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Conserved domains on  [gi|186478297|ref|NP_001117254|]
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Metallopeptidase M24 family protein [Arabidopsis thaliana]

Protein Classification

aminopeptidase P family protein( domain architecture ID 10525081)

aminopeptidase family protein P (peptidase M24) cleaves amido-, imido- or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
186-417 4.09e-109

Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.


:

Pssm-ID: 238520 [Multi-domain]  Cd Length: 243  Bit Score: 322.60  E-value: 4.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 186 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 265
Cdd:cd01087    1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 266 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 338
Cdd:cd01087   80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 339 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 413
Cdd:cd01087  160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                 ....
gi 186478297 414 VLTG 417
Cdd:cd01087  240 NLTR 243
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
26-142 1.93e-42

Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.


:

Pssm-ID: 461581 [Multi-domain]  Cd Length: 121  Bit Score: 146.11  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297   26 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 101
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 186478297  102 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 142
Cdd:pfam05195  81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
 
Name Accession Description Interval E-value
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
186-417 4.09e-109

Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.


Pssm-ID: 238520 [Multi-domain]  Cd Length: 243  Bit Score: 322.60  E-value: 4.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 186 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 265
Cdd:cd01087    1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 266 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 338
Cdd:cd01087   80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 339 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 413
Cdd:cd01087  160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                 ....
gi 186478297 414 VLTG 417
Cdd:cd01087  240 NLTR 243
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
24-430 2.18e-93

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 289.32  E-value: 2.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  24 EEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL--SDE--RGLCMFmpeSTPKD 99
Cdd:PRK10879   4 QEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLikSDDthNHSVLF---NRVRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 100 IA---WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHnvqsASQRYTNLDDFQNSAsLGKVKTLS----- 171
Cdd:PRK10879  81 LTaeiWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYH----AQGEYAYADEIVFSA-LEKLRKGSrqnlt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 172 ---SLT------HELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGS 242
Cdd:PRK10879 156 apaTLTdwrpwvHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 243 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYS 322
Cdd:PRK10879 236 NGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 323 TELLCDGLMKMGILK-------SRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSSFDCPER 393
Cdd:PRK10879 316 VRIMVSGLVKLGILKgdvdqliAENAHRPFFMHGLSHWLGLDVHDVGVYGQDrsRILEPGMVLTVEPGLYIAPDADVPEQ 395
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 186478297 394 FQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLL 430
Cdd:PRK10879 396 YRGIGIRIEDDIVITETGNENLTASVVKKPDEIEALM 432
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
165-426 2.66e-76

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 240.49  E-value: 2.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 165 GKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVRGAQRMAFNPVVGG 240
Cdd:COG0006   58 RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALR----PGVtereVAAELEAAMRRRGAEGPSFDTIVAS 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 241 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNt 320
Cdd:COG0006  134 GENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTV-AVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 321 ystELLCDGLMKMGilksrrlYHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiG 398
Cdd:COG0006  212 ---AAARDVLAEAG-------YGEYFPHGTGHGVGLDVHEgpQISPGNDRPLEPGMVFTIEPGIYIPGIG---------G 272
                        250       260
                 ....*....|....*....|....*...
gi 186478297 399 IRIEDDVLITETGYEVLTGsMPKEIKHI 426
Cdd:COG0006  273 VRIEDTVLVTEDGAEVLTR-LPRELLEL 299
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
187-409 6.28e-58

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 189.76  E-value: 6.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  187 KLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVR-GAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 261
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIR----PGVtereLAAELEAARLRRgGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  262 VLMDMGCEL-HGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNtystELLCDGLMKMGilksrr 340
Cdd:pfam00557  77 VLIDVGAEYdGGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVD----AAAREVLEEAG------ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478297  341 lYHQLNPTSIGHYLGMDVHDSSAVGY---DRPLQPGFVITIEPGVYIPssfdcPERFqgiGIRIEDDVLITE 409
Cdd:pfam00557 146 -LGEYFPHGLGHGIGLEVHEGPYISRggdDRVLEPGMVFTIEPGIYFI-----PGWG---GVRIEDTVLVTE 208
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
26-142 1.93e-42

Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.


