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Conserved domains on  [gi|1039761607|ref|XP_017174679|]
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methionine aminopeptidase 1D, mitochondrial isoform X5 [Mus musculus]

Protein Classification

M24 family metallopeptidase( domain architecture ID 320)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APP_MetAP super family cl00279
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 94-239 3.47e-78

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 cd01086:

Pssm-ID: 469704 [Multi-domain]  Cd Length: 238  Bit Score: 235.08  E-value: 3.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGD 173
Cdd:cd01086     1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 174 IINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:cd01086    81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAE 146
 
Name Accession Description Interval E-value
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 94-239 3.47e-78

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: 235.08  E-value: 3.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGD 173
Cdd:cd01086     1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 174 IINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:cd01086    81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAE 146
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 55-234 5.12e-74

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 230.11  E-value: 5.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  55 PAAVSPAHPVPKRIKKPDYVTTGI-----VPDWGDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVH 129
Cdd:PLN03158   99 PYPISPRRVVPDHIPKPDWALDGTpkiepNSDLQHSVEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVH 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607 130 WEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEV 209
Cdd:PLN03158  179 EATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKC 258

                         170       180
                  ....*....|....*....|....*
gi 1039761607 210 ARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:PLN03158  259 TYECLEKAIAIVKPGVRYREVGEVI 283
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
86-239 1.32e-73

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 224.11  E-value: 1.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:COG0024     1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761607 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:COG0024    81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAE 154
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 86-239 9.02e-59

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: 186.01  E-value: 9.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:TIGR00500   1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761607 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:TIGR00500  81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAE 154
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 95-239 2.00e-38

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: 132.75  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  95 QGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYpsplGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDI 174
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 175 INIDVTVYYN-GYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:pfam00557  77 VLIDVGAEYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLE 142
 
Name Accession Description Interval E-value
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 94-239 3.47e-78

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: 235.08  E-value: 3.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGD 173
Cdd:cd01086     1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 174 IINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:cd01086    81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAE 146
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 55-234 5.12e-74

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 230.11  E-value: 5.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  55 PAAVSPAHPVPKRIKKPDYVTTGI-----VPDWGDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVH 129
Cdd:PLN03158   99 PYPISPRRVVPDHIPKPDWALDGTpkiepNSDLQHSVEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVH 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607 130 WEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEV 209
Cdd:PLN03158  179 EATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKC 258

                         170       180
                  ....*....|....*....|....*
gi 1039761607 210 ARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:PLN03158  259 TYECLEKAIAIVKPGVRYREVGEVI 283
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
86-239 1.32e-73

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 224.11  E-value: 1.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:COG0024     1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761607 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:COG0024    81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAE 154
PRK05716 PRK05716
methionine aminopeptidase; Validated
 85-237 4.81e-69

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 212.30  E-value: 4.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  85 SIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIP 164
Cdd:PRK05716    2 AITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761607 165 DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDY 237
Cdd:PRK05716   82 SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKY 154
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 83-239 1.09e-60

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 191.20  E-value: 1.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  83 GDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHG 162
Cdd:PRK12896    5 GRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHG 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039761607 163 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:PRK12896   85 IPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAK 161
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 86-239 9.02e-59

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: 186.01  E-value: 9.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:TIGR00500   1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761607 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:TIGR00500  81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAE 154
PRK12318 PRK12318
methionyl aminopeptidase;
86-237 2.83e-46

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 155.36  E-value: 2.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGR--FPKSVCTSVNNVLCHGI 163
Cdd:PRK12318   41 IIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGI 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761607 164 PDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDY 237
Cdd:PRK12318  121 PNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENC 194
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 95-239 2.00e-38

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: 132.75  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  95 QGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYpsplGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDI 174
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 175 INIDVTVYYN-GYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:pfam00557  77 VLIDVGAEYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLE 142
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 94-239 1.97e-30

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: 112.16  E-value: 1.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPlgygrfpkSVCTSVNNV--LCHGIPDSRPLQD 171
Cdd:cd01066     1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039761607 172 GDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:cd01066    73 GDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLE 140
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
88-238 1.14e-25

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 101.82  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDA-YPSplgygrFPKSVCTSVNNVLCHGIPDS 166
Cdd:COG0006    73 IKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAeGPS------FDTIVASGENAAIPHYTPTD 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039761607 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYF 238
Cdd:COG0006   147 RPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVL 218
PRK12897 PRK12897
type I methionyl aminopeptidase;
86-236 5.24e-24

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 96.26  E-value: 5.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:PRK12897    2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761607 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRcrdeaiaACRAGAPFSVIGNTIRD 236
Cdd:PRK12897   82 DVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAEN-------ALYKGIDQAVIGNRVGD 145
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 94-238 3.70e-23

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: 92.96  E-value: 3.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAY-PSplgygrFPKSVCTSVNNVLCHGIPDSRPLQDG 172
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039761607 173 DIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYF 238
Cdd:cd01092    75 DLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVI 140
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 94-237 1.19e-09

