCDFTVKALNAQNAGAIGVIIA 576

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2018288809  183 HNAPGegiTSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGeSLEVTLL 232
Cdd:NF038112   577 NNAAG---AAPGLGGTDPAVTIPALSITQADGNAWKAALANG-PVTVRLR 622
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 244-345 1.56e-09

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: 59.43  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETK-QGDPKNVVMMGAHLDS--------VQEGPGINDDGSGTAGILEIAKSFTKYTgYKNKVRFAWWGAEESGLAG 314
Cdd:cd05642    90 NVVATLKgSEDPDRVYVVSGHYDSrvsdvmdyESDAPGANDDASGVAVSMELARIFAKHR-PKATIVFTAVAGEEQGLYG 168

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2018288809 315 SYFYGEQLTEKEADsIRFYFNYDMIGSPKPQ 345
Cdd:cd05642   169 STFLAQTYRNNSVN-VEGMLNNDIVGSSTGD 198
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 244-403 1.20e-08

M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. 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: 349948 [Multi-domain]  Cd Length: 198  Bit Score: 55.13  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKNVVMMGAHLDSVQE---------------------GPGINDDGSGTAGILEIAKSFTKYTGYKN-KVR 301
Cdd:cd18669     1 NVIARYGGGGGGKRVLLGAHIDVVPAgegdprdppffvdtveegrlyGRGALDDKGGVAAALEALKLLKENGFKLKgTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 302 FAWWGAEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQYWVQAskpadrVGGDILAAWLRK-KGKTVEWEEFGE 380
Cdd:cd18669    81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRT------PLVDALSEAARKvFGKPQHAEGTGG 154

                         170       180
                  ....*....|....*....|...
gi 2018288809 381 SSDYAAFIALGIPSSGIFTGADA 403
Cdd:cd18669   155 GTDGRYLQELGIPGVTLGAGGGK 177
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 244-403 1.05e-07

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: 52.04  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 244 NIIAETKQGDPKNVVMMGAHLDSVQEGPGIN---------------------DDGSGTAGILEIAKSFtKYTGYKNK--V 300
Cdd:cd03873     1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNrdppfaedteeegrlygrgalDDKGGVAAALEALKRL-KENGFKPKgtI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 301 RFAWWGAEESGLAGSYFYGEQLTEKEADSIRFYFNYDMIGSPKPQ--------YWVQASKPADRVGgdilaawlrkkGKT 372
Cdd:cd03873    80 VVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQkgvvirnpLVDALRKAAREVG-----------GKP 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2018288809 373 VEWEEFGESSDYAAFIALGIPSSGIFTGADA 403
Cdd:cd03873   149 QRASVIGGGTDGRLFAELGIPGVTLGPPGDK 179
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
 149-231 5.28e-06

PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239039  Cd Length: 129  Bit Score: 45.78  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 149 DAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGeGITSATLSAENLelivpVGVIPQEVGNAWRKRIEGGESle 228
Cdd:cd02124    53 DLSGYIVLVRRGTCTFATKAANAAAKGAKYVLIYNNGSG-PTDQVGSDADSI-----IAAVTPEDGEAWIDALAAGSN-- 124


                  ...
gi 2018288809 229 VTL 231
Cdd:cd02124   125 VTV 127
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
 115-231 1.71e-05

PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239040 [Multi-domain]  Cd Length: 127  Bit Score: 44.39  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 115 NVGTPA-GGVTAPLALVPIDDTRGSGCFADQWEGVDAKDK----LVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEG 189
Cdd:cd02125     1 NFGLPQyGGTLTGVVVYPKENRTGCKEFDVFFKPKKSEPGrrpvILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEPL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2018288809 190 IT----SATLSAENLELI-VPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd02125    81 LTmdtpEESGSADYIEKItIPSALITKAFGEKLKKAISNGEMVVIKL 127
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
 152-231 3.28e-05

PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239047 [Multi-domain]  Cd Length: 139  Bit Score: 43.57  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 152 DKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEGITSATLSAENLELIVPVGVIPQEVGNAWRKRIEGGESLEVTL 231
Cdd:cd02132    60 GSIALVERGECAFTEKAKIAEAGGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
 151-185 9.95e-05

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 41.99  E-value: 9.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2018288809 151 KDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNA 185
Cdd:cd02129    44 KGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRE 78
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 259-334 2.81e-04

