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Conserved domains on  [gi|495966624|ref|WP_008691203|]
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MULTISPECIES: S9 family peptidase [Longicatena]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 11445445)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  12369917

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
165-417 2.94e-22

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


:

Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 95.08  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 165 GGNIKGYLCTPEKGDKFPVVILLGGsGPSDHNETignqkpFYELAKELGKQGIATYRFDKRtleNTFTQTDTIQQEYIED 244
Cdd:COG1506    7 GTTLPGWLYLPADGKKYPVVVYVHG-GPGSRDDS------FLPLAQALASRGYAVLAPDYR---GYGESAGDWGGDEVDD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 245 ALSAIQLMQQQKQIDKQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAAPSrpiedSMVEQLTylakldgkvdaeeqkq 323
Cdd:COG1506   77 VLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLaAARHPDRFKAAVALAGVS-----DLRSYYG---------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 324 ldeaetvrkqikqiaSSKHDDTLYLGMTRAYLMDLATYDPVKTAEKIQVPVLLCQGLRDYQVTKTDLKRWQQAFAEK-AN 402
Cdd:COG1506  136 ---------------TTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgKP 200
                        250
                 ....*....|....*
gi 495966624 403 WTIRTYATANHAMSK 417
Cdd:COG1506  201 VELLVYPGEGHGFSG 215
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
165-417 2.94e-22

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 95.08  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 165 GGNIKGYLCTPEKGDKFPVVILLGGsGPSDHNETignqkpFYELAKELGKQGIATYRFDKRtleNTFTQTDTIQQEYIED 244
Cdd:COG1506    7 GTTLPGWLYLPADGKKYPVVVYVHG-GPGSRDDS------FLPLAQALASRGYAVLAPDYR---GYGESAGDWGGDEVDD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 245 ALSAIQLMQQQKQIDKQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAAPSrpiedSMVEQLTylakldgkvdaeeqkq 323
Cdd:COG1506   77 VLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLaAARHPDRFKAAVALAGVS-----DLRSYYG---------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 324 ldeaetvrkqikqiaSSKHDDTLYLGMTRAYLMDLATYDPVKTAEKIQVPVLLCQGLRDYQVTKTDLKRWQQAFAEK-AN 402
Cdd:COG1506  136 ---------------TTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgKP 200
                        250
                 ....*....|....*
gi 495966624 403 WTIRTYATANHAMSK 417
Cdd:COG1506  201 VELLVYPGEGHGFSG 215
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
183-415 4.35e-09

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: 56.84  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  183 VVILLGGsgpsdHNETIGNqkpFYELAKELGKQGIATYRFD---------KRTLENTFTQtdtiqqeYIEDALSAIQLMQ 253
Cdd:pfam12146   6 VVVLVHG-----LGEHSGR---YAHLADALAAQGFAVYAYDhrghgrsdgKRGHVPSFDD-------YVDDLDTFVDKIR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  254 QQKQIdkQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAAPSRPIEDSMVEQLTYLAKLDGKV---------------- 316
Cdd:pfam12146  71 EEHPG--LPLFLLGHSMGGLIAALyALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLfprlrvpnnllpdsls 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  317 -DAEEQKQLDEaetvrkqikqiasskhdDTLYLGMTRA-YLMDL--ATYDPVKTAEKIQVPVLLCQGLRDyQVTKTDLkr 392
Cdd:pfam12146 149 rDPEVVAAYAA-----------------DPLVHGGISArTLYELldAGERLLRRAAAITVPLLLLHGGAD-RVVDPAG-- 208
                         250       260
                  ....*....|....*....|...
gi 495966624  393 wQQAFAEKANWTIRTYATANHAM 415
Cdd:pfam12146 209 -SREFYERAGSTDKTLKLYPGLY 230
 
Name Accession Description Interval E-value
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
165-417 2.94e-22

