|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
69-314 |
1.64e-147 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 414.40 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 69 VYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGT 148
Cdd:COG0024 3 IKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 149 VLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR 228
Cdd:COG0024 83 VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 229 DFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGA 308
Cdd:COG0024 163 EFVGHGIGREMHEEPQVPNYG-RPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGP 241
|
....*.
gi 2197366932 309 EILTLP 314
Cdd:COG0024 242 EILTLP 247
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
66-314 |
4.75e-140 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 395.66 E-value: 4.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 66 ASDVYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIP 145
Cdd:PRK05716 2 AITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 146 DGTVLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYG 225
Cdd:PRK05716 82 SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 226 VVRDFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTE 305
Cdd:PRK05716 162 VVREYCGHGIGRKFHEEPQIPHYG-APGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTE 240
|
....*....
gi 2197366932 306 DGAEILTLP 314
Cdd:PRK05716 241 DGPEILTLR 249
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
75-313 |
3.00e-136 |
|
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: 385.69 E-value: 3.00e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGTVLEDGD 154
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 155 IVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFIGHG 234
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2197366932 235 VGVDFHSGLVIPHYdAAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGAEILTL 313
Cdd:cd01086 161 IGRKFHEEPQIPNY-GRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
69-313 |
8.03e-112 |
|
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: 323.92 E-value: 8.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 69 VYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGT 148
Cdd:TIGR00500 3 LKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 149 VLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR 228
Cdd:TIGR00500 83 VLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 229 DFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGA 308
Cdd:TIGR00500 163 EYCGHGIGRKFHEEPQIPNYG-KKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGP 241
|
....*
gi 2197366932 309 EILTL 313
Cdd:TIGR00500 242 EILTE 246
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
77-305 |
2.07e-61 |
|
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: 194.38 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 77 RIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYpsclGYRGFPRSICTSVNEVICHGIPDGTVLEDGDIV 156
Cdd:pfam00557 2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 157 NLDITA-YKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYG-VVRDFIGHG 234
Cdd:pfam00557 78 LIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGHG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197366932 235 VGVDFHSGLVIPHydaaPAHNRLMVPGMVFTIEPMITlggidweqWDDGWTVVtkdrrrtaQFEHTLVVTE 305
Cdd:pfam00557 158 IGLEVHEGPYISR----GGDDRVLEPGMVFTIEPGIY--------FIPGWGGV--------RIEDTVLVTE 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
69-314 |
1.64e-147 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 414.40 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 69 VYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGT 148
Cdd:COG0024 3 IKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 149 VLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR 228
Cdd:COG0024 83 VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 229 DFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGA 308
Cdd:COG0024 163 EFVGHGIGREMHEEPQVPNYG-RPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGP 241
|
....*.
gi 2197366932 309 EILTLP 314
Cdd:COG0024 242 EILTLP 247
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
66-314 |
4.75e-140 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 395.66 E-value: 4.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 66 ASDVYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIP 145
Cdd:PRK05716 2 AITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 146 DGTVLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYG 225
Cdd:PRK05716 82 SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 226 VVRDFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTE 305
Cdd:PRK05716 162 VVREYCGHGIGRKFHEEPQIPHYG-APGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTE 240
|
....*....
gi 2197366932 306 DGAEILTLP 314
Cdd:PRK05716 241 DGPEILTLR 249
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
75-313 |
3.00e-136 |
|
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: 385.69 E-value: 3.00e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGTVLEDGD 154
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 155 IVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFIGHG 234
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2197366932 235 VGVDFHSGLVIPHYdAAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGAEILTL 313
Cdd:cd01086 161 IGRKFHEEPQIPNY-GRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
72-314 |
1.58e-130 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 371.86 E-value: 1.58e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 72 AEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGTVLE 151
Cdd:PRK12896 13 PRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHGIPGPRVIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 152 DGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFI 231
Cdd:PRK12896 93 DGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 232 GHGVGVDFHSGL-VIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGAEI 310
Cdd:PRK12896 173 GHGVGRSLHEEPsVILTYT-DPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEI 251
|
....
