NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30681070|ref|NP_172401|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
217-448 6.48e-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: 323.37  E-value: 6.48e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 217 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 296
Cdd:cd01087   1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 297 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 369
Cdd:cd01087  80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 370 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 444
Cdd:cd01087 160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                ....
gi 30681070 445 VLTG 448
Cdd:cd01087 240 NLTR 243
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
57-173 3.27e-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: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070    57 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 132
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30681070   133 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 173
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 ...
217-448 6.48e-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: 323.37  E-value: 6.48e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 217 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 296
Cdd:cd01087   1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 297 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 369
Cdd:cd01087  80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 370 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 444
Cdd:cd01087 160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                ....
gi 30681070 445 VLTG 448
Cdd:cd01087 240 NLTR 243
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
55-461 8.09e-93

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 288.93  E-value: 8.09e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   55 EEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL--SDE--RGLCMFmpeSTPKD 130
Cdd:PRK10879   4 QEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLikSDDthNHSVLF---NRVRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  131 IA---WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHnvqsASQRYTNLDDFQNSAsLGKVKTLS----- 202
Cdd:PRK10879  81 LTaeiWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYH----AQGEYAYADEIVFSA-LEKLRKGSrqnlt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  203 ---SLT------HELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGS 273
Cdd:PRK10879 156 apaTLTdwrpwvHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  274 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYS 353
Cdd:PRK10879 236 NGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  354 TELLCDGLMKMGILK-------SRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSSFDCPER 424
Cdd:PRK10879 316 VRIMVSGLVKLGILKgdvdqliAENAHRPFFMHGLSHWLGLDVHDVGVYGQDrsRILEPGMVLTVEPGLYIAPDADVPEQ 395
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 30681070  425 FQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLL 461
Cdd:PRK10879 396 YRGIGIRIEDDIVITETGNENLTASVVKKPDEIEALM 432
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
196-457 6.26e-76

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 240.49  E-value: 6.26e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 196 GKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVRGAQRMAFNPVVGG 271
Cdd:COG0006  58 RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALR----PGVtereVAAELEAAMRRRGAEGPSFDTIVAS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 272 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNt 351
Cdd:COG0006 134 GENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTV-AVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD- 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 352 ystELLCDGLMKMGilksrrlYHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiG 429
Cdd:COG0006 212 ---AAARDVLAEAG-------YGEYFPHGTGHGVGLDVHEgpQISPGNDRPLEPGMVFTIEPGIYIPGIG---------G 272
                       250       260
                ....*....|....*....|....*...
gi 30681070 430 IRIEDDVLITETGYEVLTGsMPKEIKHI 457
Cdd:COG0006 273 VRIEDTVLVTEDGAEVLTR-LPRELLEL 299
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
218-440 1.29e-57

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: 1.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   218 KLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVR-GAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 292
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIR----PGVtereLAAELEAARLRRgGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   293 VLMDMGCEL-HGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNtystELLCDGLMKMGilksrr 371
Cdd:pfam00557  77 VLIDVGAEYdGGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVD----AAAREVLEEAG------ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681070   372 lYHQLNPTSIGHYLGMDVHDSSAVGY---DRPLQPGFVITIEPGVYIPssfdcPERFqgiGIRIEDDVLITE 440
Cdd:pfam00557 146 -LGEYFPHGLGHGIGLEVHEGPYISRggdDRVLEPGMVFTIEPGIYFI-----PGWG---GVRIEDTVLVTE 208
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
57-173 3.27e-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: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070    57 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 132
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30681070   133 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 173
Cdd:pfam05195  81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
AMP_N smart01011
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
52-176 1.78e-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: 1.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070     52 IRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERG---LCMFMPESTP 128
Cdd:smart01011   1 IPAAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLDPSGGggkSTLFVPPRDP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 30681070    129 KDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNV 176
Cdd:smart01011  81 EDELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLL 128
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
211-447 9.60e-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: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   211 IKSPAELKLMRESASIACQGLLktMLHSKGFPdeGILSAQVEYECRVRGAQRMA---------FNPVVGGGSNASVIHYS 281
Cdd:TIGR00500   3 LKSPDEIEKIRKAGRLAAEVLE--ELEREVKP--GVSTKELDRIAKDFIEKHGAkpaflgyygFPGSVCISVNEVVIHGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   282 RNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQLN----TYS 353
Cdd:TIGR00500  79 PDKKVLKDGDIVNIDVGVIYDGYHGDTAKTF-LVGKISPEAEKL----LECTEESlykaIEEAKPGNRIGEIGaaiqKYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   354 TELLCDGLMKMGilksrrlyhqlnptsiGHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPSSFDcpeRFQG 427
Cdd:TIGR00500 154 EAKGFSVVREYC----------------GHGIGRKFHEEPQIpNYGKKftnvrLKEGMVFTIEPMVNTGTEEI---TTAA 214
                         250       260       270
                  ....*....|....*....|....*....|.
gi 30681070   428 IG-----------IRIEDDVLITETGYEVLT 447
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 ...
217-448 6.48e-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: 323.37  E-value: 6.48e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 217 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAqRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 296
Cdd:cd01087   1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA-RLAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 297 MGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKS------- 369
Cdd:cd01087  80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGdvdeive 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 370 RRLYHQLNPTSIGHYLGMDVHDSSA----VGYDRPLQPGFVITIEPGVYIPSSFDCPER-FQGIGIRIEDDVLITETGYE 444
Cdd:cd01087 160 SGAYAKFFPHGLGHYLGLDVHDVGGylryLRRARPLEPGMVITIEPGIYFIPDLLDVPEyFRGGGIRIEDDVLVTEDGPE 239

