|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
10-369 |
1.21e-177 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 499.36 E-value: 1.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 10 CGKDATLQCPTCLKLGI--KGSFFCSQPCFKGFWKEHKAIHALAAGASNSAEQDGAYNPW--------------PHFRFT 73
Cdd:PLN03158 15 CSKPAHLQCPKCLELKLprEGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAPAEGWlyclkkgqartsklPDFDWT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 74 GKLRPFPQTPKRTVPNAIQRPDYADHpaGRSLSEEALRGTKI-KVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDE 152
Cdd:PLN03158 95 GPLRPYPISPRRVVPDHIPKPDWALD--GTPKIEPNSDLQHSvEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 153 LDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKH 232
Cdd:PLN03158 173 IDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 233 KKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFT 312
Cdd:PLN03158 253 RQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFT 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355531 313 IEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTKRRENNGQ--PW 369
Cdd:PLN03158 333 IEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDvfPW 391
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
123-360 |
1.68e-145 |
|
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: 411.50 E-value: 1.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHG 282
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355531 283 IHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
115-363 |
1.49e-133 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 381.66 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
....*....
gi 21355531 355 CEILTKRRE 363
Cdd:COG0024 241 PEILTLPDG 249
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
115-361 |
6.66e-110 |
|
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: 321.60 E-value: 6.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 21355531 355 CEILTKR 361
Cdd:TIGR00500 241 PEILTER 247
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
124-352 |
9.28e-57 |
|
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: 184.37 E-value: 9.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 124 EGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYpsplNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDL 203
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 204 CNIDVTV-YHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS-VVRSYCGH 281
Cdd:pfam00557 77 VLIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355531 282 GIHRVFHTAPNVPHYAKNsavGVMAPGHCFTIEPMIsvgvqkaetwpddwtaVTADGLYSAQFEQTLLVNE 352
Cdd:pfam00557 157 GIGLEVHEGPYISRGGDD---RVLEPGMVFTIEPGI----------------YFIPGWGGVRIEDTVLVTE 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
10-369 |
1.21e-177 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 499.36 E-value: 1.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 10 CGKDATLQCPTCLKLGI--KGSFFCSQPCFKGFWKEHKAIHALAAGASNSAEQDGAYNPW--------------PHFRFT 73
Cdd:PLN03158 15 CSKPAHLQCPKCLELKLprEGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAPAEGWlyclkkgqartsklPDFDWT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 74 GKLRPFPQTPKRTVPNAIQRPDYADHpaGRSLSEEALRGTKI-KVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDE 152
Cdd:PLN03158 95 GPLRPYPISPRRVVPDHIPKPDWALD--GTPKIEPNSDLQHSvEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 153 LDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKH 232
Cdd:PLN03158 173 IDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 233 KKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFT 312
Cdd:PLN03158 253 RQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFT 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355531 313 IEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTKRRENNGQ--PW 369
Cdd:PLN03158 333 IEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDvfPW 391
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
123-360 |
1.68e-145 |
|
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: 411.50 E-value: 1.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHG 282
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355531 283 IHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
115-363 |
1.49e-133 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 381.66 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
....*....
gi 21355531 355 CEILTKRRE 363
Cdd:COG0024 241 PEILTLPDG 249
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
115-364 |
1.34e-130 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 374.09 E-value: 1.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:PRK05716 3 ITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:PRK05716 83 DKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:PRK05716 163 VREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDG 242
|
250
....*....|
gi 21355531 355 CEILTKRREN 364
Cdd:PRK05716 243 PEILTLRPEE 252
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
115-361 |
6.66e-110 |
|
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: 321.60 E-value: 6.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 21355531 355 CEILTKR 361
Cdd:TIGR00500 241 PEILTER 247
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
109-361 |
1.34e-107 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 316.01 E-value: 1.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 109 ALRGTKIKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVI 188
Cdd:PRK12896 2 AQEGRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 189 CHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVA 268
Cdd:PRK12896 82 AHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 269 PHGFSVVRSYCGHGIHRVFHTAPNV-PHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQT 347
Cdd:PRK12896 162 KNGYSVVRDLTGHGVGRSLHEEPSViLTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHT 241
|
250
....*....|....