Methionine Aminopeptidase 2. 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: 238521 [Multi-domain]  Cd Length: 291  Bit Score: 57.26  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSplgygrFPKSVctSVNNVLCHGIP---DSRPLQ 170
Cdd:cd01088     1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPA------FPVNL--SINECAAHYTPnagDDTVLK 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761607 171 DGDIINIDVTVYYNGYHGDTSETFlvgNVDESGKKLVEVARRCRDEAIAACRAGAPFS----VIGNTIRDY 237
Cdd:cd01088    73 EGDVVKLDFGAHVDGYIADSAFTV---DFDPKYDDLLEAAKEALNAAIKEAGPDVRLGeigeAIEEVIESY 140
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 94-230 1.68e-09

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: 56.43  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAypsPLGYGrfPKSVCTSVNNVLcHGIPDSRPLQDGD 173
Cdd:cd01087     1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA---RLAYS--YIVAAGSNAAIL-HYVHNDQPLKDGD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761607 174 IINIDVTVYYNGYHGDTSETFLVgnvdeSGK------KLVEVARRCRDEAIAACRAGAPFSVI 230
Cdd:cd01087    75 LVLIDAGAEYGGYASDITRTFPV-----NGKftdeqrELYEAVLAAQKAAIAACKPGVSYEDI 132
PRK09795 PRK09795
aminopeptidase; Provisional
 87-224 1.03e-06

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 48.78  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  87 EVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPlgygrFPKSVCTSVNNVLCHGIPDS 166
Cdd:PRK09795  126 QIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKAS-----FDTIVASGWRGALPHGKASD 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761607 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKK-----LVEVARRCRDEAIAACRAG 224
Cdd:PRK09795  201 KIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfnVYQIVLQAQLAAISAIRPG 263
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
 147-224 6.25e-06

Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.


Pssm-ID: 238522  Cd Length: 228  Bit Score: 45.79  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607 147 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDES---GKK--LVEVARRCRDEA 217
Cdd:cd01089    59 FP--TCISVNNCVCHFSPlksdATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtGKKadVIAAAHYALEAA 136


                  ....*..
gi 1039761607 218 IAACRAG 224
Cdd:cd01089   137 LRLLRPG 143
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 147-224 1.00e-05

42K curved DNA binding protein; Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein. [Unknown function, General]


Pssm-ID: 273105  Cd Length: 390  Bit Score: 45.65  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607 147 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDE---SGKK--LVEVARRCRDEA 217
Cdd:TIGR00495  78 FP--TCISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvTGRKadVIAAAHLAAEAA 155


                  ....*..
gi 1039761607 218 IAACRAG 224
Cdd:TIGR00495 156 LRLVKPG 162
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
 89-197 1.55e-05

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 45.10  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  89 KDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDA-YPSplgygrFPKSVCTSVNNVLCHGIPDSR 167
Cdd:PRK10879  174 KSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGArYPS------YNTIVGSGENGCILHYTENES 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039761607 168 PLQDGDIINIDVTVYYNGYHGDTSETFLVG 197
Cdd:PRK10879  248 EMRDGDLVLIDAGCEYKGYAGDITRTFPVN 277
PRK14576 PRK14576
putative endopeptidase; Provisional
 88-239 2.07e-05

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 45.01  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIrhdAYPSPlGYGRFpkSVCTSVNNVLCHGIPDSR 167
Cdd:PRK14576  177 IKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVM---SFPET-NFSRF--NLISVGDNFSPKIIADTT 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039761607 168 PLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:PRK14576  251 PAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIK 322
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 63-236 8.46e-04

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 40.08  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  63 PVPKRIKKPDYVTTGIVPDWGDSIEVKDEDQIQGLREACRLARHV------LLLAGKSLkVDMtTEEIDALVHwEIIRHD 136
Cdd:PTZ00053  127 PVGEIQEYPGENSSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVrryaqsVIKPGVKL-IDI-CERIESKSR-ELIEAD 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607 137 AYPSPLGygrFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSET--FlvgnvDESGKKLVEVAR 211
Cdd:PTZ00053  204 GLKCGWA---FPTGC--SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDCAFTvaF-----NPKYDPLLQATK 273

                         170       180
                  ....*....|....*....|....*
gi 1039761607 212 RCRDEAIAACRAGAPFSVIGNTIRD 236
Cdd:PTZ00053  274 DATNTGIKEAGIDVRLSDIGAAIQE 298
PRK15173 PRK15173
peptidase; Provisional
 88-239 1.17e-03

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 39.32  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHdaypSPLGYGRFPK-SVCTSVNNVLchgIPDS 166
Cdd:PRK15173   95 IKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRFHLiSVGADFSPKL---IPSN 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761607 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:PRK15173  168 TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIK 240
PRK14575 PRK14575
putative peptidase; Provisional
 88-239 1.69e-03

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 38.92  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761607  88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHdaypSPLGYGRFPK-SVCTSVNNVLchgIPDS 166
Cdd:PRK14575  178 IKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRFHLiSVGADFSPKL---IPSN 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761607 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIRDYFK 239
Cdd:PRK14575  251 TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIK 323
 
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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