gi 2197366932 311 LTLP 314
Cdd:PRK12896 252 LTDR 255
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
69-313 |
8.03e-112 |
|
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: 323.92 E-value: 8.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 69 VYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGT 148
Cdd:TIGR00500 3 LKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 149 VLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR 228
Cdd:TIGR00500 83 VLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 229 DFIGHGVGVDFHSGLVIPHYDaAPAHNRLMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGA 308
Cdd:TIGR00500 163 EYCGHGIGRKFHEEPQIPNYG-KKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGP 241
|
....*
gi 2197366932 309 EILTL 313
Cdd:TIGR00500 242 EILTE 246
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
73-312 |
2.83e-101 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 302.53 E-value: 2.83e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 73 EGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGTVLED 152
Cdd:PLN03158 141 EQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLED 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 153 GDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFIG 232
Cdd:PLN03158 221 GDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 233 HGVGVDFHSGLVIPHYdaapAHNR---LMVPGMVFTIEPMITLGGIDWEQWDDGWTVVTKDRRRTAQFEHTLVVTEDGAE 309
Cdd:PLN03158 301 HGIGELFHCAPNIPHY----ARNKavgVMKAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVE 376
|
...
gi 2197366932 310 ILT 312
Cdd:PLN03158 377 VLT 379
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
71-313 |
2.07e-78 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 240.49 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 71 DAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRG--FPRSICTSVNEVICHGIPDGT 148
Cdd:PRK12318 45 TPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGIPNDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 149 VLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR 228
Cdd:PRK12318 125 PLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVVD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 229 DFIGHGVGVDFHSGLVIPHYdaapaHNR---LMVPGMVFTIEPMITLGG----IDWEqwdDGWTVVTKDRRRTAQFEHTL 301
Cdd:PRK12318 205 QFVGHGVGIKFHENPYVPHH-----RNSskiPLAPGMIFTIEPMINVGKkegvIDPI---NHWEARTCDNQPSAQWEHTI 276
|
250
....*....|..
gi 2197366932 302 VVTEDGAEILTL 313
Cdd:PRK12318 277 LITETGYEILTL 288
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
77-305 |
2.07e-61 |
|
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: 194.38 E-value: 2.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 77 RIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYpsclGYRGFPRSICTSVNEVICHGIPDGTVLEDGDIV 156
Cdd:pfam00557 2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 157 NLDITA-YKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYG-VVRDFIGHG 234
Cdd:pfam00557 78 LIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGHG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197366932 235 VGVDFHSGLVIPHydaaPAHNRLMVPGMVFTIEPMITlggidweqWDDGWTVVtkdrrrtaQFEHTLVVTE 305
Cdd:pfam00557 158 IGLEVHEGPYISR----GGDDRVLEPGMVFTIEPGIY--------FIPGWGGV--------RIEDTVLVTE 208
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
75-312 |
1.45e-54 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 178.30 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCLGYRGFPRSICTSVNEVICHGIPDGTVLEDGD 154
Cdd:PRK12897 10 IDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPADVPLTEGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 155 IVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFIGHG 234
Cdd:PRK12897 90 IVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVARDFTGHG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2197366932 235 VGVDFHSGLVIPHYDAAPAHNRLMvPGMVFTIEPMITLgGIDWEQWD-DGWTVVTKDRRRTAQFEHTLVVTEDGAEILT 312
Cdd:PRK12897 170 IGKEIHEEPAIFHFGKQGQGPELQ-EGMVITIEPIVNV-GMRYSKVDlNGWTARTMDGKLSAQYEHTIAITKDGPIILT 246
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
50-312 |
2.10e-42 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 148.04 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 50 IVRPEYVGRATVDEGNASD----VYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYpsclgY 125
Cdd:COG0006 50 FVDELEAERELVDASDLLEelraIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAE-----G 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 126 RGFPRSICTSVNEVICHGIPDGTVLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPG 205
Cdd:COG0006 125 PSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 206 REINVIGRAIESYARRFGYGvvRDFI---GHGVGVDFHSGlviPHYdaAPAHNRLMVPGMVFTIEPMItlggidweqWDD 282
Cdd:COG0006 205 VTGGEVDAAARDVLAEAGYG--EYFPhgtGHGVGLDVHEG---PQI--SPGNDRPLEPGMVFTIEPGI---------YIP 268
|
250 260 270
....*....|....*....|....*....|
gi 2197366932 283 GWTVVtkdrrRTaqfEHTLVVTEDGAEILT 312
Cdd:COG0006 269 GIGGV-----RI---EDTVLVTEDGAEVLT 290
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
75-308 |
9.93e-40 |
|
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: 138.36 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPsclgyrgfPRSICTSVNEV--ICHGIPDGTVLED 152
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYP--------AGPTIVGSGARtaLPHYRPDDRRLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 153 GDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVR-DFI 231
Cdd:cd01066 73 GDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgHRT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197366932 232 GHGVGVDFHSGLVIPHYDAAPahnrlMVPGMVFTIEPMITLGGIdweqwddgwtvvtkdrrRTAQFEHTLVVTEDGA 308
Cdd:cd01066 153 GHGIGLEIHEPPVLKAGDDTV-----LEPGMVFAVEPGLYLPGG-----------------GGVRIEDTVLVTEDGP 207
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
96-312 |
1.01e-37 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 135.36 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 96 IRPGITTDELDRIAHEFIVAAGAYPSCLGYRG----FPRSICTSVNEVICHGIPDGTVLEDGDIVNLDIT---------- 161
Cdd:PRK07281 31 IKPGVDMWEVEEYVRRRCKEENVLPLQIGVDGammdYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMVlsepldksiv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 162 ------------------AYKDGVhGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFG 223
Cdd:PRK07281 111 dvsklnfdnveqmkkyteSYRGGL-ADSCWAYAVGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 224 YGVVRDFIGHGVGVDFHSGLVIPHYDAAPAHNRLMvPGMVFTIEPMITLGgiDWEQWDD---GWTVVTKDRRRTAQFEHT 300
Cdd:PRK07281 190 YGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLR-EGMVLTIEPMINTG--TWEIDTDmktGWAHKTLDGGLSCQYEHQ 266
|
250
....*....|..