                ....
gi 30681070 445 VLTG 448
Cdd:cd01087 240 NLTR 243
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
55-461 8.09e-93

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 288.93  E-value: 8.09e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   55 EEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL--SDE--RGLCMFmpeSTPKD 130
Cdd:PRK10879   4 QEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLikSDDthNHSVLF---NRVRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  131 IA---WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHnvqsASQRYTNLDDFQNSAsLGKVKTLS----- 202
Cdd:PRK10879  81 LTaeiWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYH----AQGEYAYADEIVFSA-LEKLRKGSrqnlt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  203 ---SLT------HELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGS 273
Cdd:PRK10879 156 apaTLTdwrpwvHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  274 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYS 353
Cdd:PRK10879 236 NGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  354 TELLCDGLMKMGILK-------SRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSSFDCPER 424
Cdd:PRK10879 316 VRIMVSGLVKLGILKgdvdqliAENAHRPFFMHGLSHWLGLDVHDVGVYGQDrsRILEPGMVLTVEPGLYIAPDADVPEQ 395
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 30681070  425 FQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLL 461
Cdd:PRK10879 396 YRGIGIRIEDDIVITETGNENLTASVVKKPDEIEALM 432
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
196-457 6.26e-76

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 240.49  E-value: 6.26e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 196 GKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVRGAQRMAFNPVVGG 271
Cdd:COG0006  58 RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALR----PGVtereVAAELEAAMRRRGAEGPSFDTIVAS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 272 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNt 351
Cdd:COG0006 134 GENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTV-AVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD- 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 352 ystELLCDGLMKMGilksrrlYHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiG 429
Cdd:COG0006 212 ---AAARDVLAEAG-------YGEYFPHGTGHGVGLDVHEgpQISPGNDRPLEPGMVFTIEPGIYIPGIG---------G 272
                       250       260
                ....*....|....*....|....*...
gi 30681070 430 IRIEDDVLITETGYEVLTGsMPKEIKHI 457
Cdd:COG0006 273 VRIEDTVLVTEDGAEVLTR-LPRELLEL 299
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
218-440 1.29e-57

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: 1.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   218 KLMRESASIACQGLLKTMLHSKgfpdEGI----LSAQVEYECRVR-GAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 292
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIR----PGVtereLAAELEAARLRRgGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   293 VLMDMGCEL-HGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNtystELLCDGLMKMGilksrr 371
Cdd:pfam00557  77 VLIDVGAEYdGGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVD----AAAREVLEEAG------ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681070   372 lYHQLNPTSIGHYLGMDVHDSSAVGY---DRPLQPGFVITIEPGVYIPssfdcPERFqgiGIRIEDDVLITE 440
Cdd:pfam00557 146 -LGEYFPHGLGHGIGLEVHEGPYISRggdDRVLEPGMVFTIEPGIYFI-----PGWG---GVRIEDTVLVTE 208
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
217-443 4.02e-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: 4.02e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 217 LKLMRESASIACqgllKTMLHSKGFPDEGI----LSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDL 292
Cdd:cd01092   1 IELLRKAARIAD----KAFEELLEFIKPGMtereVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 293 VLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLcdglmkmgilkSRRL 372
Cdd:cd01092  77 VLIDFGAIYDGYCSDITRTV-AVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVI-----------EEAG 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30681070 373 YHQLNPTSIGHYLGMDVHD--SSAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiGIRIEDDVLITETGY 443
Cdd:cd01092 145 YGEYFIHRTGHGVGLEVHEapYISPGSDDVLEEGMVFTIEPGIYIPGKG---------GVRIEDDVLVTEDGC 208
AMP_N pfam05195
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
57-173 3.27e-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: 3.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070    57 YIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVL----SDERGLCMFMPESTPKDIA 132
Cdd:pfam05195   1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLeggdIDSGKETLFVPPKDPEDEI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30681070   133 WEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVF 173
Cdd:pfam05195  81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
AMP_N smart01011
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ...
52-176 1.78e-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: 1.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070     52 IRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERG---LCMFMPESTP 128
Cdd:smart01011   1 IPAAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLDPSGGggkSTLFVPPRDP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 30681070    129 KDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNV 176
Cdd:smart01011  81 EDELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLL 128
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
217-443 1.32e-35

