|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
1-248 |
0e+00 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 523.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 1 MITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
Cdd:PRK12897 1 MITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 81 ADVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFS 160
Cdd:PRK12897 81 ADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKD 240
Cdd:PRK12897 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKD 240
|
....*...
gi 446551069 241 GPIILTKL 248
Cdd:PRK12897 241 GPIILTKL 248
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
2-248 |
1.99e-141 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 396.30 E-value: 1.99e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSV 161
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDG 241
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
....*..
gi 446551069 242 PIILTKL 248
Cdd:COG0024 241 PEILTLP 247
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
10-247 |
1.70e-127 |
|
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: 360.66 E-value: 1.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 10 IDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVARDFTGHG 169
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446551069 170 IGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDGPIILTK 247
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
2-248 |
2.05e-99 |
|
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: 290.02 E-value: 2.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSV 161
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDG 241
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 446551069 242 PIILTKL 248
Cdd:TIGR00500 241 PEILTER 247
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
11-239 |
1.72e-49 |
|
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: 161.25 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 11 DLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMY-LKKHGAtseqkGYNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGG-LSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVA-RDFTG 167
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYfPHGLG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551069 168 HGIGKEIHEEPAIFHfgkQGQGPQLQEGMVITIEPIVNIgmryskvdlngwtvrtMDGKLSAQYEHTIAITK 239
Cdd:pfam00557 156 HGIGLEVHEGPYISR---GGDDRVLEPGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVTE 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
1-248 |
0e+00 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 523.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 1 MITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
Cdd:PRK12897 1 MITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 81 ADVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFS 160
Cdd:PRK12897 81 ADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKD 240
Cdd:PRK12897 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKD 240
|
....*...
gi 446551069 241 GPIILTKL 248
Cdd:PRK12897 241 GPIILTKL 248
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
2-248 |
1.99e-141 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 396.30 E-value: 1.99e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSV 161
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDG 241
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
....*..
gi 446551069 242 PIILTKL 248
Cdd:COG0024 241 PEILTLP 247
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
10-247 |
1.70e-127 |
|
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: 360.66 E-value: 1.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 10 IDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVARDFTGHG 169
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446551069 170 IGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDGPIILTK 247
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
1-247 |
1.33e-126 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 358.68 E-value: 1.33e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 1 MITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
Cdd:PRK05716 2 AITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 81 ADVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFS 160
Cdd:PRK05716 82 SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKD 240
Cdd:PRK05716 162 VVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTED 241
|
....*..
gi 446551069 241 GPIILTK 247
Cdd:PRK05716 242 GPEILTL 248
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
2-248 |
2.05e-99 |
|
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: 290.02 E-value: 2.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSV 161
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKDG 241
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 446551069 242 PIILTKL 248
Cdd:TIGR00500 241 PEILTER 247
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
2-246 |
1.78e-98 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 287.89 E-value: 1.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
Cdd:PRK12896 8 MEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHGIPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSV 161
Cdd:PRK12896 88 PRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDFTGHGIGKEIHEEPAIFHF-GKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTIAITKD 240
Cdd:PRK12896 168 VRDLTGHGVGRSLHEEPSVILTyTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRD 247
|
....*.
gi 446551069 241 GPIILT 246
Cdd:PRK12896 248 GPEILT 253
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
1-246 |
2.17e-82 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 248.22 E-value: 2.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 1 MITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNG----YPYAICASVNDEMC 76
Cdd:PRK07281 1 MITLKSAREIEAMDRAGDFLASIHIGLRDLIKPGVDMWEVEEYVRRRCKEENVLPLQIGVDGammdYPYATCCGLNDEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 77 HAFPADVPLTEGNIVTIDTVV---------------------------NLNGGLSDSAWTYRVGKVSDEAEKLLLVAENA 129
Cdd:PRK07281 81 HAFPRHYILKEGDLLKVDMVLsepldksivdvsklnfdnveqmkkyteSYRGGLADSCWAYAVGTPSDEVKNLMDVTKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 130 LYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMR 209
Cdd:PRK07281 161 MYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLREGMVLTIEPMINTGTW 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 446551069 210 YSKVDLN-GWTVRTMDGKLSAQYEHTIAITKDGPIILT 246
Cdd:PRK07281 241 EIDTDMKtGWAHKTLDGGLSCQYEHQFVITKDGPVILT 278
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
2-248 |
3.55e-54 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 176.16 E-value: 3.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSEQKGYNG--YPYAICASVNDEMCHAF 79
Cdd:PRK12318 41 IIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 80 PADVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGF 159
Cdd:PRK12318 121 PNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 160 SVARDFTGHGIGKEIHEEPAIFHFGKQGQGPqLQEGMVITIEPIVNIGMRYSKVD-LNGWTVRTMDGKLSAQYEHTIAIT 238
Cdd:PRK12318 201 SVVDQFVGHGVGIKFHENPYVPHHRNSSKIP-LAPGMIFTIEPMINVGKKEGVIDpINHWEARTCDNQPSAQWEHTILIT 279
|
250
....*....|
gi 446551069 239 KDGPIILTKL 248
Cdd:PRK12318 280 ETGYEILTLL 289
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
2-247 |
6.59e-51 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 170.79 E-value: 6.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 2 ITIKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVemylkkHGATSEQKGYNG------YPYAICASVNDEM 75
Cdd:PLN03158 135 VEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVV------HEATIAAGGYPSplnyhfFPKSCCTSVNEVI 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 76 CHAFPADVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVT 155
Cdd:PLN03158 209 CHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHAT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 156 NEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPQLQEGMVITIEPIVNIGMRYSKVDLNGWTVRTMDGKLSAQYEHTI 235
Cdd:PLN03158 289 MSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTL 368
|
250
....*....|..
gi 446551069 236 AITKDGPIILTK 247
Cdd:PLN03158 369 LVTETGVEVLTA 380
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
11-239 |
1.72e-49 |
|
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: 161.25 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 11 DLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMY-LKKHGAtseqkGYNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGG-LSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVA-RDFTG 167
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYfPHGLG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446551069 168 HGIGKEIHEEPAIFHfgkQGQGPQLQEGMVITIEPIVNIgmryskvdlngwtvrtMDGKLSAQYEHTIAITK 239
Cdd:pfam00557 156 HGIGLEVHEGPYISR---GGDDRVLEPGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVTE 208
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
4-248 |
2.44e-39 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 138.03 E-value: 2.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 4 IKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGAtseqkgyNGYPYA-ICAS-VNDEMCHAFPA 81
Cdd:COG0006 73 IKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGA-------EGPSFDtIVASgENAAIPHYTPT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 82 DVPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFsv 161
Cdd:COG0006 146 DRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGY-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 162 ARDF---TGHGIGKEIHEEPAIfhfgKQGQGPQLQEGMVITIEPIVnigmrYSKvdlNGWTVRTmdgklsaqyEHTIAIT 238
Cdd:COG0006 224 GEYFphgTGHGVGLDVHEGPQI----SPGNDRPLEPGMVFTIEPGI-----YIP---GIGGVRI---------EDTVLVT 282
|
250
....*....|
gi 446551069 239 KDGPIILTKL 248
Cdd:COG0006 283 EDGAEVLTRL 292
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
10-242 |
1.94e-35 |
|
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 125.26 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 10 IDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGatseqkGYNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGARTALPHYRPDDRRLQEGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVAR-DFTGH 168
Cdd:cd01066 75 LVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgHRTGH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446551069 169 GIGKEIHEEPAIFHFGKQgqgpQLQEGMVITIEPIVNIGMRYskvdlngwtvrtmdgklSAQYEHTIAITKDGP 242
Cdd:cd01066 155 GIGLEIHEPPVLKAGDDT----VLEPGMVFAVEPGLYLPGGG-----------------GVRIEDTVLVTEDGP 207
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
10-202 |
2.10e-27 |
|
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: 104.13 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 10 IDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSE------QKGYNGypyaicasvndEMCHAFPADV 83
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPsfdtivASGPNS-----------ALPHGVPSDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 84 PLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFsvAR 163
Cdd:cd01092 70 KIEEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY--GE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446551069 164 DF---TGHGIGKEIHEEPAIFHFGKQgqgpQLQEGMVITIEP 202
Cdd:cd01092 148 YFihrTGHGVGLEVHEAPYISPGSDD----VLEEGMVFTIEP 185
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
15-210 |
3.50e-25 |
|
methionine aminopeptidase, type II; Methionine aminopeptidase (map) 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. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation. [Protein fate, Protein modification and repair]
Pssm-ID: 129592 Cd Length: 295 Bit Score: 100.63 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 15 ESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSeqkgynGYPYAIcaSVNDEMCHAFPA---DVPLTEGNIV 91
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP------AFPCNI--SINECAAHFTPKagdKTVFKDGDVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 92 TIDTVVNLNGGLSDSAWTYRVGKVSDEaekLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVARDFTGHGIG 171
Cdd:TIGR00501 82 KLDLGAHVDGYIADTAITVDLGDQYDN---LVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSMA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446551069 172 K-EIHEEPAIFHFgKQGQGPQLQEGMVITIEPIVNIGMRY 210
Cdd:TIGR00501 159 PyRLHGGKSIPNV-KERDTTKLEEGDVVAIEPFATDGVGY 197
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
15-247 |
3.96e-24 |
|
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: 97.71 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 15 ESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATSeqkgynGYPYAIcaSVNDEMCHAFPA---DVPLTEGNIV 91
Cdd:cd01088 6 EAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGP------AFPVNL--SINECAAHYTPNagdDTVLKEGDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 92 TIDTVVNLNGGLSDSAWTYRVGKVSDEaekLLLVAENALYKGIDQAVIGNHVGDIGYAIESYVTNEGFSVARDFTGHGIG 171
Cdd:cd01088 78 KLDFGAHVDGYIADSAFTVDFDPKYDD---LLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 172 K-EIHEEPAIFHFgKQGQGPQLQEGMVITIEPI-------------VNIGMRYSKVDL---------------------- 215
Cdd:cd01088 155 RyRLHAGKSIPNV-KGGEGTRLEEGDVYAIEPFattgkgyvhdgpeCSIYMLNRDKPLrlprarklldviyenfgtlpfa 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446551069 216 NGWTVRTM--------------------------DGKLSAQYEHTIAITKDGPIILTK 247
Cdd:cd01088 234 RRWLDRLGetkllmalknlckagivypypvlkeiSGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
10-247 |
4.44e-12 |
|