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 95.08  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 165 GGNIKGYLCTPEKGDKFPVVILLGGsGPSDHNETignqkpFYELAKELGKQGIATYRFDKRtleNTFTQTDTIQQEYIED 244
Cdd:COG1506    7 GTTLPGWLYLPADGKKYPVVVYVHG-GPGSRDDS------FLPLAQALASRGYAVLAPDYR---GYGESAGDWGGDEVDD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 245 ALSAIQLMQQQKQIDKQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAAPSrpiedSMVEQLTylakldgkvdaeeqkq 323
Cdd:COG1506   77 VLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLaAARHPDRFKAAVALAGVS-----DLRSYYG---------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 324 ldeaetvrkqikqiaSSKHDDTLYLGMTRAYLMDLATYDPVKTAEKIQVPVLLCQGLRDYQVTKTDLKRWQQAFAEK-AN 402
Cdd:COG1506  136 ---------------TTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgKP 200
                        250
                 ....*....|....*
gi 495966624 403 WTIRTYATANHAMSK 417
Cdd:COG1506  201 VELLVYPGEGHGFSG 215
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
154-415 2.21e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 80.82  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 154 KQKEMDLKIATGGNIKGYLCTPEKGDKfPVVILLGGSGpsDHNETignqkpFYELAKELGKQGIATYRFDKR-------- 225
Cdd:COG2267    2 TRRLVTLPTRDGLRLRGRRWRPAGSPR-GTVVLVHGLG--EHSGR------YAELAEALAAAGYAVLAFDLRghgrsdgp 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 226 -TLENTFtqtdtiqQEYIEDALSAIQLMQQQkqiDKQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAapSRPIEDSmv 303
Cdd:COG2267   73 rGHVDSF-------DDYVDDLRAALDALRAR---PGLPVVLLGHSMGGLIALLyAARYPDRVAGLVLLA--PAYRADP-- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 304 eqltylakldgkvdaeeqkqldeaetvrkqikqiasskhddtlYLGMTRAYLMDLATYDpvkTAEKIQVPVLLCQGLRDY 383
Cdd:COG2267  139 -------------------------------------------LLGPSARWLRALRLAE---ALARIDVPVLVLHGGADR 172
                        250       260       270
                 ....*....|....*....|....*....|..
gi 495966624 384 QVTKTDLKRWQQAFAEKAnwTIRTYATANHAM 415
Cdd:COG2267  173 VVPPEAARRLAARLSPDV--ELVLLPGARHEL 202
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
153-431 6.57e-15

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 73.85  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 153 IKQKEMDLKIATGGNIKGYLCTPEKGDKFPVVILL-GGSGPSDHNETIGNQkpfyeLAKE---------LGKQGIATYRF 222
Cdd:COG0412    1 MTTETVTIPTPDGVTLPGYLARPAGGGPRPGVVVLhEIFGLNPHIRDVARR-----LAAAgyvvlapdlYGRGGPGDDPD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 223 DKRTLENTFTqtdtiQQEYIEDALSAIQLMQQQKQIDKQRIYVLGHSQGGYIlprlneqtkdvagyIFMAAPSRPiedsm 302
Cdd:COG0412   76 EARALMGALD-----PELLAADLRAALDWLKAQPEVDAGRVGVVGFCFGGGL--------------ALLAAARGP----- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 303 veqltylakldgKVDAeeqkqldeaeTVrkqikqiasskhddTLYLGMTRAYLMDLatydpvktAEKIQVPVLLCQGLRD 382
Cdd:COG0412  132 ------------DLAA----------AV--------------SFYGGLPADDLLDL--------AARIKAPVLLLYGEKD 167
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 495966624 383 YQVTKTDLKRWQQAFAE-KANWTIRTYATANHAMskgsEQPSPKDYNQEA 431
Cdd:COG0412  168 PLVPPEQVAALEAALAAaGVDVELHVYPGAGHGF----TNPGRPRYDPAA 213
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
183-415 4.35e-09

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: 56.84  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  183 VVILLGGsgpsdHNETIGNqkpFYELAKELGKQGIATYRFD---------KRTLENTFTQtdtiqqeYIEDALSAIQLMQ 253
Cdd:pfam12146   6 VVVLVHG-----LGEHSGR---YAHLADALAAQGFAVYAYDhrghgrsdgKRGHVPSFDD-------YVDDLDTFVDKIR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  254 QQKQIdkQRIYVLGHSQGGYILPR-LNEQTKDVAGYIFMAAPSRPIEDSMVEQLTYLAKLDGKV---------------- 316
Cdd:pfam12146  71 EEHPG--LPLFLLGHSMGGLIAALyALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLLGKLfprlrvpnnllpdsls 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  317 -DAEEQKQLDEaetvrkqikqiasskhdDTLYLGMTRA-YLMDL--ATYDPVKTAEKIQVPVLLCQGLRDyQVTKTDLkr 392
Cdd:pfam12146 149 rDPEVVAAYAA-----------------DPLVHGGISArTLYELldAGERLLRRAAAITVPLLLLHGGAD-RVVDPAG-- 208
                         250       260
                  ....*....|....*....|...
gi 495966624  393 wQQAFAEKANWTIRTYATANHAM 415
Cdd:pfam12146 209 -SREFYERAGSTDKTLKLYPGLY 230
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
182-385 5.74e-09

