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Conserved domains on  [gi|1958641937|ref|XP_038940400|]
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xaa-Pro aminopeptidase 1 isoform X2 [Rattus norvegicus]

Protein Classification

aminopeptidase P family protein( domain architecture ID 11047996)

aminopeptidase P family protein (metallopeptidase 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

EC:  3.4.11.9
Gene Ontology:  GO:0004177|GO:0016020|GO:0070006|GO:0046872|GO:0006508
PubMed:  16229471

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
 347-547 7.61e-125

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: 367.27  E-value: 7.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 347 KVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTR 425
Cdd:cd01085    23 EVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISPDGLYLIDSGGQYLDGTTDITR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 426 TMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGIsYKTF 505
Cdd:cd01085   103 TVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTGHGVGSFLNVHEGPQSI-SPAP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958641937 506 SDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 547
Cdd:cd01085   182 NNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
Creatinase_N_2 pfam16189
Creatinase/Prolidase N-terminal domain;
200-347 1.85e-55

Creatinase/Prolidase N-terminal domain;


:

Pssm-ID: 465053  Cd Length: 159  Bit Score: 185.00  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 200 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 279
Cdd:pfam16189   1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641937 280 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPK 347
Cdd:pfam16189  81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPA 137
Peptidase_M24_C pfam16188
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ...
 553-615 7.91e-26

C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.


:

Pssm-ID: 465052  Cd Length: 63  Bit Score: 100.56  E-value: 7.91e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641937 553 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 615
Cdd:pfam16188   3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
Creatinase_N super family cl46291
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 53-197 1.55e-09

Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.


The actual alignment was detected with superfamily member pfam01321:

Pssm-ID: 480631  Cd Length: 128  Bit Score: 56.16  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937  53 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 130
Cdd:pfam01321   2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958641937 131 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 197
Cdd:pfam01321  63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
 
Name Accession Description Interval E-value
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
 347-547 7.61e-125

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: 367.27  E-value: 7.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 347 KVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTR 425
Cdd:cd01085    23 EVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISPDGLYLIDSGGQYLDGTTDITR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 426 TMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGIsYKTF 505
Cdd:cd01085   103 TVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTGHGVGSFLNVHEGPQSI-SPAP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958641937 506 SDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 547
Cdd:cd01085   182 NNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
226-562 4.42e-67

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 220.85  E-value: 4.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 226 ADLRLKMAERSIVWFVVTALDEIAWLFNLRGSdvehnPVFFSYAIIGLE-RIMLFIDGdridapgvkqhllldlgLEAEY 304
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGS-----PERLAALLVTADgEPVLFVDE-----------------LEAER 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 305 KIQ-----VLPYKSILS--ELKTLcadlspREKVWVSDKASYAVSEAIpkvpKGGVTEISAADKAEEFRRQQaDFVDLSF 377
Cdd:COG0006    59 ELVdasdlLEELRAIKSpeEIELM------RKAARIADAAHEAALAAL----RPGVTEREVAAELEAAMRRR-GAEGPSF 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 378 PTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVfPT 457
Cdd:COG0006   128 DTIVASGENAAIPHYTP---TDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAAL-KP 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 458 GTKGHLLDSFARSALWDSGL--DYLHGTGHGVGsfLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENV 535
Cdd:COG0006   204 GVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHEGP---QISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIEDT 278

                         330       340
                  ....*....|....*....|....*..
gi 1958641937 536 VLVVPAKtkynfnnrgsltFEPLTLVP 562
Cdd:COG0006   279 VLVTEDG------------AEVLTRLP 293
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 336-540 5.36e-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: 193.61  E-value: 5.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 336 KASYAVSEAIPKVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQ 415
Cdd:pfam00557   8 RIAAAALEAALAAIRPGVTERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIP---NDRVLKPGDLVLIDVGAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 416 YKDG-TTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGLD--YLHGTGHGVGsfLN 492
Cdd:pfam00557  85 YDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKP-GVTGGDVDAAAREVLEEAGLGeyFPHGLGHGIG--LE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958641937 493 VHEGPcgISYKTFSDEPLEAGMIVTDEPGYYE-DGAFGIRIENVVLVVP 540
Cdd:pfam00557 162 VHEGP--YISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
Creatinase_N_2 pfam16189
Creatinase/Prolidase N-terminal domain;
200-347 1.85e-55

Creatinase/Prolidase N-terminal domain;


Pssm-ID: 465053  Cd Length: 159  Bit Score: 185.00  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 200 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 279
Cdd:pfam16189   1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641937 280 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPK 347
Cdd:pfam16189  81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPA 137
Peptidase_M24_C pfam16188
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ...
 553-615 7.91e-26

C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.