gi 2197366932 301 LVVTEDGAEILT 312
Cdd:PRK07281 267 FVITKDGPVILT 278
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
75-290 |
1.75e-35 |
|
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: 127.24 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAY-PSclgyrgFPRSICTSVNEVICHGIPDGTVLEDG 153
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 154 DIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGreinVIGRAIESYARRF----GYGvvRD 229
Cdd:cd01092 75 DLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPG----VTAKEVDKAARDVieeaGYG--EY 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197366932 230 FI---GHGVGVDFHSGlviPhyDAAPAHNRLMVPGMVFTIEPMITL---GGIDWEqwDDGwtVVTKD 290
Cdd:cd01092 149 FIhrtGHGVGLEVHEA---P--YISPGSDDVLEEGMVFTIEPGIYIpgkGGVRIE--DDV--LVTED 206
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
78-312 |
8.21e-30 |
|
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: 114.65 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 78 IREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPsclgyrGFPRSIctSVNEVICHGIP---DGTVLEDGD 154
Cdd:cd01088 4 YREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGP------AFPVNL--SINECAAHYTPnagDDTVLKEGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 155 IVNLDITAYKDGVHGDHNRTYlvgDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGVVRDFIGHG 234
Cdd:cd01088 76 VVKLDFGAHVDGYIADSAFTV---DFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTGHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 235 VGV-DFHSGLVIPHYDAapAHNRLMVPGMVFTIEPMITLGG-------------------------------ID------ 276
Cdd:cd01088 153 IERyRLHAGKSIPNVKG--GEGTRLEEGDVYAIEPFATTGKgyvhdgpecsiymlnrdkplrlprarklldvIYenfgtl 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 277 --WEQWDDGWTV--------------------VTKDRRR--TAQFEHTLVVTEDGAEILT 312
Cdd:cd01088 231 pfARRWLDRLGEtkllmalknlckagivypypVLKEISGgyVAQFEHTIIVREDGKEVTT 290
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
72-314 |
3.81e-17 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 80.75 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 72 AEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAYPSCL------GYRGfprsictsvneVICHGIP 145
Cdd:PRK09795 130 PEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFdtivasGWRG-----------ALPHGKA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 146 DGTVLEDGDIVNLDITAYKDGVHGDHNRTYLVG--DVDEESRLLV---ERTEEALRRGIKAVKPGreinVIGRAIESYAR 220
Cdd:PRK09795 199 SDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNgeGVSAESHPLFnvyQIVLQAQLAAISAIRPG----VRCQQVDDAAR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 221 RF----GYGvvrDFI----GHGVGVDFHSGlviPHYdaAPAHNRLMVPGMVFTIEPMITLGGidweqwddgwtvvtkdrR 292
Cdd:PRK09795 275 RViteaGYG---DYFghntGHAIGIEVHED---PRF--SPRDTTTLQPGMLLTVEPGIYLPG-----------------Q 329
|
250 260
....*....|....*....|...