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 42.72  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 259 MMGAHLDSVQE-----------------GPGINDDGSGTAGILEIAKSFTKYTGYKNKVRFAWWGAEESGLAGSYFYGEQ 321
Cdd:pfam01546   1 LLRGHMDVVPDeetwgwpfkstedgklyGRGHDDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGGARALIED 80

                          90
                  ....*....|...
gi 2018288809 322 LTEkEADSIRFYF 334
Cdd:pfam01546  81 GLL-EREKVDAVF 92
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 233-442 3.30e-04

M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) subfamily. TfRs 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). While related in sequence to peptidase M28 glutamate carboxypeptidase II (also called prostate-specific membrane antigen or PSMA), TfR lacks the metal ion coordination centers and protease activity of that group.


Pssm-ID: 349946 [Multi-domain]  Cd Length: 285  Bit Score: 42.36  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 233 VDSFYETRetwNIIAETK-QGDPKNVVMMGAHLDSVqeGPGINDDGSGTAGILEIAKSFT---KYTGYKNK--VRFAWWG 306
Cdd:cd09848    50 TDEHYKIH---NIFGVIKgFVEPDRYVVIGAQRDAW--GPGAAKSGVGTALLLELARTFSdmvKNDGFKPRrsIVFASWS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 307 AEESGLAGSY----FYGEQLtEKEADSirfYFNYDMIGSPKPQYWVQAS--------------KPADRVGGDILAAWLRK 368
Cdd:cd09848   125 AGDFGSVGATewleGYLSSL-HLKAFT---YISLDGAVLGDDSFKASASpllytliestmkqvKSPVHSGQSYYETRSSW 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018288809 369 KGKTVewEEFGESSDYAAFIAL-GIPS-SGIFTgADAETDPCYHLACDTIDNIHW---DALTLNTKTAGRAAAQFALSL 442
Cdd:cd09848   201 WASIV--EPLGLDSAAYPFLAFsGIPSvSFHFT-EDDEDYPFLGTKEDTKENLDKftnGELWEVAAAAAEVAGQMALRL 276
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
 156-189 2.81e-03

PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239037 [Multi-domain]  Cd Length: 138  Bit Score: 38.05  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2018288809 156 LVKRGSCAISDKLKLAKKAGARGVlLVHNAPGEG 189
Cdd:cd02122    65 LIQRGNCTFEEKIKLAAERNASAV-VIYNNPGTG 97
M28_nicalin_like cd03882
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ...
 262-353 4.19e-03

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: 39.27  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 262 AHLDS--VQEGPGINDD--GSGTAGILEIAKSF-----TKYTGYKNKVRFAWWGAEESGLAGSYFYGEQLTEKEADSIRF 332
Cdd:cd03882    96 AHYDTfgVAPWLSSGADsnGSGVAALLELMRLFsrlysNPRTRAKYNLLFLLTGGGKLNYQGTKHWLESNLDHFLDNVEF 175

                          90       100
                  ....*....|....*....|.
gi 2018288809 333 YFNYDMIGSPKPQYWVQASKP 353
Cdd:cd03882   176 VLCLDSIGSKDSDLYLHVSKP 196
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 128-219 4.60e-03

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 37.39  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 128 ALVPIDDTRGSGCFADQWEGVDAKDKLVLVKRGS-CAISDKLKLAKKAGARGVLLVhNAPGEGITSATLSaenleLIVPV 206
Cdd:cd02120    28 KSANSGDVDASLCLPGSLDPSKVKGKIVLCDRGGnTSRVAKGDAVKAAGGAGMILA-NDPTDGLDVVADA-----HVLPA 101

                          90
                  ....*....|...
gi 2018288809 207 GVIPQEVGNAWRK 219
Cdd:cd02120   102 VHVDYEDGTAILS 114
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 129-188 4.62e-03

PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239042 [Multi-domain]  Cd Length: 118  Bit Score: 36.97  E-value: 4.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018288809 129 LVPIDDTRGSGCFADqweGVDAKDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGE 188
Cdd:cd02127    15 LVPADPLEACEELRN---IHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNNDS 71
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
 151-191 7.35e-03

PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this PA domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup.


Pssm-ID: 240117 [Multi-domain]  Cd Length: 117  Bit Score: 36.60  E-value: 7.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2018288809 151 KDKLVLVKRGSCAISDKLKLAKKAGARGVLLVHNAPGEG-IT 191
Cdd:cd04813    39 DGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEPGRGlIT 80
 
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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