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: 1.32e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 217 LKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQrMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMD 296
Cdd:cd01066   1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGY-PAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 297 MGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLntysTELLCDGLmkmgilkSRRLYHQL 376
Cdd:cd01066  80 LGGVYDGYHADLTRTF-VIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEV----DAAAREVL-------EEHGLGPN 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30681070 377 NPTSIGHYLGMDVHDSSAV--GYDRPLQPGFVITIEPGVYIPssfdcperfQGIGIRIEDDVLITETGY 443
Cdd:cd01066 148 FGHRTGHGIGLEIHEPPVLkaGDDTVLEPGMVFAVEPGLYLP---------GGGGVRIEDTVLVTEDGP 207
PRK09795 PRK09795
aminopeptidase; Provisional
197-454 1.21e-29

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 119.27  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  197 KVKTLSSLTHELRLIKSPAELKLMRESASIACQGllktMLHSKGFPDEGI----LSAQVEYECRVRGAQRMAFNPVVGGG 272
Cdd:PRK09795 113 NAKLVSATPDVLRQIKTPEEVEKIRLACGIADRG----AEHIRRFIQAGMsereIAAELEWFMRQQGAEKASFDTIVASG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  273 SNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEE----LYDLILQTNKECIKQCKPGTTIRQ 348
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAESHplfnVYQIVLQAQLAAISAIRPGVRCQQ 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  349 LNTYSTELLcdglmkmgilkSRRLYHQLNPTSIGHYLGMDVHDSSAVGYD--RPLQPGFVITIEPGVYIPSsfdcperfQ 426
Cdd:PRK09795 269 VDDAARRVI-----------TEAGYGDYFGHNTGHAIGIEVHEDPRFSPRdtTTLQPGMLLTVEPGIYLPG--------Q 329
                        250       260
                 ....*....|....*....|....*...
gi 30681070  427 GiGIRIEDDVLITETGYEVLTgSMPKEI 454
Cdd:PRK09795 330 G-GVRIEDVVLVTPQGAEVLY-AMPKTV 355
PRK13607 PRK13607
proline dipeptidase; Provisional
206-447 1.42e-20