Pssm-ID: 461581 [Multi-domain]  Cd Length: 121  Bit Score: 146.11  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297   26 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 101
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 186478297  102 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 142
Cdd:pfam05195  81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
AMP_N smart01011
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
21-145 1.13e-37

Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.


Pssm-ID: 198079  Cd Length: 135  Bit Score: 133.90  E-value: 1.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297    21 IRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERG---LCMFMPESTP 97
Cdd:smart01011   1 IPAAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLDPSGGggkSTLFVPPRDP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 186478297    98 KDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNV 145
Cdd:smart01011  81 EDELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLL 128
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
180-416 8.60e-15

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 73.92  E-value: 8.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  180 IKSPAELKLMRESASIACQGLLktMLHSKGFPdeGILSAQVEYECRVRGAQRMA---------FNPVVGGGSNASVIHYS 250
Cdd:TIGR00500   3 LKSPDEIEKIRKAGRLAAEVLE--ELEREVKP--GVSTKELDRIAKDFIEKHGAkpaflgyygFPGSVCISVNEVVIHGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  251 RNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQLN----TYS 322
Cdd:TIGR00500  79 PDKKVLKDGDIVNIDVGVIYDGYHGDTAKTF-LVGKISPEAEKL----LECTEESlykaIEEAKPGNRIGEIGaaiqKYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  323 TELLCDGLMKMGilksrrlyhqlnptsiGHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPSSFDcpeRFQG 396
Cdd:TIGR00500 154 EAKGFSVVREYC----------------GHGIGRKFHEEPQIpNYGKKftnvrLKEGMVFTIEPMVNTGTEEI---TTAA 214
                         250       260       270
                  ....*....|....*....|....*....|.
gi 186478297  397 IG-----------IRIEDDVLITETGYEVLT 416
Cdd:TIGR00500 215 DGwtvktkdgslsAQFEHTIVITDNGPEILT 245
 
Name Accession Description Interval E-value
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
186-417 4.09e-109

Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.


Pssm-ID: 238520 [Multi-domain]  Cd Length: 243  Bit Score: 322.60  E-value: 4.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 186 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 265
Cdd:cd01087    1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 266 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 338
Cdd:cd01087   80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 339 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 413
Cdd:cd01087  160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                 ....
gi 186478297 414 VLTG 417
Cdd:cd01087  240 NLTR 243
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
24-430 2.18e-93

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 289.32  E-value: 2.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  24 EEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL--SDE--RGLCMFmpeSTPKD 99
Cdd:PRK10879   4 QEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLikSDDthNHSVLF---NRVRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 100 IA---WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHnvqsASQRYTNLDDFQNSAsLGKVKTLS----- 171
Cdd:PRK10879  81 LTaeiWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYH----AQGEYAYADEIVFSA-LEKLRKGSrqnlt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 172 ---SLT------HELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGS 242
Cdd:PRK10879 156 apaTLTdwrpwvHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 243 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYS 322
Cdd:PRK10879 236 NGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 323 TELLCDGLMKMGILK-------SRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSSFDCPER 393
Cdd:PRK10879 316 VRIMVSGLVKLGILKgdvdqliAENAHRPFFMHGLSHWLGLDVHDVGVYGQDrsRILEPGMVLTVEPGLYIAPDADVPEQ 395
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 186478297 394 FQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLL 430
Cdd:PRK10879 396 YRGIGIRIEDDIVITETGNENLTASVVKKPDEIEALM 432
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
165-426 2.66e-76

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 240.49  E-value: 2.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 165 GKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVRGAQRMAFNPVVGG 240
Cdd:COG0006   58 RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALR----PGVtereVAAELEAAMRRRGAEGPSFDTIVAS 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 241 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNt 320
Cdd:COG0006  134 GENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTV-AVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 321 ystELLCDGLMKMGilksrrlYHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiG 398
Cdd:COG0006  212 ---AAARDVLAEAG-------YGEYFPHGTGHGVGLDVHEgpQISPGNDRPLEPGMVFTIEPGIYIPGIG---------G 272
                        250       260
                 ....*....|....*....|....*...
gi 186478297 399 IRIEDDVLITETGYEVLTGsMPKEIKHI 426
Cdd:COG0006  273 VRIEDTVLVTEDGAEVLTR-LPRELLEL 299
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
187-409 6.28e-58

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 189.76  E-value: 6.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  187 KLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVR-GAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 261
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIR----PGVtereLAAELEAARLRRgGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  262 VLMDMGCEL-HGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNtystELLCDGLMKMGilksrr 340
Cdd:pfam00557  77 VLIDVGAEYdGGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVD----AAAREVLEEAG------ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478297  341 lYHQLNPTSIGHYLGMDVHDSSAVGY---DRPLQPGFVITIEPGVYIPssfdcPERFqgiGIRIEDDVLITE 409
Cdd:pfam00557 146 -LGEYFPHGLGHGIGLEVHEGPYISRggdDRVLEPGMVFTIEPGIYFI-----PGWG---GVRIEDTVLVTE 208
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
186-412 2.13e-49

Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.


Pssm-ID: 238525 [Multi-domain]  Cd Length: 208  Bit Score: 167.69  E-value: 2.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 186 LKLMRESASIACqgllKTMLHSKGFPDEGI----LSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 261
Cdd:cd01092    1 IELLRKAARIAD----KAFEELLEFIKPGMtereVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 262 VLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLcdglmkmgilkSRRL 341
Cdd:cd01092   77 VLIDFGAIYDGYCSDITRTV-AVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVI-----------EEAG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186478297 342 YHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiGIRIEDDVLITETGY 412
Cdd:cd01092  145 YGEYFIHRTGHGVGLEVHEapYISPGSDDVLEEGMVFTIEPGIYIPGKG---------GVRIEDDVLVTEDGC 208
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
26-142 1.93e-42

Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.


Pssm-ID: 461581 [Multi-domain]  Cd Length: 121  Bit Score: 146.11  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297   26 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 101
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 186478297  102 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 142
Cdd:pfam05195  81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
AMP_N smart01011
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
21-145 1.13e-37

Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.


Pssm-ID: 198079  Cd Length: 135  Bit Score: 133.90  E-value: 1.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297    21 IRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERG---LCMFMPESTP 97
Cdd:smart01011   1 IPAAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLDPSGGggkSTLFVPPRDP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 186478297    98 KDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNV 145
Cdd:smart01011  81 EDELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLL 128
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
186-412 8.47e-36

A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.


Pssm-ID: 238514 [Multi-domain]  Cd Length: 207  Bit Score: 131.42  E-value: 8.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 186 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQrMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 265
Cdd:cd01066    1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGY-PAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 266 MGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLntysTELLCDGLmkmgilkSRRLYHQL 345
Cdd:cd01066   80 LGGVYDGYHADLTRTF-VIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEV----DAAAREVL-------EEHGLGPN 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478297 346 NPTSIGHYLGMDVHDSSAV--GYDRPLQPGFVITIEPGVYIPssfdcperfQGIGIRIEDDVLITETGY 412
Cdd:cd01066  148 FGHRTGHGIGLEIHEPPVLkaGDDTVLEPGMVFAVEPGLYLP---------GGGGVRIEDTVLVTEDGP 207
PRK09795 PRK09795
aminopeptidase; Provisional
166-423 8.40e-30

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 119.27  E-value: 8.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 166 KVKTLSSLTHELRLIKSPAELKLMRESASIACQGllktMLHSKGFPDEGI----LSAQVEYECRVRGAQRMAFNPVVGGG 241
Cdd:PRK09795 113 NAKLVSATPDVLRQIKTPEEVEKIRLACGIADRG----AEHIRRFIQAGMsereIAAELEWFMRQQGAEKASFDTIVASG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 242 SNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEE----LYDLILQTNKECIKQCKPGTTIRQ 317
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAESHplfnVYQIVLQAQLAAISAIRPGVRCQQ 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 318 LNTYSTELLcdglmkmgilkSRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSsfdcperfQ 395
Cdd:PRK09795 269 VDDAARRVI-----------TEAGYGDYFGHNTGHAIGIEVHEDPRFSPRdtTTLQPGMLLTVEPGIYLPG--------Q 329
                        250       260
                 ....*....|....*....|....*...
gi 186478297 396 GiGIRIEDDVLITETGYEVLTgSMPKEI 423
Cdd:PRK09795 330 G-GVRIEDVVLVTPQGAEVLY-AMPKTV 355
PRK13607 PRK13607
proline dipeptidase; Provisional
175-416 1.14e-20

proline dipeptidase; Provisional


Pssm-ID: 237444 [Multi-domain]  Cd Length: 443  Bit Score: 93.81  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 175 HELRLIKSPAELKLMRESASIACQGllktmlH--SKgfpdEGILSAQVEYECRVR-------GAQRMAFNPVVGGGSNAS 245
Cdd:PRK13607 156 HYHRAYKTDYELACMREAQKIAVAG------HraAK----EAFRAGMSEFDINLAyltatgqRDNDVPYGNIVALNEHAA 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 246 VIHYSRNDQRIKDGDL-VLMDMGCELHGYVSDLTRTWPpcgkfSSVQEELYDLILQTNKE---CIKQCKPGTTIRQLNTY 321
Cdd:PRK13607 226 VLHYTKLDHQAPAEMRsFLIDAGAEYNGYAADITRTYA-----AKEDNDFAALIKDVNKEqlaLIATMKPGVSYVDLHIQ 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 322 STELLcdglmkMGILKSRRLYHQLNP--------TS------IGHYLGMDVHDSSAVGYD------------------RP 369
Cdd:PRK13607 301 MHQRI------AKLLRKFQIVTGLSEeamveqgiTSpffphgLGHPLGLQVHDVAGFMQDdrgthlaapekhpylrctRV 374
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478297 370 LQPGFVITIEPGVY-IPSSFDcP----ERFQGI------------GIRIEDDVLITETGYEVLT 416
Cdd:PRK13607 375 LEPGMVLTIEPGLYfIDSLLA-PlregPFSKHFnwqkidalkpfgGIRIEDNVVVHENGVENMT 437
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
201-411 2.22e-17

X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.


Pssm-ID: 238518 [Multi-domain]  Cd Length: 224  Bit Score: 80.68  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 201 LKTMLHSKGFPDEGILSAQVEYecrVRGAQRM----AFNPVVGGGSNASVIHYSRNDQ---RIKDGDLVLMDMGCELHGY 273
Cdd:cd01085   20 LEQEVPKGETITELSAADKLEE---FRRQQKGyvglSFDTISGFGPNGAIVHYSPTEEsnrKISPDGLYLIDSGGQYLDG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 274 VSDLTRTWPpCGKFSSVQEELYDLILQTNKECIKQCKP-GTTIRQLntystellcDGLMKMGILKSRRLY-----Hqlnp 347
Cdd:cd01085   97 TTDITRTVH-LGEPTAEQKRDYTLVLKGHIALARAKFPkGTTGSQL---------DALARQPLWKAGLDYghgtgH---- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478297 348 tSIGHYLGmdVHDS----SAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiGIRIEDDVLITETG 411
Cdd:cd01085  163 -GVGSFLN--VHEGpqsiSPAPNNVPLKAGMILSNEPGYYKEGKY---------GIRIENLVLVVEAE 218
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
180-416 8.60e-15

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 73.92  E-value: 8.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  180 IKSPAELKLMRESASIACQGLLktMLHSKGFPdeGILSAQVEYECRVRGAQRMA---------FNPVVGGGSNASVIHYS 250
Cdd:TIGR00500   3 LKSPDEIEKIRKAGRLAAEVLE--ELEREVKP--GVSTKELDRIAKDFIEKHGAkpaflgyygFPGSVCISVNEVVIHGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  251 RNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQLN----TYS 322
Cdd:TIGR00500  79 PDKKVLKDGDIVNIDVGVIYDGYHGDTAKTF-LVGKISPEAEKL----LECTEESlykaIEEAKPGNRIGEIGaaiqKYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  323 TELLCDGLMKMGilksrrlyhqlnptsiGHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPSSFDcpeRFQG 396
Cdd:TIGR00500 154 EAKGFSVVREYC----------------GHGIGRKFHEEPQIpNYGKKftnvrLKEGMVFTIEPMVNTGTEEI---TTAA 214
                         250       260       270
                  ....*....|....*....|....*....|.
gi 186478297  397 IG-----------IRIEDDVLITETGYEVLT 416
Cdd:TIGR00500 215 DGwtvktkdgslsAQFEHTIVITDNGPEILT 245
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
243-416 6.37e-14

Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238519 [Multi-domain]  Cd Length: 238  Bit Score: 70.98  E-value: 6.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 243 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQL 318
Cdd:cd01086   63 NEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTF-IVGEVSEEAKKL----VEVTEEAlykgIEAVKPGNRIGDI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 319 ----NTYstellcdglmkmgiLKSRRLYhqLNPTSIGHYLGMDVHDSSAV------GYDRPLQPGFVITIEPGVYIPSSF 388
Cdd:cd01086  138 ghaiEKY--------------AEKNGYS--VVREFGGHGIGRKFHEEPQIpnygrpGTGPKLKPGMVFTIEPMINLGTYE 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 186478297 389 dcperfqgigIRIEDD------------------VLITETGYEVLT 416
Cdd:cd01086  202 ----------VVTLPDgwtvvtkdgslsaqfehtVLITEDGPEILT 237
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
180-416 2.19e-12

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 66.95  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 180 IKSPAELKLMRESASIACQGL--LKTMLHskgfpdEGI----LSAQVEYECRVRGAQrmafnpvvgggsnASVIHY---- 249
Cdd:COG0024    3 IKTPEEIEKMREAGRIVAEVLdeLAEAVK------PGVttleLDRIAEEFIRDHGAI-------------PAFLGYygfp 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 250 -----SRNDQ---------RIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKfssVQEELYDLIlQTNKEC----IKQCKP 311
Cdd:COG0024   64 ksictSVNEVvvhgipsdrVLKDGDIVNIDVGAILDGYHGDSARTF-VVGE---VSPEARRLV-EVTEEAlyagIAAAKP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 312 GTTIRQL----------NTYS--TELlcdglmkmgilksrrlyhqlnptsIGHYLGMDVHDSSAV-GYDRP-----LQPG 373
Cdd:COG0024  139 GNRLGDIghaiqsyaesNGYSvvREF------------------------VGHGIGREMHEEPQVpNYGRPgrgprLKPG 194
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478297 374 FVITIEPGVYipssfdcperfQG-IGIRIEDD------------------VLITETGYEVLT 416
Cdd:COG0024  195 MVLAIEPMIN-----------AGtPEVKVLDDgwtvvtkdgslsaqfehtVAVTEDGPEILT 245
PRK05716 PRK05716
methionine aminopeptidase; Validated
180-418 1.06e-10

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 61.69  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 180 IKSPAELKLMRESASIACQgllkTMLHSKGFPDEGILSAQVEYEC----RVRGAqRMAFN-----PvvggGS-----NAS 245
Cdd:PRK05716   5 IKTPEEIEKMRVAGRLAAE----VLDEIEPHVKPGVTTKELDRIAeeyiRDQGA-IPAPLgyhgfP----KSictsvNEV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 246 VIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQL--- 318
Cdd:PRK05716  76 VCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTF-GVGEISPEDKRL----CEVTKEAlylgIAAVKPGARLGDIgha 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 319 -NTYstellcdglmkmgiLKSRRLyhqlnptSI-----GHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPS 386
Cdd:PRK05716 151 iQKY--------------AEAEGF-------SVvreycGHGIGRKFHEEPQIpHYGAPgdgpvLKEGMVFTIEPMINAGK 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 186478297 387 SFdcperfqgigIRIEDD------------------VLITETGYEVLTGS 418
Cdd:PRK05716 210 RE----------VKTLKDgwtvvtkdgslsaqyehtVAVTEDGPEILTLR 249
PRK14576 PRK14576
putative endopeptidase; Provisional
171-416 4.35e-10

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 61.18  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 171 SSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYS 250
Cdd:PRK14576 168 TALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 251 rNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYStellcdgl 330
Cdd:PRK14576 248 -DTTPAKVGDLIKFDCGIDVAGYGADLARTF-VLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDST-------- 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 331 mkMGILKSRRLYHqLNPTSIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcperfqGIG---IRIED 403
Cdd:PRK14576 318 --MAVIKTSGLPH-YNRGHLGHgdgvFLGLEEVPFVSTQATETFCPGMVLSLETPYY------------GIGvgsIMLED 382
                        250
                 ....*....|...
gi 186478297 404 DVLITETGYEVLT 416
Cdd:PRK14576 383 MILITDSGFEFLS 395
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
180-416 2.24e-08

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 54.84  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 180 IKSPAELKLMRESASIaCQGLLKTMlhsKGFPDEGI----LSAQVEYECRVRGAqRMAFNPVVG-GGS-----NASVIHY 249
Cdd:PRK12896  10 IKSPRELEKMRKIGRI-VATALKEM---GKAVEPGMttkeLDRIAEKRLEEHGA-IPSPEGYYGfPGStcisvNEEVAHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 250 SRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPpcgkFSSVQEELYDLIlQTNKEC----IKQCKPGTTIrqlntystel 325
Cdd:PRK12896  85 IPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFA----VGPVSEEAEKLC-RVAEEAlwagIKQVKAGRPL---------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 326 lcdglmkMGILKSRRLYHQLNPTSI-----GHYLGMDVHDSSAV--GYDRP-----LQPGFVITIEPGVYIPSSFdcper 393
Cdd:PRK12896 150 -------NDIGRAIEDFAKKNGYSVvrdltGHGVGRSLHEEPSVilTYTDPlpnrlLRPGMTLAVEPFLNLGAKD----- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 186478297 394 fqgigIRIEDD------------------VLITETGYEVLT 416
Cdd:PRK12896 218 -----AETLDDgwtvvtpdkslsaqfehtVVVTRDGPEILT 253
PRK15173 PRK15173
peptidase; Provisional
171-423 2.56e-08

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 55.49  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 171 SSLTHELRLIKSPAELKLMRESASIACQGLLKtmlhSKGFPDEGILSAQV--EYECRVRGAQRMAFNPV----VGGGSNA 244
Cdd:PRK15173  86 SSIFNELRVIKSPWEIKRLRKSAEITEYGITE----ASKLIRVGCTSAELtaAYKAAVMSKSETHFSRFhlisVGADFSP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 245 SVIhysRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTE 324
Cdd:PRK15173 162 KLI---PSNTKACSGDLIKFDCGVDVDGYGADIARTF-VVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTME 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 325 LlcdgLMKMGILKSRRLYhqlnptsIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcpeRFQGIGIR 400
Cdd:PRK15173 238 V----IKKSGLPNYNRGH-------LGHgngvFLGLEESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIM 297
                        250       260
                 ....*....|....*....|...
gi 186478297 401 IEDDVLITETGYEVLTgSMPKEI 423
Cdd:PRK15173 298 IEDMILINKEGIEFLS-KLPRDL 319
PRK14575 PRK14575
putative peptidase; Provisional
171-423 4.95e-08

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 55.10  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 171 SSLTHELRLIKSPAELKLMRESASIACQGLLKtmlhSKGFPDEGILSAQV--EYECRVRGAQRMAFNPV----VGGGSNA 244
Cdd:PRK14575 169 SSIFNELRVIKSPWEIKRLRKSAEITEYGITE----ASKLIRVGCTSAELtaAYKAAVMSKSETHFSRFhlisVGADFSP 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 245 SVIhysRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTE 324
Cdd:PRK14575 245 KLI---PSNTKACSGDLIKFDCGVDVDGYGADIARTF-VVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTME 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 325 LlcdgLMKMGILKSRRLYhqlnptsIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcpeRFQGIGIR 400
Cdd:PRK14575 321 V----IKKSGLPNYNRGH-------LGHgngvFLGLEESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIM 380
                        250       260
                 ....*....|....*....|...
gi 186478297 401 IEDDVLITETGYEVLTgSMPKEI 423
Cdd:PRK14575 381 IEDMILINKEGIEFLS-KLPRDL 402
CDC68-like cd01091
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
232-417 3.08e-07

Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.


Pssm-ID: 238524 [Multi-domain]  Cd Length: 243  Bit Score: 51.19  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 232 MAFNPVVGGGSNASVIHYSRNDQRIKDGD-LVLMDMGCELHGYVSDLTRTW---PpcgkfSSVQEELYDLILQTNKECIK 307
Cdd:cd01091   63 WCYPPIIQSGGNYDLLKSSSSSDKLLYHFgVIICSLGARYKSYCSNIARTFlidP-----TSEQQKNYNFLLALQEEILK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 308 QCKPGTTIRQLNTYSTELlcdglmkmgILKSRRLYHQLNPTSIGHYLGMDVHDSSAV---GYDRPLQPGFVITIEPGVY- 383
Cdd:cd01091  138 ELKPGAKLSDVYQKTLDY---------IKKKKPELEPNFTKNLGFGIGLEFRESSLIinaKNDRKLKKGMVFNLSIGFSn 208
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 186478297 384 IPSSFDCPERFQGIGIRIEDDVLITETG-YEVLTG 417
Cdd:cd01091  209 LQNPEPKDKESKTYALLLSDTILVTEDEpAIVLTN 243
COG5406 COG5406
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and ...
234-456 1.63e-04

Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and repair, Chromatin structure and dynamics];


Pssm-ID: 227693 [Multi-domain]  Cd Length: 1001  Bit Score: 44.23  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  234 FNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWppCGKFSSVQEELYDLILQTNKECIKQCKPGT 313
Cdd:COG5406   245 YTPIIQSGGSIDLTPSAFSFPMELTGDVVLLSIGIRYNGYCSNMSRTI--LTDPDSEQQKNYEFLYMLQKYILGLVRPGT 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297  314 TIRQLntYSTELlcdglmkmGILKSRRLYHQLNPT-SIGHYLGMDVHDSS---AVGYDRPLQPG--FVITIEPGVYIPss 387
Cdd:COG5406   323 DSGII--YSEAE--------KYISSNGPELGPNFIyNVGLMIGIEFRSSQkpfNVKNGRVLQAGciFNISLGFGNLIN-- 390
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186478297  388 fdcPERFQGIGIRIEDDVLITETGYEVLTGSmPKEIKHIETLLNNhcHDNS------ARTSPVSLCKVKGLHTNR 456
Cdd:COG5406   391 ---PHPKNNYALLLIDTEQISLSNPIVFTDS-PKAQGDISFLFGE--DDETpeyltlQDKAPDFLDKTISSHRSK 459
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
241-417 3.81e-03

Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 38.67  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 241 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPpCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNT 320
Cdd:cd01090   62 GINTDGAHNPVTNRKVQRGDILSLNCFPMIAGYYTALERTLF-LDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478297 321 YSTELLcdglMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIpssfdcPERFQGIGIR 400
Cdd:cd01090  141 ELNEMY----REHDLLRYRTFGYGHSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIML------PEGQPGAGGY 210
                        170
                 ....*....|....*...
gi 186478297 401 IEDDVL-ITETGYEVLTG 417
Cdd:cd01090  211 REHDILvINENGAENITG 228
 
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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