Pssm-ID: 465052  Cd Length: 63  Bit Score: 100.56  E-value: 7.91e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641937 553 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 615
Cdd:pfam16188   3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
PRK09795 PRK09795
aminopeptidase; Provisional
 313-540 1.13e-19

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 91.15  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 313 SILSELKTLCADLSPREKVWVSDKASyavsEAIPKVPKGGVTEISAADKAEEFRRQQADfVDLSFPTISSTGPNGAIIHY 392
Cdd:PRK09795  122 DVLRQIKTPEEVEKIRLACGIADRGA----EHIRRFIQAGMSEREIAAELEWFMRQQGA-EKASFDTIVASGWRGALPHG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 393 APipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF---GTPTAYEKECFTY--VLKGHIAVSAAVFPtGTKGHLLDSF 467
Cdd:PRK09795  197 KA---SDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHPLFNVYqiVLQAQLAAISAIRP-GVRCQQVDDA 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958641937 468 ARSALWDSGL-DYL-HGTGHGVGsfLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVP 540
Cdd:PRK09795  273 ARRVITEAGYgDYFgHNTGHAIG--IEVHEDP---RFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTP 342
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 53-197 1.55e-09

Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.


Pssm-ID: 460159  Cd Length: 128  Bit Score: 56.16  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937  53 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 130
Cdd:pfam01321   2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958641937 131 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 197
Cdd:pfam01321  63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
 
Name Accession Description Interval E-value
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
 347-547 7.61e-125

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: 367.27  E-value: 7.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 347 KVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLSLDEVYLIDSGAQYKDGTTDVTR 425
Cdd:cd01085    23 EVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISPDGLYLIDSGGQYLDGTTDITR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 426 TMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGIsYKTF 505
Cdd:cd01085   103 TVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTGHGVGSFLNVHEGPQSI-SPAP 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958641937 506 SDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 547
Cdd:cd01085   182 NNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
226-562 4.42e-67

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 220.85  E-value: 4.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 226 ADLRLKMAERSIVWFVVTALDEIAWLFNLRGSdvehnPVFFSYAIIGLE-RIMLFIDGdridapgvkqhllldlgLEAEY 304
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGS-----PERLAALLVTADgEPVLFVDE-----------------LEAER 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 305 KIQ-----VLPYKSILS--ELKTLcadlspREKVWVSDKASYAVSEAIpkvpKGGVTEISAADKAEEFRRQQaDFVDLSF 377
Cdd:COG0006    59 ELVdasdlLEELRAIKSpeEIELM------RKAARIADAAHEAALAAL----RPGVTEREVAAELEAAMRRR-GAEGPSF 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 378 PTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVfPT 457
Cdd:COG0006   128 DTIVASGENAAIPHYTP---TDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAAL-KP 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 458 GTKGHLLDSFARSALWDSGL--DYLHGTGHGVGsfLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENV 535
Cdd:COG0006   204 GVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHEGP---QISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIEDT 278

                         330       340
                  ....*....|....*....|....*..
gi 1958641937 536 VLVVPAKtkynfnnrgsltFEPLTLVP 562
Cdd:COG0006   279 VLVTEDG------------AEVLTRLP 293
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 336-540 5.36e-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: 193.61  E-value: 5.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 336 KASYAVSEAIPKVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQ 415
Cdd:pfam00557   8 RIAAAALEAALAAIRPGVTERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIP---NDRVLKPGDLVLIDVGAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 416 YKDG-TTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGLD--YLHGTGHGVGsfLN 492
Cdd:pfam00557  85 YDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKP-GVTGGDVDAAAREVLEEAGLGeyFPHGLGHGIG--LE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958641937 493 VHEGPcgISYKTFSDEPLEAGMIVTDEPGYYE-DGAFGIRIENVVLVVP 540
Cdd:pfam00557 162 VHEGP--YISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
Creatinase_N_2 pfam16189
Creatinase/Prolidase N-terminal domain;
200-347 1.85e-55