gi 21355531 348 LLVNETGCEILTKR 361
Cdd:PRK12896 242 VVVTRDGPEILTDR 255
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
104-359 |
3.16e-80 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 247.42 E-value: 3.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 104 SLSEEALRGTKIKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYN--FPKSCC 181
Cdd:PRK12318 30 NLKQLYASQYDIIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTIC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 182 TSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGN 261
Cdd:PRK12318 110 TSLNEVICHGIPNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 262 VIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYaKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDD-WTAVTADGLY 340
Cdd:PRK12318 190 VIENCADKYGFSVVDQFVGHGVGIKFHENPYVPHH-RNSSKIPLAPGMIFTIEPMINVGKKEGVIDPINhWEARTCDNQP 268
|
250
....*....|....*....
gi 21355531 341 SAQFEQTLLVNETGCEILT 359
Cdd:PRK12318 269 SAQWEHTILITETGYEILT 287
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
124-352 |
9.28e-57 |
|
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: 184.37 E-value: 9.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 124 EGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYpsplNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDL 203
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 204 CNIDVTV-YHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS-VVRSYCGH 281
Cdd:pfam00557 77 VLIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355531 282 GIHRVFHTAPNVPHYAKNsavGVMAPGHCFTIEPMIsvgvqkaetwpddwtaVTADGLYSAQFEQTLLVNE 352
Cdd:pfam00557 157 GIGLEVHEGPYISRGGDD---RVLEPGMVFTIEPGI----------------YFIPGWGGVRIEDTVLVTE 208
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
115-360 |
1.19e-52 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 175.22 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVhEAAIERECYPSPLNYYN-FPKSCCTSVNEVICHGIP 193
Cdd:PRK12897 2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFV-EAYLEKHGATSEQKGYNgYPYAICASVNDEMCHAFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 194 DQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS 273
Cdd:PRK12897 81 ADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 274 VVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNET 353
Cdd:PRK12897 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKD 240
|
....*..
gi 21355531 354 GCEILTK 360
Cdd:PRK12897 241 GPIILTK 247
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
123-355 |
1.76e-45 |
|
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: 154.92 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPlnyynfpkSCCTSVNEV--ICHGIPDQRPLQD 200
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVR-SYC 279
Cdd:cd01066 73 GDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgHRT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355531 280 GHGIHRVFHTAPNVPHYAKnsavGVMAPGHCFTIEPMISVgvqkaetwpddwtavtaDGLYSAQFEQTLLVNETGC 355
Cdd:cd01066 153 GHGIGLEIHEPPVLKAGDD----TVLEPGMVFAVEPGLYL-----------------PGGGGVRIEDTVLVTEDGP 207
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
117-360 |
4.32e-37 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 135.72 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 117 VLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECypsplNYYNFPKSCCTSVNEVICHGIPDQR 196
Cdd:COG0006 73 IKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGA-----EGPSFDTIVASGENAAIPHYTPTDR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 197 PLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFsvvR 276
Cdd:COG0006 148 PLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGY---G 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 277 SY----CGHGIHRVFHTapnVPHYAKNSAVgVMAPGHCFTIEPMISVgvqkaetwpddwtavtaDGLYSAQFEQTLLVNE 352
Cdd:COG0006 225 EYfphgTGHGVGLDVHE---GPQISPGNDR-PLEPGMVFTIEPGIYI-----------------PGIGGVRIEDTVLVTE 283
|
....*...