proline dipeptidase; Provisional


Pssm-ID: 237444 [Multi-domain]  Cd Length: 443  Bit Score: 93.81  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  206 HELRLIKSPAELKLMRESASIACQGllktmlH--SKgfpdEGILSAQVEYECRVR-------GAQRMAFNPVVGGGSNAS 276
Cdd:PRK13607 156 HYHRAYKTDYELACMREAQKIAVAG------HraAK----EAFRAGMSEFDINLAyltatgqRDNDVPYGNIVALNEHAA 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  277 VIHYSRNDQRIKDGDL-VLMDMGCELHGYVSDLTRTWPpcgkfSSVQEELYDLILQTNKE---CIKQCKPGTTIRQLNTY 352
Cdd:PRK13607 226 VLHYTKLDHQAPAEMRsFLIDAGAEYNGYAADITRTYA-----AKEDNDFAALIKDVNKEqlaLIATMKPGVSYVDLHIQ 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  353 STELLcdglmkMGILKSRRLYHQLNP--------TS------IGHYLGMDVHDSSAVGYD------------------RP 400
Cdd:PRK13607 301 MHQRI------AKLLRKFQIVTGLSEeamveqgiTSpffphgLGHPLGLQVHDVAGFMQDdrgthlaapekhpylrctRV 374
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30681070  401 LQPGFVITIEPGVY-IPSSFDcP----ERFQGI------------GIRIEDDVLITETGYEVLT 447
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 ...
232-442 2.56e-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: 2.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 232 LKTMLHSKGFPDEGILSAQVEYecrVRGAQRM----AFNPVVGGGSNASVIHYSRNDQ---RIKDGDLVLMDMGCELHGY 304
Cdd:cd01085  20 LEQEVPKGETITELSAADKLEE---FRRQQKGyvglSFDTISGFGPNGAIVHYSPTEEsnrKISPDGLYLIDSGGQYLDG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 305 VSDLTRTWPpCGKFSSVQEELYDLILQTNKECIKQCKP-GTTIRQLntystellcDGLMKMGILKSRRLY-----Hqlnp 378
Cdd:cd01085  97 TTDITRTVH-LGEPTAEQKRDYTLVLKGHIALARAKFPkGTTGSQL---------DALARQPLWKAGLDYghgtgH---- 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681070 379 tSIGHYLGmdVHDS----SAVGYDRPLQPGFVITIEPGVYIPSSFdcperfqgiGIRIEDDVLITETG 442
Cdd:cd01085 163 -GVGSFLN--VHEGpqsiSPAPNNVPLKAGMILSNEPGYYKEGKY---------GIRIENLVLVVEAE 218
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
211-447 9.60e-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: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   211 IKSPAELKLMRESASIACQGLLktMLHSKGFPdeGILSAQVEYECRVRGAQRMA---------FNPVVGGGSNASVIHYS 281
Cdd:TIGR00500   3 LKSPDEIEKIRKAGRLAAEVLE--ELEREVKP--GVSTKELDRIAKDFIEKHGAkpaflgyygFPGSVCISVNEVVIHGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   282 RNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQLN----TYS 353
Cdd:TIGR00500  79 PDKKVLKDGDIVNIDVGVIYDGYHGDTAKTF-LVGKISPEAEKL----LECTEESlykaIEEAKPGNRIGEIGaaiqKYA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070   354 TELLCDGLMKMGilksrrlyhqlnptsiGHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPSSFDcpeRFQG 427
Cdd:TIGR00500 154 EAKGFSVVREYC----------------GHGIGRKFHEEPQIpNYGKKftnvrLKEGMVFTIEPMVNTGTEEI---TTAA 214
                         250       260       270
                  ....*....|....*....|....*....|.
gi 30681070   428 IG-----------IRIEDDVLITETGYEVLT 447
Cdd:TIGR00500 215 DGwtvktkdgslsAQFEHTIVITDNGPEILT 245
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
274-447 6.14e-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: 71.37  E-value: 6.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 274 NASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQL 349
Cdd:cd01086  63 NEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTF-IVGEVSEEAKKL----VEVTEEAlykgIEAVKPGNRIGDI 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 350 ----NTYstellcdglmkmgiLKSRRLYhqLNPTSIGHYLGMDVHDSSAV------GYDRPLQPGFVITIEPGVYIPSSF 419
Cdd:cd01086 138 ghaiEKY--------------AEKNGYS--VVREFGGHGIGRKFHEEPQIpnygrpGTGPKLKPGMVFTIEPMINLGTYE 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 30681070 420 dcperfqgigIRIEDD------------------VLITETGYEVLT 447
Cdd:cd01086 202 ----------VVTLPDgwtvvtkdgslsaqfehtVLITEDGPEILT 237
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
211-447 2.42e-12

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 66.95  E-value: 2.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 211 IKSPAELKLMRESASIACQGL--LKTMLHskgfpdEGI----LSAQVEYECRVRGAQrmafnpvvgggsnASVIHY---- 280
Cdd:COG0024   3 IKTPEEIEKMREAGRIVAEVLdeLAEAVK------PGVttleLDRIAEEFIRDHGAI-------------PAFLGYygfp 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 281 -----SRNDQ---------RIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKfssVQEELYDLIlQTNKEC----IKQCKP 342
Cdd:COG0024  64 ksictSVNEVvvhgipsdrVLKDGDIVNIDVGAILDGYHGDSARTF-VVGE---VSPEARRLV-EVTEEAlyagIAAAKP 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 343 GTTIRQL----------NTYS--TELlcdglmkmgilksrrlyhqlnptsIGHYLGMDVHDSSAV-GYDRP-----LQPG 404
Cdd:COG0024 139 GNRLGDIghaiqsyaesNGYSvvREF------------------------VGHGIGREMHEEPQVpNYGRPgrgprLKPG 194
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30681070 405 FVITIEPGVYipssfdcperfQG-IGIRIEDD------------------VLITETGYEVLT 447
Cdd:COG0024 195 MVLAIEPMIN-----------AGtPEVKVLDDgwtvvtkdgslsaqfehtVAVTEDGPEILT 245
PRK05716 PRK05716
methionine aminopeptidase; Validated
211-449 8.88e-11

