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Conserved domains on  [gi|1728504115|ref|WP_148071213|]
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MULTISPECIES: aminopeptidase P family N-terminal domain-containing protein, partial [Lactobacillales]

Protein Classification

Creatinase_N domain-containing protein( domain architecture ID 10473644)

Creatinase_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 4-128 1.07e-32

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: 113.17  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   4 RVEKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTTGLA-VITLEKAFFITD-FRYTEQAAAQAQGFEII--KNVGPIFDE 79
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAAAESAPDFDVVpyRDYEALADL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1728504115  80 VANLVRKEElhSLAFEETTVSFLEYSVLEEII-DAELVPVSQMIEELREV 128
Cdd:pfam01321  81 LKELGAGGK--RVGFEADALTVAFYEALKEALpGAELVDVSGLIERLRMV 128
APP_MetAP super family cl00279
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 134-173 1.47e-11

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.


The actual alignment was detected with superfamily member cd01092:

Pssm-ID: 469704 [Multi-domain]  Cd Length: 208  Bit Score: 60.22  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728504115 134 IAIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMR 40
 
Name Accession Description Interval E-value
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 4-128 1.07e-32

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: 113.17  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   4 RVEKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTTGLA-VITLEKAFFITD-FRYTEQAAAQAQGFEII--KNVGPIFDE 79
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAAAESAPDFDVVpyRDYEALADL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1728504115  80 VANLVRKEElhSLAFEETTVSFLEYSVLEEII-DAELVPVSQMIEELREV 128
Cdd:pfam01321  81 LKELGAGGK--RVGFEADALTVAFYEALKEALpGAELVDVSGLIERLRMV 128
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
6-173 3.47e-27

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 103.36  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   6 EKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTT---GLAVITLE-KAFFITDFRYTEQaaaqaqgfeiiknvgpifdeva 81
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSPerlAALLVTADgEPVLFVDELEAER---------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115  82 nlvrkeelhslafeettvsfleysvleeiidaELVPVSQMIEELREVKDEEEIAIIEKACHIADMAYDHILKMIQPGMTE 161
Cdd:COG0006    59 --------------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTE 106

                         170
                  ....*....|..
gi 1728504115 162 IEVANQLDFYMR 173
Cdd:COG0006   107 REVAAELEAAMR 118
PRK09795 PRK09795
aminopeptidase; Provisional
 2-173 3.26e-25

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 99.24  E-value: 3.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   2 MLRVEKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTTGLAVITLEKAFFITDFRYTEQAAAQAQGFEI--IKNVGPIFDE 79
Cdd:PRK09795    1 MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYADVEARAQGYQLhlLDATNTLTTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115  80 VANLVRKEELHSLAFEETTVSFLEYSVLEEIIDAELVPVSqmIEELREVKDEEEIAIIEKACHIADMAYDHILKMIQPGM 159
Cdd:PRK09795   81 VNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGM 158

                         170
                  ....*....|....
gi 1728504115 160 TEIEVANQLDFYMR 173
Cdd:PRK09795  159 SEREIAAELEWFMR 172
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 134-173 1.47e-11

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: 60.22  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728504115 134 IAIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMR 40
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 135-173 8.33e-06

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: 44.15  E-value: 8.33e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1728504115 135 AIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARL 39
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 127-160 1.33e-04

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 40.98  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1728504115 127 EVKDEEEIAIIEKACHIADMAYDHILKMIQPGMT 160
Cdd:PRK12896    9 EIKSPRELEKMRKIGRIVATALKEMGKAVEPGMT 42
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
127-160 4.21e-04

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 39.60  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1728504115 127 EVKDEEEIAIIEKACHIADMAYDHILKMIQPGMT 160
Cdd:COG0024     2 EIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVT 35
 
Name Accession Description Interval E-value
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 4-128 1.07e-32

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: 113.17  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   4 RVEKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTTGLA-VITLEKAFFITD-FRYTEQAAAQAQGFEII--KNVGPIFDE 79
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAAAESAPDFDVVpyRDYEALADL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1728504115  80 VANLVRKEElhSLAFEETTVSFLEYSVLEEII-DAELVPVSQMIEELREV 128
Cdd:pfam01321  81 LKELGAGGK--RVGFEADALTVAFYEALKEALpGAELVDVSGLIERLRMV 128
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
6-173 3.47e-27

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 103.36  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   6 EKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTT---GLAVITLE-KAFFITDFRYTEQaaaqaqgfeiiknvgpifdeva 81
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSPerlAALLVTADgEPVLFVDELEAER---------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115  82 nlvrkeelhslafeettvsfleysvleeiidaELVPVSQMIEELREVKDEEEIAIIEKACHIADMAYDHILKMIQPGMTE 161
Cdd:COG0006    59 --------------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTE 106

                         170
                  ....*....|..
gi 1728504115 162 IEVANQLDFYMR 173
Cdd:COG0006   107 REVAAELEAAMR 118
PRK09795 PRK09795
aminopeptidase; Provisional
 2-173 3.26e-25

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 99.24  E-value: 3.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115   2 MLRVEKLRKKMQEENLDSFLVTSPYNLRYLTNFTGTTGLAVITLEKAFFITDFRYTEQAAAQAQGFEI--IKNVGPIFDE 79
Cdd:PRK09795    1 MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYADVEARAQGYQLhlLDATNTLTTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728504115  80 VANLVRKEELHSLAFEETTVSFLEYSVLEEIIDAELVPVSqmIEELREVKDEEEIAIIEKACHIADMAYDHILKMIQPGM 159
Cdd:PRK09795   81 VNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGM 158

                         170
                  ....*....|....
gi 1728504115 160 TEIEVANQLDFYMR 173
Cdd:PRK09795  159 SEREIAAELEWFMR 172
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 134-173 1.47e-11

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: 60.22  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728504115 134 IAIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMR 40
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 135-173 8.33e-06

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: 44.15  E-value: 8.33e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1728504115 135 AIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARL 39
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 127-160 1.33e-04

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 40.98  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1728504115 127 EVKDEEEIAIIEKACHIADMAYDHILKMIQPGMT 160
Cdd:PRK12896    9 EIKSPRELEKMRKIGRIVATALKEMGKAVEPGMT 42
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
127-160 4.21e-04

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 39.60  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1728504115 127 EVKDEEEIAIIEKACHIADMAYDHILKMIQPGMT 160
Cdd:COG0024     2 EIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVT 35
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 134-173 9.75e-04

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: 38.20  E-value: 9.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728504115 134 IAIIEKACHIADMAYDHILKMIQPGMTEIEVANQLDFYMR 173
Cdd:cd01066     1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALR 40
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
 121-161 4.02e-03

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 37.01  E-value: 4.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1728504115 121 MIEELREVKDEEEIAIIEKACHIADMAYDHILKMIQPGMTE 161
Cdd:PRK10879  166 WVHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFE 206
PRK05716 PRK05716
methionine aminopeptidase; Validated
 128-163 4.04e-03

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 36.65  E-value: 4.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1728504115 128 VKDEEEIAIIEKACHIADMAYDHILKMIQPGMTEIE 163
Cdd:PRK05716    5 IKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKE 40
 
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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