Creatinase/Prolidase N-terminal domain;


Pssm-ID: 465053  Cd Length: 159  Bit Score: 185.00  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 200 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 279
Cdd:pfam16189   1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641937 280 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPK 347
Cdd:pfam16189  81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPA 137
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 343-538 1.47e-40

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: 146.89  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 343 EAIPKVPKGGVTEISAADKAE-EFRRQQADfvDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYKDGTT 421
Cdd:cd01092    16 EELLEFIKPGMTEREVAAELEyFMRKLGAE--GPSFDTIVASGPNSALPHGVP---SDRKIEEGDLVLIDFGAIYDGYCS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 422 DVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL-DYL-HGTGHGVGsfLNVHEGPcG 499
Cdd:cd01092    91 DITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKP-GVTAKEVDKAARDVIEEAGYgEYFiHRTGHGVG--LEVHEAP-Y 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958641937 500 ISykTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 538
Cdd:cd01092   167 IS--PGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLV 203
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 336-543 2.13e-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: 135.27  E-value: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 336 KASYAVSEAIPKVPKGGVTEISAAdkAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQ 415
Cdd:cd01066     9 EIAEAAMAAAAEAIRPGVTEAEVA--AAIEQALRAAGGYPAGPTIVGSGARTALPHYRP---DDRRLQEGDLVLVDLGGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 416 YKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL--DYLHGTGHGVGsfLNV 493
Cdd:cd01066    84 YDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRP-GVTAEEVDAAAREVLEEHGLgpNFGHRTGHGIG--LEI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958641937 494 HEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKT 543
Cdd:cd01066   161 HEPP---VLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP 207
Peptidase_M24_C pfam16188
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ...
 553-615 7.91e-26

C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.


Pssm-ID: 465052  Cd Length: 63  Bit Score: 100.56  E-value: 7.91e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641937 553 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 615
Cdd:pfam16188   3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
PRK09795 PRK09795
aminopeptidase; Provisional
 313-540 1.13e-19

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 91.15  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 313 SILSELKTLCADLSPREKVWVSDKASyavsEAIPKVPKGGVTEISAADKAEEFRRQQADfVDLSFPTISSTGPNGAIIHY 392
Cdd:PRK09795  122 DVLRQIKTPEEVEKIRLACGIADRGA----EHIRRFIQAGMSEREIAAELEWFMRQQGA-EKASFDTIVASGWRGALPHG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 393 APipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF---GTPTAYEKECFTY--VLKGHIAVSAAVFPtGTKGHLLDSF 467
Cdd:PRK09795  197 KA---SDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHPLFNVYqiVLQAQLAAISAIRP-GVRCQQVDDA 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958641937 468 ARSALWDSGL-DYL-HGTGHGVGsfLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVP 540
Cdd:PRK09795  273 ARRVITEAGYgDYFgHNTGHAIG--IEVHEDP---RFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTP 342
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 364-538 3.45e-18

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: 84.16  E-value: 3.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 364 EFRRQQADfvdLSFPTISSTGPNGAIIHYApipETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-GTPTAYEKECFTY 442
Cdd:cd01087    38 EFRSRGAR---LAYSYIVAAGSNAAILHYV---HNDQPLKDGDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 443 VLKGHIAVSAAVFPtGTK---GHLL-DSFARSALWDSGLD----------------YLHGTGHGVGsfLNVHEgpCGISY 502
Cdd:cd01087   112 VLAAQKAAIAACKP-GVSyedIHLLaHRVLAEGLKELGILkgdvdeivesgayakfFPHGLGHYLG--LDVHD--VGGYL 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958641937 503 KTFS-DEPLEAGMIVTDEPGYY---EDGAF-------GIRIENVVLV 538
Cdd:cd01087   187 RYLRrARPLEPGMVITIEPGIYfipDLLDVpeyfrggGIRIEDDVLV 233
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
 364-538 5.83e-11

