|
Name |
Accession |
Description |
Interval |
E-value |
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
94-234 |
2.54e-77 |
|
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: 233.92 E-value: 2.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGD 173
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761605 174 IINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAI 141
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
55-247 |
1.08e-75 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 235.12 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 55 PAAVSPAHPVPKRIKKPDYVTTGI-----VPDWGDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVH 129
Cdd:PLN03158 99 PYPISPRRVVPDHIPKPDWALDGTpkiepNSDLQHSVEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 130 WEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEV 209
Cdd:PLN03158 179 EATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKC 258
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039761605 210 ARRCRDEAIAACRAGAPFSVIGNTISRR----GQRTLDSYSG 247
Cdd:PLN03158 259 TYECLEKAIAIVKPGVRYREVGEVINRHatmsGLSVVKSYCG 300
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
86-234 |
4.99e-73 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 223.34 E-value: 4.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039761605 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAI 149
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
86-234 |
1.30e-56 |
|
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: 181.39 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039761605 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
95-234 |
2.42e-36 |
|
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: 128.13 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 95 QGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYpsplGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDI 174
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761605 175 INIDVTVYYN-GYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:pfam00557 77 VLIDVGAEYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAA 137
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
94-234 |
2.54e-77 |
|
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: 233.92 E-value: 2.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGD 173
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761605 174 IINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAI 141
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
55-247 |
1.08e-75 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 235.12 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 55 PAAVSPAHPVPKRIKKPDYVTTGI-----VPDWGDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVH 129
Cdd:PLN03158 99 PYPISPRRVVPDHIPKPDWALDGTpkiepNSDLQHSVEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 130 WEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEV 209
Cdd:PLN03158 179 EATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKC 258
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039761605 210 ARRCRDEAIAACRAGAPFSVIGNTISRR----GQRTLDSYSG 247
Cdd:PLN03158 259 TYECLEKAIAIVKPGVRYREVGEVINRHatmsGLSVVKSYCG 300
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
86-234 |
4.99e-73 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 223.34 E-value: 4.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039761605 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAI 149
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
85-247 |
1.11e-68 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 212.30 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 85 SIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIP 164
Cdd:PRK05716 2 AITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 165 DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIG----NTISRRGQR 240
Cdd:PRK05716 82 SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGhaiqKYAEAEGFS 161
|
....*..
gi 1039761605 241 TLDSYSG 247
Cdd:PRK05716 162 VVREYCG 168
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
83-235 |
3.68e-59 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 188.12 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 83 GDSIEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHG 162
Cdd:PRK12896 5 GRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHG 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761605 163 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIS 235
Cdd:PRK12896 85 IPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIE 157
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
86-234 |
1.30e-56 |
|
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: 181.39 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039761605 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
86-234 |
3.42e-46 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 156.13 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGR--FPKSVCTSVNNVLCHGI 163
Cdd:PRK12318 41 IIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGI 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761605 164 PDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:PRK12318 121 PNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVI 191
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
95-234 |
2.42e-36 |
|
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: 128.13 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 95 QGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYpsplGYGRFPKSVCTSVNNVLCHGIPDSRPLQDGDI 174
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039761605 175 INIDVTVYYN-GYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTI 234
Cdd:pfam00557 77 VLIDVGAEYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAA 137
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
94-236 |
1.30e-28 |
|
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: 107.92 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPlgygrfpkSVCTSVNNV--LCHGIPDSRPLQD 171
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQE 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039761605 172 GDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISR 236
Cdd:cd01066 73 GDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAARE 137
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
88-230 |
6.88e-25 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 100.28 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDA-YPSplgygrFPKSVCTSVNNVLCHGIPDS 166
Cdd:COG0006 73 IKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAeGPS------FDTIVASGENAAIPHYTPTD 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039761605 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVI 230
Cdd:COG0006 147 RPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEV 210
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
86-245 |
1.81e-23 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 95.49 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 86 IEVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPLGYGRFPKSVCTSVNNVLCHGIPD 165
Cdd:PRK12897 2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 166 SRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRcrdeaiaACRAGAPFSVIGNTISRRGQrTLDSY 245
Cdd:PRK12897 82 DVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAEN-------ALYKGIDQAVIGNRVGDIGY-AIESY 153
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
94-230 |
9.42e-22 |
|
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: 89.88 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAY-PSplgygrFPKSVCTSVNNVLCHGIPDSRPLQDG 172
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039761605 173 DIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGAPFSVI 230
Cdd:cd01092 75 DLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEV 132
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
94-245 |
3.08e-10 |
|
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: 59.19 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSplgygrFPKSVctSVNNVLCHGIP---DSRPLQ 170
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPA------FPVNL--SINECAAHYTPnagDDTVLK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039761605 171 DGDIINIDVTVYYNGYHGDTSETFlvgNVDESGKKLVEVARRCRDEAIAACRAGAPFSVIGNTIsrrgQRTLDSY 245
Cdd:cd01088 73 EGDVVKLDFGAHVDGYIADSAFTV---DFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAI----EEVIESY 140
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
94-230 |
1.62e-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: 56.81 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 94 IQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAypsPLGYGrfPKSVCTSVNNVLcHGIPDSRPLQDGD 173
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGA---RLAYS--YIVAAGSNAAIL-HYVHNDQPLKDGD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761605 174 IINIDVTVYYNGYHGDTSETFLVgnvdeSGK------KLVEVARRCRDEAIAACRAGAPFSVI 230
Cdd:cd01087 75 LVLIDAGAEYGGYASDITRTFPV-----NGKftdeqrELYEAVLAAQKAAIAACKPGVSYEDI 132
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
87-224 |
1.85e-06 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 48.40 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 87 EVKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDAYPSPlgygrFPKSVCTSVNNVLCHGIPDS 166
Cdd:PRK09795 126 QIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKAS-----FDTIVASGWRGALPHGKASD 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039761605 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 |
6.27e-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: 46.17 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 147 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDES---GKK--LVEVARRCRDEA 217
Cdd:cd01089 59 FP--TCISVNNCVCHFSPlksdATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtGKKadVIAAAHYALEAA 136
|
....*..