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: 63.75 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 10 IDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGATseqkgyNGYPYAICASVNDEMCHAFPADVPLTEGN 89
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGAR------LAYSYIVAAGSNAAILHYVHNDQPLKDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGGLSDSAWTYRV-GKVSDEAEKLLLVAENALYKGIDQA---------------VIGNHVGDIGYAIESY 153
Cdd:cd01087 75 LVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACkpgvsyedihllahrVLAEGLKELGILKGDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 154 VTNEGFSVARDF----TGHGIGKEIHEEPAIFHFGKQGQgpQLQEGMVITIEPIVNIGMRYSKVD--LNGWTVRTmdgkl 227
Cdd:cd01087 155 DEIVESGAYAKFfphgLGHYLGLDVHDVGGYLRYLRRAR--PLEPGMVITIEPGIYFIPDLLDVPeyFRGGGIRI----- 227
|
250 260
....*....|....*....|
gi 446551069 228 saqyEHTIAITKDGPIILTK 247
Cdd:cd01087 228 ----EDDVLVTEDGPENLTR 243
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
4-202 |
1.12e-10 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 60.72 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 4 IKTKNEIDLMHESGKLLASCHKEIAKMIKPGITTQEIDTFVEMYLKKHGAtsEQKGYNgypyAICAS-VNDEMCHAFPAD 82
Cdd:PRK09795 127 IKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGA--EKASFD----TIVASgWRGALPHGKASD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 83 VPLTEGNIVTIDTVVNLNGGLSDSAWTYRVGKVSDEAE--------KLLLVAENALYKGIDQAVIGNHVGDigyAIESYV 154
Cdd:PRK09795 201 KIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEshplfnvyQIVLQAQLAAISAIRPGVRCQQVDD---AARRVI 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446551069 155 TNEGFSvarDF----TGHGIGKEIHEEPaifHFGKQgQGPQLQEGMVITIEP 202
Cdd:PRK09795 278 TEAGYG---DYfghnTGHAIGIEVHEDP---RFSPR-DTTTLQPGMLLTVEP 322
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
21-175 |
9.10e-08 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 52.02 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 21 ASCHKEIAKM----IKPGIT----TQEIDTFVEMYLKKHGATSEQkgynGYPYAiCaSVNDEMCHAFPA---DVPLTEGN 89
Cdd:PTZ00053 165 AEVHRQVRRYaqsvIKPGVKlidiCERIESKSRELIEADGLKCGW----AFPTG-C-SLNHCAAHYTPNtgdKTVLTYDD 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 90 IVTIDTVVNLNGGLSDSAWTYrvgKVSDEAEKLLLVAENALYKGIDQAVIGNHVGDIGYAI----ESY---VTNEGFSVA 162
Cdd:PTZ00053 239 VCKLDFGTHVNGRIIDCAFTV---AFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIqeviESYeveIKGKTYPIK 315
|
170
....*....|....*.
gi 446551069 163 --RDFTGHGIGK-EIH 175
Cdd:PTZ00053 316 siRNLNGHSIGPyIIH 331
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
25-246 |
2.29e-05 |
|
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: 44.24 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 25 KEIAKMIKPGITTQEI----DTFVEMYLKKHgATSEQKGYNGYPYAICASVNDEMCHAFP----ADVPLTEGNIVTIDTV 96
Cdd:cd01089 16 KQVISLCVPGAKVVDLcekgDKLILEELGKV-YKKEKKLEKGIAFPTCISVNNCVCHFSPlksdATYTLKDGDVVKIDLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 97 VNLNGGLSDSAWTYRVGKVSDE-----AEKLLLVAENALYKGIDQAVIGNHVGDIGYAIEsyvtnegfSVARDFTGHGI- 170
Cdd:cd01089 95 CHIDGYIAVVAHTIVVGAEAETpvtgkKADVIAAAHYALEAALRLLRPGNQNSDITEAIQ--------KVIVDYGCTPVe 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 171 GKEIHEEPAIFHFGKqGQgPQLQE----GMVITIEPIvnigmrYSKvdlngwtvrtmDGKLSAQYEHTIAITKDGPIILT 246
Cdd:cd01089 167 GVLSHQLKRVVSSGE-GK-AKLVEcvkhGLLFPYPVL------YEK-----------EGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
166-202 |
4.12e-03 |
|
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: 37.54 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446551069 166 TGHGIGK--EIHEEPAifHFGKQGQGPQLQEGMVITIEP 202
Cdd:cd01085 160 TGHGVGSflNVHEGPQ--SISPAPNNVPLKAGMILSNEP 196
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
25-118 |
5.09e-03 |
|
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: 37.56 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446551069 25 KEIAKMIKPGITTQEI----DTFVEMYLKKHgATSEQKGYNGYPYAICASVNDEMCHAFP----ADVPLTEGNIVTIDTV 96
Cdd:TIGR00495 35 KSVVEACSPGAKVVDIcekgDAFIMEETAKI-FKKEKEMEKGIAFPTCISVNNCVGHFSPlksdQDYILKEGDVVKIDLG 113
|
90 100
....*....|....*....|..
gi 446551069 97 VNLNGGLSDSAWTYRVGKVSDE 118
Cdd:TIGR00495 114 CHIDGFIALVAHTFVVGVAQEE 135
|
|
| |
