|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
23-379 |
2.04e-166 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 471.24 E-value: 2.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 23 SGLQCGR-ETSSQMKCPVCLKQGI---VSIFCDTSCYENNYKAHKALHNAKDGLEGAY--------------------DP 78
Cdd:PLN03158 8 SPLACARcSKPAHLQCPKCLELKLpreGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQnsdapaegwlyclkkgqartSK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 79 FPKFKYSGKVKAsYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRP 158
Cdd:PLN03158 88 LPDFDWTGPLRP-YPISPRRVVPDHIPKPDWALDGTPKIEPNSDLQHSVEIKTPEQIQRMRETCRIAREVLDAAARAIKP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 159 GITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVG 238
Cdd:PLN03158 167 GVTTDEIDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 239 eNISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVM 318
Cdd:PLN03158 247 -NVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVM 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323273 319 KPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSP 379
Cdd:PLN03158 326 KAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSP 386
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
127-374 |
1.50e-148 |
|
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: 420.22 E-value: 1.50e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 127 IPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPD 206
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 207 KTVLKEGDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCS 286
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGK-ISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 287 VVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEH 366
Cdd:TIGR00500 160 VVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDN 239
|
....*...
gi 6323273 367 GVEILTAR 374
Cdd:TIGR00500 240 GPEILTER 247
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
135-372 |
3.08e-142 |
|
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: 403.80 E-value: 3.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGD 214
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 215 IVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGH 294
Cdd:cd01086 81 IVNIDVGVELDGYHGDSARTFIVGE-VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGH 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323273 295 GVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILT 372
Cdd:cd01086 160 GIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILT 237
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
127-376 |
6.61e-132 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 377.81 E-value: 6.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 127 IPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPD 206
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 207 KTVLKEGDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCS 286
Cdd:COG0024 81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGE-VSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 287 VVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEH 366
Cdd:COG0024 160 VVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTED 239
|
250
....*....|
gi 6323273 367 GVEILTARNK 376
Cdd:COG0024 240 GPEILTLPDG 249
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
127-377 |
2.37e-129 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 371.39 E-value: 2.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 127 IPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPD 206
Cdd:PRK05716 3 ITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 207 KTVLKEGDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCS 286
Cdd:PRK05716 83 DKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGE-ISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 287 VVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEH 366
Cdd:PRK05716 162 VVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTED 241
|
250
....*....|.
gi 6323273 367 GVEILTARNKK 377
Cdd:PRK05716 242 GPEILTLRPEE 252
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
133-374 |
9.71e-96 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 286.35 E-value: 9.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 133 DQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKE 212
Cdd:PRK12896 14 RELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHGIPGPRVIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 213 GDIVNLDVSLYYQGYHADLNETYYVGeNISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYC 292
Cdd:PRK12896 94 GDLVNIDVSAYLDGYHGDTGITFAVG-PVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 293 GHGVGEFFHCSPN-IPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEIL 371
Cdd:PRK12896 173 GHGVGRSLHEEPSvILTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEIL 252
|
...
gi 6323273 372 TAR 374
Cdd:PRK12896 253 TDR 255
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
126-376 |
4.99e-78 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 242.42 E-value: 4.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 126 NIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYN--FPKSLCTSVNEVICHG 203
Cdd:PRK12318 40 DIIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 204 VPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATEN 283
Cdd:PRK12318 120 IPNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGE-VSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 284 KCSVVRTYCGHGVGEFFHCSPNIPHYaKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDD-WTSTTQDGKLSAQFEHTLL 362
Cdd:PRK12318 199 GFSVVDQFVGHGVGIKFHENPYVPHH-RNSSKIPLAPGMIFTIEPMINVGKKEGVIDPINhWEARTCDNQPSAQWEHTIL 277
|
250
....*....|....
gi 6323273 363 VTEHGVEILTARNK 376
Cdd:PRK12318 278 ITETGYEILTLLDK 291
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
136-365 |
6.10e-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: 195.54 E-value: 6.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 136 KKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYpsplNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDI 215
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 216 VNLDVSLYYQ-GYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENK-CSVVRTYCG 293
Cdd:pfam00557 77 VLIDVGAEYDgGYCSDITRTFVVGK-PSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGlGEYFPHGLG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323273 294 HGVGEFFHCSPNIPHyakNRTPGVMKPGMVFTIEPMINEgtwkdmtwpddwtsttQDGKLSAQFEHTLLVTE 365
Cdd:pfam00557 156 HGIGLEVHEGPYISR---GGDDRVLEPGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVTE 208
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
127-372 |
7.63e-44 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 152.50 E-value: 7.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 127 IPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPD 206
Cdd:PRK12897 2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 207 KTVLKEGDIVNLDVSLYYQGYHADLNETYYVGeNISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCS 286
Cdd:PRK12897 82 DVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVG-KVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 287 VVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEH 366
Cdd:PRK12897 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKD 240
|
....*.