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 64.75  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 364 EFRRQQADFVdlSFPTISSTGPNGAIIHYApipETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-GTPTAYEKECFTY 442
Cdd:PRK10879  216 EFNRHGARYP--SYNTIVGSGENGCILHYT---ENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDI 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 443 VLKGhIAVSAAVFPTGT-----------------------KG---HLLDSFARSALwdsgldYLHGTGHGVGsfLNVHEg 496
Cdd:PRK10879  291 VLES-LETSLRLYRPGTsirevtgevvrimvsglvklgilKGdvdQLIAENAHRPF------FMHGLSHWLG--LDVHD- 360

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958641937 497 pCGiSYKTFSDEPLEAGMIVTDEPGYY---------EDGAFGIRIENVVLV 538
Cdd:PRK10879  361 -VG-VYGQDRSRILEPGMVLTVEPGLYiapdadvpeQYRGIGIRIEDDIVI 409
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 53-197 1.55e-09

Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.


Pssm-ID: 460159  Cd Length: 128  Bit Score: 56.16  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937  53 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 130
Cdd:pfam01321   2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958641937 131 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 197
Cdd:pfam01321  63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
PRK15173 PRK15173
peptidase; Provisional
 313-538 1.59e-08

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 56.65  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 313 SILSELKTLCADLSPREKVWVSDKASYAVSEAiPKVPKGGVT--EISAADKAEEFRRQQADFVDLSFPTIsstgpnGAII 390
Cdd:PRK15173   87 SIFNELRVIKSPWEIKRLRKSAEITEYGITEA-SKLIRVGCTsaELTAAYKAAVMSKSETHFSRFHLISV------GADF 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 391 HYAPIPETNRTLSLDEVYLiDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARS 470
Cdd:PRK15173  160 SPKLIPSNTKACSGDLIKF-DCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TME 237

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 471 ALWDSGL-DYLHG-TGHGVGSFLNVHEGPCgisYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 538
Cdd:PRK15173  238 VIKKSGLpNYNRGhLGHGNGVFLGLEESPF---VSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILI 304
PRK14575 PRK14575
putative peptidase; Provisional
 313-538 3.22e-08

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 56.25  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 313 SILSELKTLCADLSPREKVWVSDKASYAVSEAiPKVPKGGVT--EISAADKAEEFRRQQADFVDLSFPTIsstgpnGAII 390
Cdd:PRK14575  170 SIFNELRVIKSPWEIKRLRKSAEITEYGITEA-SKLIRVGCTsaELTAAYKAAVMSKSETHFSRFHLISV------GADF 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 391 HYAPIPETNRTLSLDEVYLiDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARS 470
Cdd:PRK14575  243 SPKLIPSNTKACSGDLIKF-DCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TME 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 471 ALWDSGL-DYLHG-TGHGVGSFLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 538
Cdd:PRK14575  321 VIKKSGLpNYNRGhLGHGNGVFLGLEESP---FVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILI 387
PRK14576 PRK14576
putative endopeptidase; Provisional
 339-538 1.95e-04

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 44.24  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 339 YAVSEAIPKVPKG-GVTEISAADKAEEFRRQQADFVDLSfptISSTGPNgaiihYAP--IPETNRTLSLDEVYLiDSGAQ 415
Cdd:PRK14576  195 YGIASAAKKIRVGcTAAELTAAFKAAVMSFPETNFSRFN---LISVGDN-----FSPkiIADTTPAKVGDLIKF-DCGID 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641937 416 YKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARSALWDSGLDYLH--GTGHGVGSFLNV 493
Cdd:PRK14576  266 VAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDS-TMAVIKTSGLPHYNrgHLGHGDGVFLGL 344

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958641937 494 HEGPCgisYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 538
Cdd:PRK14576  345 EEVPF---VSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILI 386
 
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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