gi 21355531 353 TGCEILTK 360
Cdd:COG0006 284 DGAEVLTR 291
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
172-363 |
7.30e-30 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 116.10 E-value: 7.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 172 NYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTV------------------------YHRGFHGDLNET---FF 224
Cdd:PRK07281 63 AMMDYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMVLsepldksivdvsklnfdnveqmkkYTESYRGGLADScwaYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 225 VGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGV 304
Cdd:PRK07281 143 VGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLR 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355531 305 MAPGHCFTIEPMISVGvqkaeTWPDD------WTAVTADGLYSAQFEQTLLVNETGCEILTKRRE 363
Cdd:PRK07281 223 LREGMVLTIEPMINTG-----TWEIDtdmktgWAHKTLDGGLSCQYEHQFVITKDGPVILTSQGE 282
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
123-360 |
5.47e-28 |
|
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: 111.19 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSplnyynFPKSCctSVNEVICHGIP---DQRPLQ 199
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPA------FPVNL--SINECAAHYTPnagDDTVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 200 DGDLCNIDVTVYHRGFHGDlneTFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYC 279
Cdd:cd01088 73 EGDVVKLDFGAHVDGYIAD---SAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 280 GHGIHR-VFHTAPNVPHYaKNSAVGVMAPGHCFTIEPMISVGVQK----------------------------------- 323
Cdd:cd01088 150 GHSIERyRLHAGKSIPNV-KGGEGTRLEEGDVYAIEPFATTGKGYvhdgpecsiymlnrdkplrlprarklldviyenfg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355531 324 ----AETWPDDWTA----------------------VTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01088 229 tlpfARRWLDRLGEtkllmalknlckagivypypvlKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| zf-C6H2 |
pfam15801 |
zf-MYND-like zinc finger, mRNA-binding; zf-C6H2 is an unusual zinc-finger similar to zf-MYND, ... |
5-48 |
3.73e-25 |
|
zf-MYND-like zinc finger, mRNA-binding; zf-C6H2 is an unusual zinc-finger similar to zf-MYND, pfam01753.This zinc-finger is found at the N-terminus of Pfam families Exo_endo_phos pfam03372 and Peptidase_M24 pfam00557. The domain is missing in prokaryotic methionine aminopeptidases, and is a unique type of zinc-finger domain. It consists of a C2-C2 zinc-finger motif similar to the RING finger family followed by a C2H2 motif similar to zinc-fingers involved in RNA-binding. In yeast the domain chelates zinc in a 2:1 ratio. The domain is found in yeast, plants and mammals. The domain is necessary for the association of the methionine aminopeptidase with the ribosome and the normal processing of the peptidase.
Pssm-ID: 464880 [Multi-domain] Cd Length: 46 Bit Score: 96.15 E-value: 3.73e-25
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 21355531 5 CETTNCGKDA-TLQCPTCLKLGIKGSFFCSQPCFKGFWKEHKAIH 48
Cdd:pfam15801 1 CAGPGCGKEAsSLQCPTCLKLGIKGSFFCSQDCFKKNWKSHKAIH 45
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
123-317 |
1.02e-24 |
|
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: 99.89 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGIT----TDELDRLVHEAAIERecyPSplnyynFPKSCCTSVNEVICHGIPDQRPL 198
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTerevAAELEYFMRKLGAEG---PS------FDTIVASGPNSALPHGVPSDRKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 199 QDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSvvrSY 278
Cdd:cd01092 72 EEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYG---EY 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21355531 279 ----CGHGIHRVFHTAPNVPHYAKnsavGVMAPGHCFTIEPMI 317
Cdd:cd01092 149 fihrTGHGVGLEVHEAPYISPGSD----DVLEEGMVFTIEPGI 187
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
123-360 |
3.27e-11 |
|
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: 62.59 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSplnyYNFPksCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARLA----YSYI--VAAGSNAAILHYVHNDQPLKDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFV-GNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDI----GNVIQKYVAPHGF----- 272
Cdd:cd01087 75 LVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGIlkgdv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 273 ------SVVRSYCGHGI-HRVFHTAPNVPHYAK-NSAVGVMAPGHCFTIEPMISVgvqkaetwPDDWTAVTADglysAQF 344
Cdd:cd01087 155 deivesGAYAKFFPHGLgHYLGLDVHDVGGYLRyLRRARPLEPGMVITIEPGIYF--------IPDLLDVPEY----FRG 222
|
250 260
....*....|....*....|.
gi 21355531 345 -----EQTLLVNETGCEILTK 360
Cdd:cd01087 223 ggiriEDDVLVTEDGPENLTR 243
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
176-285 |
1.41e-08 |
|
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: 56.05 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 176 FPKscCTSVNEVICHGIP----DQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSE-----KHKKLVQVTHEALSKA 246
Cdd:TIGR00495 78 FPT--CISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvtgRKADVIAAAHLAAEAA 155
|
90 100 110
....*....|....*....|....*....|....*....
gi 21355531 247 IEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHR 285
Cdd:TIGR00495 156 LRLVKPGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQ 194
|
|
| PLN03144 |
PLN03144 |
Carbon catabolite repressor protein 4 homolog; Provisional |
11-107 |
4.04e-08 |
|
Carbon catabolite repressor protein 4 homolog; Provisional
Pssm-ID: 178689 [Multi-domain] Cd Length: 606 Bit Score: 55.12 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 11 GKDATLQCPTCLKLGIKG--SFFCSQPCFKGFWKEHKAIHALAA--GASNSAEQD------GAYNPWPHFRFTGKLRPFP 80
Cdd:PLN03144 70 SEPATLQCVGCVKAKLPVskSYHCSPKCFSDAWRHHRVLHERAAsaVRENGNEEDelfgrfNSSGSGVLSTSDSGSASSA 149
|
90 100
....*....|....*....|....*..
gi 21355531 81 QTPKRTVPNAIQRPDYADHPAGRSLSE 107
Cdd:PLN03144 150 SLTNGSVPLYPSGIEQKTQVGGETWIE 176
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
120-359 |
8.76e-08 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 53.57 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 120 DEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELD-RLVHEAAIERECYPSplnyYNfpksccTSV----NEVICHGIPD 194
Cdd:PRK10879 176 PEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEgEIHHEFNRHGARYPS----YN------TIVgsgeNGCILHYTEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFV-GNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDI-GNVIQKYVAP--- 269
Cdd:PRK10879 246 ESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVtGEVVRIMVSGlvk 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 270 ----HG-------FSVVRSYCGHGI-HRVFHTAPNVPHYAKNSAvGVMAPGHCFTIEPMISVGvqkaetwPDDWTAVTAD 337
Cdd:PRK10879 326 lgilKGdvdqliaENAHRPFFMHGLsHWLGLDVHDVGVYGQDRS-RILEPGMVLTVEPGLYIA-------PDADVPEQYR 397
|
250 260
....*....|....*....|..
gi 21355531 338 GLySAQFEQTLLVNETGCEILT 359
Cdd:PRK10879 398 GI-GIRIEDDIVITETGNENLT 418
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
122-360 |
2.69e-07 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 51.94 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIErecYPSPlnyyNFPKSCCTSVNEVICHGI-PDQRPLQD 200
Cdd:PRK14576 182 EIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMS---FPET----NFSRFNLISVGDNFSPKIiADTTPAKV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGN----VIQKYVAPHgfsVVR 276
Cdd:PRK14576 255 GDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDstmaVIKTSGLPH---YNR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 277 SYCGHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIE-PMISVGVQkaetwpddwtavtadglySAQFEQTLLVNETGC 355
Cdd:PRK14576 332 GHLGHG-DGVFLGLEEVP-FVSTQATETFCPGMVLSLEtPYYGIGVG------------------SIMLEDMILITDSGF 391
|
....*
gi 21355531 356 EILTK 360
Cdd:PRK14576 392 EFLSK 396
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
127-294 |
5.91e-07 |
|
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: 50.02 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 127 RVAGRLGRECLDEGAKAVEVGITTDEL----DRLVHEAAieRECYPSPLNYYN---FPKscCTSVNEVICHGIP----DQ 195
Cdd:cd01089 5 KTAGQIANKVLKQVISLCVPGAKVVDLcekgDKLILEEL--GKVYKKEKKLEKgiaFPT--CISVNNCVCHFSPlksdAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 196 RPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSE-----KHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPH 270
Cdd:cd01089 81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAEtpvtgKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
|
170 180
....*....|....*....|....