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 62.07  E-value: 8.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  211 IKSPAELKLMRESASIACQgllkTMLHSKGFPDEGILSAQVEYEC----RVRGAqRMAFN-----PvvggGS-----NAS 276
Cdd:PRK05716   5 IKTPEEIEKMRVAGRLAAE----VLDEIEPHVKPGVTTKELDRIAeeyiRDQGA-IPAPLgyhgfP----KSictsvNEV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  277 VIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELydliLQTNKEC----IKQCKPGTTIRQL--- 349
Cdd:PRK05716  76 VCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTF-GVGEISPEDKRL----CEVTKEAlylgIAAVKPGARLGDIgha 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  350 -NTYstellcdglmkmgiLKSRRLyhqlnptSI-----GHYLGMDVHDSSAV-GYDRP-----LQPGFVITIEPGVYIPS 417
Cdd:PRK05716 151 iQKY--------------AEAEGF-------SVvreycGHGIGRKFHEEPQIpHYGAPgdgpvLKEGMVFTIEPMINAGK 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 30681070  418 SFdcperfqgigIRIEDD------------------VLITETGYEVLTGS 449
Cdd:PRK05716 210 RE----------VKTLKDgwtvvtkdgslsaqyehtVAVTEDGPEILTLR 249
PRK14576 PRK14576
putative endopeptidase; Provisional
202-447 5.80e-10

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 61.18  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  202 SSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYS 281
Cdd:PRK14576 168 TALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  282 rNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYStellcdgl 361
Cdd:PRK14576 248 -DTTPAKVGDLIKFDCGIDVAGYGADLARTF-VLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDST-------- 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  362 mkMGILKSRRLYHqLNPTSIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcperfqGIG---IRIED 434
Cdd:PRK14576 318 --MAVIKTSGLPH-YNRGHLGHgdgvFLGLEEVPFVSTQATETFCPGMVLSLETPYY------------GIGvgsIMLED 382
                        250
                 ....*....|...
gi 30681070  435 DVLITETGYEVLT 447
Cdd:PRK14576 383 MILITDSGFEFLS 395
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
211-447 2.46e-08

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 54.84  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  211 IKSPAELKLMRESASIaCQGLLKTMlhsKGFPDEGI----LSAQVEYECRVRGAqRMAFNPVVG-GGS-----NASVIHY 280
Cdd:PRK12896  10 IKSPRELEKMRKIGRI-VATALKEM---GKAVEPGMttkeLDRIAEKRLEEHGA-IPSPEGYYGfPGStcisvNEEVAHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  281 SRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPpcgkFSSVQEELYDLIlQTNKEC----IKQCKPGTTIrqlntystel 356
Cdd:PRK12896  85 IPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFA----VGPVSEEAEKLC-RVAEEAlwagIKQVKAGRPL---------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  357 lcdglmkMGILKSRRLYHQLNPTSI-----GHYLGMDVHDSSAV--GYDRP-----LQPGFVITIEPGVYIPSSFdcper 424
Cdd:PRK12896 150 -------NDIGRAIEDFAKKNGYSVvrdltGHGVGRSLHEEPSVilTYTDPlpnrlLRPGMTLAVEPFLNLGAKD----- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 30681070  425 fqgigIRIEDD------------------VLITETGYEVLT 447
Cdd:PRK12896 218 -----AETLDDgwtvvtpdkslsaqfehtVVVTRDGPEILT 253
PRK15173 PRK15173
peptidase; Provisional
202-454 2.84e-08

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 55.49  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  202 SSLTHELRLIKSPAELKLMRESASIACQGLLKtmlhSKGFPDEGILSAQV--EYECRVRGAQRMAFNPV----VGGGSNA 275
Cdd:PRK15173  86 SSIFNELRVIKSPWEIKRLRKSAEITEYGITE----ASKLIRVGCTSAELtaAYKAAVMSKSETHFSRFhlisVGADFSP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  276 SVIhysRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTE 355
Cdd:PRK15173 162 KLI---PSNTKACSGDLIKFDCGVDVDGYGADIARTF-VVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTME 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  356 LlcdgLMKMGILKSRRLYhqlnptsIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcpeRFQGIGIR 431
Cdd:PRK15173 238 V----IKKSGLPNYNRGH-------LGHgngvFLGLEESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIM 297
                        250       260
                 ....*....|....*....|...
gi 30681070  432 IEDDVLITETGYEVLTgSMPKEI 454
Cdd:PRK15173 298 IEDMILINKEGIEFLS-KLPRDL 319
PRK14575 PRK14575
putative peptidase; Provisional
202-454 5.52e-08