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 56.49  E-value: 5.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 182 PVVILLGG--SGPSDhnetignqkpFYELAKELGKQGIATYRFDKR---TLENTFTQTDTiqQEYIEDALSAIQLMQQQK 256
Cdd:COG1647   16 KGVLLLHGftGSPAE----------MRPLAEALAKAGYTVYAPRLPghgTSPEDLLKTTW--EDWLEDVEEAYEILKAGY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 257 QidkqRIYVLGHSQGGYILPRLNEQTKDVAGYIFMAAPSRPIEDSMVEQ--LTYLAK-LDGKVDAEEQKQLDEAETVRKQ 333
Cdd:COG1647   84 D----KVIVIGLSMGGLLALLLAARYPDVAGLVLLSPALKIDDPSAPLLplLKYLARsLRGIGSDIEDPEVAEYAYDRTP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495966624 334 IKQIASSkhddTLYLGMTRAYLmdlatydpvktaEKIQVPVLLCQGLRDYQV 385
Cdd:COG1647  160 LRALAEL----QRLIREVRRDL------------PKITAPTLIIQSRKDEVV 195
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
182-299 2.20e-04

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: 42.49  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624  182 PVVILLGGsGPSDHNEtignqkpFYELAKELGKQGIATYRFDKRTlentFTQTDTI--QQEYIEDALSAIQLMQQQKqID 259
Cdd:pfam00561   1 PPVLLLHG-LPGSSDL-------WRKLAPALARDGFRVIALDLRG----FGKSSRPkaQDDYRTDDLAEDLEYILEA-LG 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 495966624  260 KQRIYVLGHSQGGYILPRLNEQTKD-VAGYIFMAAPSRPIE 299
Cdd:pfam00561  68 LEKVNLVGHSMGGLIALAYAAKYPDrVKALVLLGALDPPHE 108
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
178-273 3.52e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 42.40  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 178 GDKFPVVILLGGSGPSDHNetignqkpFYELAKELGKQGIA---------TYRFDKRTLENTFTQTDTiqQEYIE----- 243
Cdd:COG4188   59 GGPFPLVVLSHGLGGSREG--------YAYLAEHLASHGYVvaapdhpgsNAADLSAALDGLADALDP--EELWErpldl 128
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495966624 244 ----DALSAIQLMQQ--QKQIDKQRIYVLGHSQGGY 273
Cdd:COG4188  129 sfvlDQLLALNKSDPplAGRLDLDRIGVIGHSLGGY 164
COG4099 COG4099
Predicted peptidase [General function prediction only];
163-273 5.49e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 41.49  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 163 ATGGNIKGYLCTPE---KGDKFPVVILLGGSG--PSDHNETIGNQKPFYELAKELGKQG---IA-TYRFDKrtlenTFTQ 233
Cdd:COG4099   28 SDGDTLPYRLYLPKgydPGKKYPLVLFLHGAGerGTDNEKQLTHGAPKFINPENQAKFPaivLApQCPEDD-----YWSD 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495966624 234 TDtiqqeYIEDALSAIQLMQQQKQIDKQRIYVLGHSQGGY 273
Cdd:COG4099  103 TK-----ALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGY 137
YpfH COG0400
Predicted esterase [General function prediction only];
182-274 2.77e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 182 PVVILLGGSGpsdhnetiGNQKPFYELAKELGKQGI------ATYR--------FDKRTLENTFTQTDTIQ-QEYIEDAL 246
Cdd:COG0400    6 PLVVLLHGYG--------GDEEDLLPLAPELALPGAavlaprAPVPegpggrawFDLSFLEGREDEEGLAAaAEALAAFI 77
                         90       100
                 ....*....|....*....|....*...
gi 495966624 247 SAIQlmqQQKQIDKQRIYVLGHSQGGYI 274
Cdd:COG0400   78 DELE---ARYGIDPERIVLAGFSQGAAM 102
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
172-274 5.24e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.93  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 172 LCTPEKG-DKFPVVILL-GG---SGPSDHNETIGNqkpfyELAKElgkQGIAT----YRfdkRTLENTFTQTdtiqqeyI 242
Cdd:COG0657    3 VYRPAGAkGPLPVVVYFhGGgwvSGSKDTHDPLAR-----RLAAR---AGAAVvsvdYR---LAPEHPFPAA-------L 64
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495966624 243 EDALSAIQLMQQQKQ---IDKQRIYVLGHSQGGYI 274
Cdd:COG0657   65 EDAYAALRWLRANAAelgIDPDRIAVAGDSAGGHL 99
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
184-296 7.94e-03

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 35.96  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495966624 184 VILLGGsgpsdhneTIGNQKPFYELAKELGKQGIATYRFDKRTLENTftqtdtiqqeyIEDalSAIQLMQQQKQIDK--- 260
Cdd:COG1075    8 VVLVHG--------LGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS-----------IED--SAEQLAAFVDAVLAatg 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495966624 261 -QRIYVLGHSQGGyILPRL----NEQTKDVAGYIFMAAPSR 296
Cdd:COG1075   67 aEKVDLVGHSMGG-LVARYylkrLGGAAKVARVVTLGTPHH 106
 
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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