gi 1039761605 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 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 147 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDE---SGKK--LVEVARRCRDEA 217
Cdd:TIGR00495 78 FP--TCISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvTGRKadVIAAAHLAAEAA 155
|
....*..
gi 1039761605 218 IAACRAG 224
Cdd:TIGR00495 156 LRLVKPG 162
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
89-197 |
1.87e-05 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 45.49 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 89 KDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHDA-YPSplgygrFPKSVCTSVNNVLCHGIPDSR 167
Cdd:PRK10879 174 KSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGArYPS------YNTIVGSGENGCILHYTENES 247
|
90 100 110
....*....|....*....|....*....|
gi 1039761605 168 PLQDGDIINIDVTVYYNGYHGDTSETFLVG 197
Cdd:PRK10879 248 EMRDGDLVLIDAGCEYKGYAGDITRTFPVN 277
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
88-211 |
7.44e-05 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 43.47 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIrhdAYPSPlGYGRFpkSVCTSVNNVLCHGIPDSR 167
Cdd:PRK14576 177 IKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVM---SFPET-NFSRF--NLISVGDNFSPKIIADTT 250
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039761605 168 PLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVAR 211
Cdd:PRK14576 251 PAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIR 294
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
63-245 |
1.76e-04 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 42.39 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 63 PVPKRIKKPDYVTTGIVPDWGDSIEVKDEDQIQGLREACRLARHV------LLLAGKSLkVDMtTEEIDALVHwEIIRHD 136
Cdd:PTZ00053 127 PVGEIQEYPGENSSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVrryaqsVIKPGVKL-IDI-CERIESKSR-ELIEAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 137 AYPSPLGygrFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSET--FlvgnvDESGKKLVEVAR 211
Cdd:PTZ00053 204 GLKCGWA---FPTGC--SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDCAFTvaF-----NPKYDPLLQATK 273
|
170 180 190
....*....|....*....|....*....|....
gi 1039761605 212 RCRDEAIAACRAGAPFSVIGNTIsrrgQRTLDSY 245
Cdd:PTZ00053 274 DATNTGIKEAGIDVRLSDIGAAI----QEVIESY 303
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
88-262 |
1.33e-03 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 39.32 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHdaypSPLGYGRFPK-SVCTSVNNVLchgIPDS 166
Cdd:PRK15173 95 IKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRFHLiSVGADFSPKL---IPSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGApfsvigntisrRGQRTLDSYS 246
Cdd:PRK15173 168 TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGV-----------KMKDVFDSTM 236
|
170
....*....|....*.
gi 1039761605 247 GILWSSAFMAVSKGHV 262
Cdd:PRK15173 237 EVIKKSGLPNYNRGHL 252
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
88-262 |
2.02e-03 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 38.92 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 88 VKDEDQIQGLREACRLARHVLLLAGKSLKVDMTTEEIDALVHWEIIRHdaypSPLGYGRFPK-SVCTSVNNVLchgIPDS 166
Cdd:PRK14575 178 IKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRFHLiSVGADFSPKL---IPSN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039761605 167 RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDESGKKLVEVARRCRDEAIAACRAGApfsvigntisrRGQRTLDSYS 246
Cdd:PRK14575 251 TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGV-----------KMKDVFDSTM 319
|
170
....*....|....*.
gi 1039761605 247 GILWSSAFMAVSKGHV 262
Cdd:PRK14575 320 EVIKKSGLPNYNRGHL 335
|
|
|