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 55.10  E-value: 5.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  202 SSLTHELRLIKSPAELKLMRESASIACQGLLKtmlhSKGFPDEGILSAQV--EYECRVRGAQRMAFNPV----VGGGSNA 275
Cdd:PRK14575 169 SSIFNELRVIKSPWEIKRLRKSAEITEYGITE----ASKLIRVGCTSAELtaAYKAAVMSKSETHFSRFhlisVGADFSP 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  276 SVIhysRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWpPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTE 355
Cdd:PRK14575 245 KLI---PSNTKACSGDLIKFDCGVDVDGYGADIARTF-VVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTME 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  356 LlcdgLMKMGILKSRRLYhqlnptsIGH----YLGMDVHDSSAVGYDRPLQPGFVITIEPGVYipssfdcpeRFQGIGIR 431
Cdd:PRK14575 321 V----IKKSGLPNYNRGH-------LGHgngvFLGLEESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIM 380
                        250       260
                 ....*....|....*....|...
gi 30681070  432 IEDDVLITETGYEVLTgSMPKEI 454
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 ...
263-448 3.37e-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: 3.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 263 MAFNPVVGGGSNASVIHYSRNDQRIKDGD-LVLMDMGCELHGYVSDLTRTW---PpcgkfSSVQEELYDLILQTNKECIK 338
Cdd:cd01091  63 WCYPPIIQSGGNYDLLKSSSSSDKLLYHFgVIICSLGARYKSYCSNIARTFlidP-----TSEQQKNYNFLLALQEEILK 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 339 QCKPGTTIRQLNTYSTELlcdglmkmgILKSRRLYHQLNPTSIGHYLGMDVHDSSAV---GYDRPLQPGFVITIEPGVY- 414
Cdd:cd01091 138 ELKPGAKLSDVYQKTLDY---------IKKKKPELEPNFTKNLGFGIGLEFRESSLIinaKNDRKLKKGMVFNLSIGFSn 208
                       170       180       190
                ....*....|....*....|....*....|....*
gi 30681070 415 IPSSFDCPERFQGIGIRIEDDVLITETG-YEVLTG 448
Cdd:cd01091 209 LQNPEPKDKESKTYALLLSDTILVTEDEpAIVLTN 243
COG5406 COG5406
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and ...
265-487 1.80e-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: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  265 FNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWppCGKFSSVQEELYDLILQTNKECIKQCKPGT 344
Cdd:COG5406  245 YTPIIQSGGSIDLTPSAFSFPMELTGDVVLLSIGIRYNGYCSNMSRTI--LTDPDSEQQKNYEFLYMLQKYILGLVRPGT 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070  345 TIRQLntYSTELlcdglmkmGILKSRRLYHQLNPT-SIGHYLGMDVHDSS---AVGYDRPLQPG--FVITIEPGVYIPss 418
Cdd:COG5406  323 DSGII--YSEAE--------KYISSNGPELGPNFIyNVGLMIGIEFRSSQkpfNVKNGRVLQAGciFNISLGFGNLIN-- 390
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30681070  419 fdcPERFQGIGIRIEDDVLITETGYEVLTGSmPKEIKHIETLLNNhcHDNS------ARTSPVSLCKVKGLHTNR 487
Cdd:COG5406  391 ---PHPKNNYALLLIDTEQISLSNPIVFTDS-PKAQGDISFLFGE--DDETpeyltlQDKAPDFLDKTISSHRSK 459
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
272-448 4.14e-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: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 272 GSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPpCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNT 351
Cdd:cd01090  62 GINTDGAHNPVTNRKVQRGDILSLNCFPMIAGYYTALERTLF-LDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAA 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681070 352 YSTELLcdglMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIpssfdcPERFQGIGIR 431
Cdd:cd01090 141 ELNEMY----REHDLLRYRTFGYGHSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIML------PEGQPGAGGY 210
                       170
                ....*....|....*...
gi 30681070 432 IEDDVL-ITETGYEVLTG 448
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH