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Conserved domains on  [gi|497571736|ref|WP_009885920|]
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prolyl aminopeptidase [Mycoplasmoides genitalium]

Protein Classification

alpha/beta hydrolase; tannase/feruloyl esterase family alpha/beta hydrolase( domain architecture ID 10796800)

uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds| tannase/feruloyl esterase family alpha/beta hydrolase similar to Aspergillus oryzae tannase and Aspergillus niger feruloyl esterase B

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
3-308 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


:

Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 542.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736    3 TKLNVKGYLNVGDNHQLYYWTQGNPNGKPVLYIHGGPGSGTDEGCLKYFDLETTWIILLDQRGCGKSKTNDIFYENNTDK 82
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   83 LVSDFEILRQKLNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFLRALFLAREKDWSEALMGLGKMFYPYEHQRFMDSIP 162
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  163 KAYQNsyEQIVNYCYDQFQNGDESTKEKLAKAWVDWEST-LLSPINKIHSTATDFKLVEKLALLECHYAVNKSFLD-ENF 240
Cdd:TIGR01249 161 ENERN--EQLVNAYHDRLQSGDEETKLAAAKAWVDWESTtLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDvENF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497571736  241 ILDNISVLKNKSIYLAHGRFDLICPLYQPLALKQAFPELQLYVTNNAGHSGSDANNLATIKHLLKTYL 308
Cdd:TIGR01249 239 ILDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
3-308 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 542.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736    3 TKLNVKGYLNVGDNHQLYYWTQGNPNGKPVLYIHGGPGSGTDEGCLKYFDLETTWIILLDQRGCGKSKTNDIFYENNTDK 82
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   83 LVSDFEILRQKLNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFLRALFLAREKDWSEALMGLGKMFYPYEHQRFMDSIP 162
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  163 KAYQNsyEQIVNYCYDQFQNGDESTKEKLAKAWVDWEST-LLSPINKIHSTATDFKLVEKLALLECHYAVNKSFLD-ENF 240
Cdd:TIGR01249 161 ENERN--EQLVNAYHDRLQSGDEETKLAAAKAWVDWESTtLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDvENF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497571736  241 ILDNISVLKNKSIYLAHGRFDLICPLYQPLALKQAFPELQLYVTNNAGHSGSDANNLATIKHLLKTYL 308
Cdd:TIGR01249 239 ILDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
30-289 1.39e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 91.41  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   30 KPVLYIHGGPGSGTDEGCLKYFDLETTW-IILLDQRGCGKSKTNDIFYENNTDKLVSDFEILRQKLNIKNWTLFGGSWGS 108
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFrVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  109 ALALVYAIKHPQVVDKIFLralflarekdwsealmgLGKMFYPYEHQRFMDSIPKAYQNSYEQIVNYCydqFQNGDE-ST 187
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVL-----------------LGALDPPHELDEADRFILALFPGFFDGFVADF---APNPLGrLV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  188 KEKLAKAWVDWESTLLSPiNKIHSTATDFKLVEKLALLEChyavnKSFLDENFILDNISVL--KNKSIYLAHGRFDLICP 265
Cdd:pfam00561 141 AKLLALLLLRLRLLKALP-LLNKRFPSGDYALAKSLVTGA-----LLFIETWSTELRAKFLgrLDEPTLIIWGDQDPLVP 214
                         250       260
                  ....*....|....*....|....
gi 497571736  266 LYQPLALKQAFPELQLYVTNNAGH 289
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAGH 238
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
15-127 1.31e-19

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 85.44  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  15 DNHQLYYWTQGnPNGKPVLYIHGGPGSGTD-EGCLKYFDlETTWIILLDQRGCGKSKTNDIFYenNTDKLVSDFEILRQK 93
Cdd:COG0596   10 DGVRLHYREAG-PDGPPVVLLHGLPGSSYEwRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGY--TLDDLADDLAALLDA 85
                         90       100       110
                 ....*....|....*....|....*....|....
gi 497571736  94 LNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFL 127
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVL 119
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
24-145 1.87e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 45.67  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  24 QGNPNGKPVLYIHG-GPGSGTdegCLKYFD-LETTW-IILLDQRGCGKSKTNDiFYENNTDK----LVSDFEILRQKLNI 96
Cdd:PLN02894 100 DSKEDAPTLVMVHGyGASQGF---FFRNFDaLASRFrVIAIDQLGWGGSSRPD-FTCKSTEEteawFIDSFEEWRKAKNL 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497571736  97 KNWTLFGGSWGSALALVYAIKHPQVVDKIFL--RALFLAREKDWSEALMGL 145
Cdd:PLN02894 176 SNFILLGHSFGGYVAAKYALKHPEHVQHLILvgPAGFSSESDDKSEWLTKF 226
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
3-308 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 542.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736    3 TKLNVKGYLNVGDNHQLYYWTQGNPNGKPVLYIHGGPGSGTDEGCLKYFDLETTWIILLDQRGCGKSKTNDIFYENNTDK 82
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   83 LVSDFEILRQKLNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFLRALFLAREKDWSEALMGLGKMFYPYEHQRFMDSIP 162
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  163 KAYQNsyEQIVNYCYDQFQNGDESTKEKLAKAWVDWEST-LLSPINKIHSTATDFKLVEKLALLECHYAVNKSFLD-ENF 240
Cdd:TIGR01249 161 ENERN--EQLVNAYHDRLQSGDEETKLAAAKAWVDWESTtLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDvENF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497571736  241 ILDNISVLKNKSIYLAHGRFDLICPLYQPLALKQAFPELQLYVTNNAGHSGSDANNLATIKHLLKTYL 308
Cdd:TIGR01249 239 ILDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
30-289 1.39e-21

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 91.41  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   30 KPVLYIHGGPGSGTDEGCLKYFDLETTW-IILLDQRGCGKSKTNDIFYENNTDKLVSDFEILRQKLNIKNWTLFGGSWGS 108
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFrVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  109 ALALVYAIKHPQVVDKIFLralflarekdwsealmgLGKMFYPYEHQRFMDSIPKAYQNSYEQIVNYCydqFQNGDE-ST 187
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVL-----------------LGALDPPHELDEADRFILALFPGFFDGFVADF---APNPLGrLV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  188 KEKLAKAWVDWESTLLSPiNKIHSTATDFKLVEKLALLEChyavnKSFLDENFILDNISVL--KNKSIYLAHGRFDLICP 265
Cdd:pfam00561 141 AKLLALLLLRLRLLKALP-LLNKRFPSGDYALAKSLVTGA-----LLFIETWSTELRAKFLgrLDEPTLIIWGDQDPLVP 214
                         250       260
                  ....*....|....*....|....
gi 497571736  266 LYQPLALKQAFPELQLYVTNNAGH 289
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAGH 238
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
15-127 1.31e-19

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 85.44  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  15 DNHQLYYWTQGnPNGKPVLYIHGGPGSGTD-EGCLKYFDlETTWIILLDQRGCGKSKTNDIFYenNTDKLVSDFEILRQK 93
Cdd:COG0596   10 DGVRLHYREAG-PDGPPVVLLHGLPGSSYEwRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGY--TLDDLADDLAALLDA 85
                         90       100       110
                 ....*....|....*....|....*....|....
gi 497571736  94 LNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFL 127
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVL 119
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
7-289 1.53e-18

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 83.58  E-value: 1.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736    7 VKGYLNVGDNHQLYYWTQGNPNGKPVLYIHGGPGSGTD--EGCLKYFDLETTWIILLDQRGCGKSKTNDIFYEN--NTDK 82
Cdd:TIGR01250   3 IEGIITVDGGYHLFTKTGGEGEKIKLLLLHGGPGMSHEylENLRELLKEEGREVIMYDQLGCGYSDQPDDSDEElwTIDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   83 LVSDFEILRQKLNIKNWTLFGGSWGSALALVYAIKHPQvvdkiFLRALFLAREKD----WSEALMGLGKMFyPYEHQRFM 158
Cdd:TIGR01250  83 FVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQ-----HLKGLIISSMLDsapeYVKELNRLRKEL-PPEVRAAI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  159 DSIPKA--YQNS-YEQIVNYCYDQFQNGDESTKEKLAKAwvdwESTLLSPINKIHSTATDFKLVEKLALLEChyaVNKsf 235
Cdd:TIGR01250 157 KRCEASgdYDNPeYQEAVEVFYHHLLCRLRKWPEALKHL----KSGGNTNVYNIMQGPNEFTITGNLKDWDI---TDK-- 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 497571736  236 ldenfiLDNISVlknkSIYLAHGRFDLiCPLYQPLALKQAFPELQLYVTNNAGH 289
Cdd:TIGR01250 228 ------LSEIKV----PTLLTVGEFDT-MTPEAAREMQELIAGSRLVVFPDGSH 270
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-127 5.29e-08

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 52.31  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   1 MNTKLnvkGYLNVGDNHQLYY--WTQGNPNGKPVLYIHGGpgsgtDEGCLKYFDLETTW------IILLDQRGCGKSkTN 72
Cdd:COG2267    1 MTRRL---VTLPTRDGLRLRGrrWRPAGSPRGTVVLVHGL-----GEHSGRYAELAEALaaagyaVLAFDLRGHGRS-DG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497571736  73 DIFYENNTDKLVSDF----EILRQKLNIKnWTLFGGSWGSALALVYAIKHPQVVDKIFL 127
Cdd:COG2267   72 PRGHVDSFDDYVDDLraalDALRARPGLP-VVLLGHSMGGLIALLYAARYPDRVAGLVL 129
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
24-145 1.87e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 45.67  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  24 QGNPNGKPVLYIHG-GPGSGTdegCLKYFD-LETTW-IILLDQRGCGKSKTNDiFYENNTDK----LVSDFEILRQKLNI 96
Cdd:PLN02894 100 DSKEDAPTLVMVHGyGASQGF---FFRNFDaLASRFrVIAIDQLGWGGSSRPD-FTCKSTEEteawFIDSFEEWRKAKNL 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497571736  97 KNWTLFGGSWGSALALVYAIKHPQVVDKIFL--RALFLAREKDWSEALMGL 145
Cdd:PLN02894 176 SNFILLGHSFGGYVAAKYALKHPEHVQHLILvgPAGFSSESDDKSEWLTKF 226
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
61-127 2.20e-05

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 44.90  E-value: 2.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497571736   61 LDQRGCGKS--KTNDIfyeNNTDKLVSD----FEILRQKLNIKNWTLFGGSWGSALALVYAIKHPQVVDKIFL 127
Cdd:pfam12146  37 YDHRGHGRSdgKRGHV---PSFDDYVDDldtfVDKIREEHPGLPLFLLGHSMGGLIAALYALRYPDKVDGLIL 106
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
15-145 8.41e-05

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 43.08  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736  15 DNHQLYYWTQGNPNGKP---VLYIHGGPGSGTDegclkYFDLETTW-------IILLDQRGCGKSkTNDIFYENNTDkLV 84
Cdd:COG1506    6 DGTTLPGWLYLPADGKKypvVVYVHGGPGSRDD-----SFLPLAQAlasrgyaVLAPDYRGYGES-AGDWGGDEVDD-VL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497571736  85 SDFEILRQKLNI--KNWTLFGGSWGSALALVYAIKHPQVVDKIFLRA------LFLAREKDWSEALMGL 145
Cdd:COG1506   79 AAIDYLAARPYVdpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAgvsdlrSYYGTTREYTERLMGG 147
Peptidase_S28 pfam05577
Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as ...
21-123 8.25e-03

Serine carboxypeptidase S28; These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-peptidase II, and thymus-specific serine peptidase.


Pssm-ID: 310284  Cd Length: 434  Bit Score: 37.74  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497571736   21 YWTQGNPNgkpVLYIHG-GPGSGTDEGCLKYFDLETTW---IILLDQRGCGKSK-TNDIFYEN----NTDKLVSDFEILR 91
Cdd:pfam05577  24 HYRNGGPI---FLMIGGeGPESASWVRNGHWLDLAKEFgalVFSLEHRFYGQSRpIGDLSTENlrylSSLQALADLASFI 100
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 497571736   92 QKLNIK-------NWTLFGGSWGSALALVYAIKHPQVVD 123
Cdd:pfam05577 101 KAMNQKfnglsssKWITFGGSYSGSLAAWFRKKYPHLVV 139
 
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.
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