gi 21355531 271 GFSVVRSYCGHGIHRVFHTAPNVP 294
Cdd:cd01089 161 GCTPVEGVLSHQLKRVVSSGEGKA 184
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
122-360 |
9.25e-07 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 50.10 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERecypsplNYYNFPKSCCTSVNEVICHG-IPDQRPLQD 200
Cdd:PRK15173 100 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK-------SETHFSRFHLISVGADFSPKlIPSNTKACS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF-SVVRSYC 279
Cdd:PRK15173 173 GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLpNYNRGHL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 280 GHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIEpmisvgvqkaetwpddwTAVTADGLYSAQFEQTLLVNETGCEILT 359
Cdd:PRK15173 253 GHG-NGVFLGLEESP-FVSTHATESFTSGMVLSLE-----------------TPYYGYNLGSIMIEDMILINKEGIEFLS 313
|
.
gi 21355531 360 K 360
Cdd:PRK15173 314 K 314
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
122-360 |
1.67e-06 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 49.70 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERecypsplNYYNFPKSCCTSVNEVICHG-IPDQRPLQD 200
Cdd:PRK14575 183 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK-------SETHFSRFHLISVGADFSPKlIPSNTKACS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF-SVVRSYC 279
Cdd:PRK14575 256 GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLpNYNRGHL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 280 GHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIEpmisvgvqkaetwpddwTAVTADGLYSAQFEQTLLVNETGCEILT 359
Cdd:PRK14575 336 GHG-NGVFLGLEESP-FVSTHATESFTSGMVLSLE-----------------TPYYGYNLGSIMIEDMILINKEGIEFLS 396
|
.
gi 21355531 360 K 360
Cdd:PRK14575 397 K 397
|
|
| Creatinase |
cd01090 |
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea. |
124-320 |
9.24e-06 |
|
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
Pssm-ID: 238523 [Multi-domain] Cd Length: 228 Bit Score: 46.38 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 124 EGMRVA---GRLGRECLDEGAKAVEVGITTDEldrlvheaAIERECYPSplnyynFPKSCC--------TSVNEVICHGI 192
Cdd:cd01090 6 HGARIAdigGAAVVEAIREGVPEYEVALAGTQ--------AMVREIAKT------FPEVELmdtwtwfqSGINTDGAHNP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 193 PDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF 272
Cdd:cd01090 72 VTNRKVQRGDILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21355531 273 SVVRSYcGHGihrvfHTAPNVPHYAKNSA--------VGVMAPGHCFTIEPMISVG 320
Cdd:cd01090 152 LRYRTF-GYG-----HSFGVLSHYYGREAglelrediDTVLEPGMVVSMEPMIMLP 201
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
104-358 |
1.17e-04 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 43.77 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 104 SLSEEALRGTKIKvlddEEIEGMRVAGRLGreclDEGAKAVEVGITTDELDRlvhEAAIERECY--PSPLNYYNFPKSCC 181
Cdd:PRK09795 118 SATPDVLRQIKTP----EEVEKIRLACGIA----DRGAEHIRRFIQAGMSER---EIAAELEWFmrQQGAEKASFDTIVA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 182 TSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFV---GNVSEKHK--KLVQVTHEALSKAIEFVRPGEKY 256
Cdd:PRK09795 187 SGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHPlfNVYQIVLQAQLAAISAIRPGVRC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 257 RDIGNVIQKYVAPHGFSVVRSY-CGHGIHRVFHTAPNVphyaKNSAVGVMAPGHCFTIEPMISVGVQKAetwpddwtavt 335
Cdd:PRK09795 267 QQVDDAARRVITEAGYGDYFGHnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGIYLPGQGG----------- 331
|
250 260
....*....|....*....|...
gi 21355531 336 adglysAQFEQTLLVNETGCEIL 358
Cdd:PRK09795 332 ------VRIEDVVLVTPQGAEVL 348
|
|
|