gi 2197366932 293 RTAQFEHTLVVTEDGAEIL-TLP 314
Cdd:PRK09795 330 GGVRIEDVVLVTPQGAEVLyAMP 352
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
75-312 |
1.58e-16 |
|
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: 77.23 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELDR-IAHEFIVAAG--AYPsclgyrgfPRSICTSvNEVICHGIPDGTVLE 151
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAeFEYEFRSRGArlAYS--------YIVAAGS-NAAILHYVHNDQPLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 152 DGDIVNLDITAYKDGVHGDHNRTYLV-GDVDEESRLLVERTEEALRRGIKAVKPGREINVI----GRAIESYARRFGY-- 224
Cdd:cd01087 72 DGDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGIlk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 225 ---------GVVRDF----IGHGVGVDFH-SGLVIPHYDAapahNRLMVPGMVFTIEPmitlgGIDWEQWDDgwtvvtkD 290
Cdd:cd01087 152 gdvdeivesGAYAKFfphgLGHYLGLDVHdVGGYLRYLRR----ARPLEPGMVITIEP-----GIYFIPDLL-------D 215
|
250 260
....*....|....*....|....*..
gi 2197366932 291 RRRTAQF-----EHTLVVTEDGAEILT 312
Cdd:cd01087 216 VPEYFRGggiriEDDVLVTEDGPENLT 242
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
72-312 |
7.63e-13 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 68.60 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 72 AEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELD-RIAHEFIVAAGAYPSclgyrgFPRSICTSVNEVICHGIPDGTVL 150
Cdd:PRK10879 176 PEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEgEIHHEFNRHGARYPS------YNTIVGSGENGCILHYTENESEM 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 151 EDGDIVNLDITAYKDGVHGDHNRTYLV-GDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRA--------------- 214
Cdd:PRK10879 250 RDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEvvrimvsglvklgil 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 215 -------IESYARR--FGYGvvrdfIGHGVGVDFHSglvIPHYdaAPAHNRLMVPGMVFTIEPMITLGgidweqwDDGwT 285
Cdd:PRK10879 330 kgdvdqlIAENAHRpfFMHG-----LSHWLGLDVHD---VGVY--GQDRSRILEPGMVLTVEPGLYIA-------PDA-D 391
|
250 260
....*....|....*....|....*..
gi 2197366932 286 VVTKDRRRTAQFEHTLVVTEDGAEILT 312
Cdd:PRK10879 392 VPEQYRGIGIRIEDDIVITETGNENLT 418
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
79-312 |
2.71e-10 |
|
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: 59.27 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 79 REAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVA--AGAYPSCLG-YRGFPRSICTSVNEVICHGIP----DGTVLE 151
Cdd:cd01089 5 KTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEelGKVYKKEKKlEKGIAFPTCISVNNCVCHFSPlksdATYTLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 152 DGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRL-----LVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGYGV 226
Cdd:cd01089 85 DGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTgkkadVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDYGCTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 227 VRDFIGHGVGVDFHSGlviphyDAAPAHNRLMVPGMVFTIEPMItlggidweqwddgwtvvTKDRRRTAQFEHTLVVTED 306
Cdd:cd01089 165 VEGVLSHQLKRVVSSG------EGKAKLVECVKHGLLFPYPVLY-----------------EKEGEVVAQFKLTVLLTPN 221
|
....*.
gi 2197366932 307 GAEILT 312
Cdd:cd01089 222 GVTVLT 227
|
|
| Creatinase |
cd01090 |
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea. |
78-312 |
1.45e-08 |
|
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
Pssm-ID: 238523 [Multi-domain] Cd Length: 228 Bit Score: 54.47 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 78 IREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGAypsclgyRGFPRS--------ICTSVNEVICHGIPDGTV 149
Cdd:cd01090 4 IRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIA-------KTFPEVelmdtwtwFQSGINTDGAHNPVTNRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 150 LEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPG-------REINVIGRAIESYA-RR 221
Cdd:cd01090 77 VQRGDILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGarckdiaAELNEMYREHDLLRyRT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 222 FGYGvvrdfighgvgvdfHSGLVIPHYDAAPAHNRL-------MVPGMVFTIEPMITLGgiDWEQWDDGWTvvtkdrrrt 294
Cdd:cd01090 157 FGYG--------------HSFGVLSHYYGREAGLELredidtvLEPGMVVSMEPMIMLP--EGQPGAGGYR--------- 211
|
250
....*....|....*....
gi 2197366932 295 aqfEH-TLVVTEDGAEILT 312
Cdd:cd01090 212 ---EHdILVINENGAENIT 227
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
66-233 |
1.49e-07 |
|
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: 52.20 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 66 ASDVYDAEGIGRIREAGRIAAQAMEHTAEHIRPGITTDELDRIAHEFIVAAGA--YPSCLG-YRGFPRSICTSVNEVICH 142
Cdd:TIGR00495 11 AYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAkiFKKEKEmEKGIAFPTCISVNNCVGH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 143 GIP----DGTVLEDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRL-----LVERTEEALRRGIKAVKPGREINVIGR 213
Cdd:TIGR00495 91 FSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTgrkadVIAAAHLAAEAALRLVKPGNTNTQVTE 170
|
170 180
....*....|....*....|
gi 2197366932 214 AIESYARRFGYGVVRDFIGH 233
Cdd:TIGR00495 171 AINKVAHSYGCTPVEGMLSH 190
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
64-267 |
4.29e-05 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 44.71 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 64 GNASDVYDAEgigrIREAGRIAA---QAMEHTAE-H----------IRPGIT----TDELDRIAHEFIVAAGAypSClGY 125
Cdd:PTZ00053 137 ENSSRTSSEE----KRELEKLSEeqyQDLRRAAEvHrqvrryaqsvIKPGVKlidiCERIESKSRELIEADGL--KC-GW 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 126 rGFPRSiCtSVNEVICHGIP---DGTVLEDGDIVNLDItaykdGVHGDhnrTYLVgD------VDEESRLLVERTEEALR 196
Cdd:PTZ00053 210 -AFPTG-C-SLNHCAAHYTPntgDKTVLTYDDVCKLDF-----GTHVN---GRII-DcaftvaFNPKYDPLLQATKDATN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 197 RGIKAVKPGREINVIGRAI----ESYARRFG---YGV--VRDFIGHGVG-VDFHSGLVIPhyDAAPAHNRLMVPGMVFTI 266
Cdd:PTZ00053 278 TGIKEAGIDVRLSDIGAAIqeviESYEVEIKgktYPIksIRNLNGHSIGpYIIHGGKSVP--IVKGGENTRMEEGELFAI 355
|
.
gi 2197366932 267 E 267
Cdd:PTZ00053 356 E 356
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
75-297 |
6.76e-04 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 41.15 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELdriAHEFIVAAGAYPSClgyrGFPRSICTSVNEVICHGI-PDGTVLEDG 153
Cdd:PRK14576 183 IEHLRKSAEITEYGIASAAKKIRVGCTAAEL---TAAFKAAVMSFPET----NFSRFNLISVGDNFSPKIiADTTPAKVG 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 154 DIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREINVIGRAIESYARRFGY-GVVRDFIG 232
Cdd:PRK14576 256 DLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSGLpHYNRGHLG 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2197366932 233 HGVGVDFhsGLVIPHYDAAPAhNRLMVPGMVFTIEPM---ITLGGIDWEQW----DDGWTVVTKDRRRTAQF 297
Cdd:PRK14576 336 HGDGVFL--GLEEVPFVSTQA-TETFCPGMVLSLETPyygIGVGSIMLEDMilitDSGFEFLSKLDRDLRRY 404
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
75-237 |
7.87e-04 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 40.47 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELdriahefivaAGAYPSCLGYRG---FPRSICTSVNEVICHG-IPDGTVL 150
Cdd:PRK15173 101 IKRLRKSAEITEYGITEASKLIRVGCTSAEL----------TAAYKAAVMSKSethFSRFHLISVGADFSPKlIPSNTKA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 151 EDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREI-NVIGRAIESYARRFGYGVVRD 229
Cdd:PRK15173 171 CSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMkDVFDSTMEVIKKSGLPNYNRG 250
|
....*...
gi 2197366932 230 FIGHGVGV 237
Cdd:PRK15173 251 HLGHGNGV 258
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
75-237 |
1.21e-03 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 40.07 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 75 IGRIREAGRIAAQAMEHTAEHIRPGITTDELdriahefivaAGAYPSCLGYRG---FPRSICTSVNEVICHG-IPDGTVL 150
Cdd:PRK14575 184 IKRLRKSAEITEYGITEASKLIRVGCTSAEL----------TAAYKAAVMSKSethFSRFHLISVGADFSPKlIPSNTKA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197366932 151 EDGDIVNLDITAYKDGVHGDHNRTYLVGDVDEESRLLVERTEEALRRGIKAVKPGREI-NVIGRAIESYARRFGYGVVRD 229
Cdd:PRK14575 254 CSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMkDVFDSTMEVIKKSGLPNYNRG 333
|
....*...
gi 2197366932 230 FIGHGVGV 237
Cdd:PRK14575 334 HLGHGNGV 341
|
|
| |