gi 6323273 367 GVEILT 372
Cdd:PRK12897 241 GPIILT 246
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
135-367 |
8.08e-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: 140.67 E-value: 8.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNyynfpkslCTSVNEV--ICHGVPDKTVLKE 212
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAGPT--------IVGSGARtaLPHYRPDDRRLQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 213 GDIVNLDVSLYYQGYHADLNETYYVGENiSKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRT-Y 291
Cdd:cd01066 73 GDLVLVDLGGVYDGYHADLTRTFVIGEP-SDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFGhR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323273 292 CGHGVGEFFHCSPniphYAKNRTPGVMKPGMVFTIEPMINEgtwkdmtwpddwtsttqDGKLSAQFEHTLLVTEHG 367
Cdd:cd01066 152 TGHGIGLEIHEPP----VLKAGDDTVLEPGMVFAVEPGLYL-----------------PGGGGVRIEDTVLVTEDG 206
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
156-374 |
1.11e-36 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 134.59 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 156 VRPGITTDELDEIVHNETIKRGAYPSPL----NYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSL--------- 222
Cdd:PRK07281 31 IKPGVDMWEVEEYVRRRCKEENVLPLQIgvdgAMMDYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMVLsepldksiv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 223 ------------------YYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENK 284
Cdd:PRK07281 111 dvsklnfdnveqmkkyteSYRGGLADSCWAYAVGT-PSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 285 CSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWK-DMTWPDDWTSTTQDGKLSAQFEHTLLV 363
Cdd:PRK07281 190 YGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLREGMVLTIEPMINTGTWEiDTDMKTGWAHKTLDGGLSCQYEHQFVI 269
|
250
....*....|.
gi 6323273 364 TEHGVEILTAR 374
Cdd:PRK07281 270 TKDGPVILTSQ 280
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
133-373 |
1.70e-33 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 126.47 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 133 DQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAypsplNYYNFPKSLCTSVNEVICHGVPDKTVLKE 212
Cdd:COG0006 77 EEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGA-----EGPSFDTIVASGENAAIPHYTPTDRPLKP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 213 GDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKcsvVRTY- 291
Cdd:COG0006 152 GDLVLIDAGAEYDGYTSDITRTVAVGE-PSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAG---YGEYf 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 292 ---CGHGVGEFFHCSPNIphYAKNRTPgvMKPGMVFTIEPMInegtwkdmtwpddwtstTQDGKLSAQFEHTLLVTEHGV 368
Cdd:COG0006 228 phgTGHGVGLDVHEGPQI--SPGNDRP--LEPGMVFTIEPGI-----------------YIPGIGGVRIEDTVLVTEDGA 286
|
....*
gi 6323273 369 EILTA 373
Cdd:COG0006 287 EVLTR 291
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
135-330 |
6.84e-30 |
|
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: 114.14 E-value: 6.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAY-PSplnyynFPKSLCTSVNEVICHGVPDKTVLKEG 213
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 214 DIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELgDH-----IEK--------HA 280
Cdd:cd01092 75 DLVLIDFGAIYDGYCSDITRTVAVGE-PSDELKEIYEIVLEAQQAAIKAVKPGVTAKEV-DKaardvIEEagygeyfiHR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6323273 281 TenkcsvvrtycGHGVGEFFHCSPNIPHYAKnrtpGVMKPGMVFTIEPMI 330
Cdd:cd01092 153 T-----------GHGVGLEVHEAPYISPGSD----DVLEEGMVFTIEPGI 187
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
135-373 |
7.80e-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: 110.80 E-value: 7.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSplnyynFPKSLctSVNEVICHGVP---DKTVLK 211
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPA------FPVNL--SINECAAHYTPnagDDTVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 212 EGDIVNLDVSLYYQGYHADLNETYYVGENI------SKEALNTtetsreclklAIKMCKPGTTFQELGDHIEKHATENKC 285
Cdd:cd01088 73 EGDVVKLDFGAHVDGYIADSAFTVDFDPKYddlleaAKEALNA----------AIKEAGPDVRLGEIGEAIEEVIESYGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 286 SVVRTYCGHGVGEF-FHCSPNIPHYaKNRTPGVMKPGMVFTIEP-------MINEGTW-------KDMT----------- 339
Cdd:cd01088 143 KPIRNLTGHSIERYrLHAGKSIPNV-KGGEGTRLEEGDVYAIEPfattgkgYVHDGPEcsiymlnRDKPlrlprarklld 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 340 --------------WPDDWTSTT----------------------QDGKLSAQFEHTLLVTEHGVEILTA 373
Cdd:cd01088 222 viyenfgtlpfarrWLDRLGETKllmalknlckagivypypvlkeISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
135-372 |
4.41e-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: 103.33 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSplnyynFPKSLctSVNEVICHGVP---DKTVLK 211
Cdd:TIGR00501 5 AEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEPA------FPCNI--SINECAAHFTPkagDKTVFK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 212 EGDIVNLDVSLYYQGYHADLNETYYVGENISkealNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTY 291
Cdd:TIGR00501 77 DGDVVKLDLGAHVDGYIADTAITVDLGDQYD----NLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 292 CGHGVGEF-FHCSPNIPHYaKNRTPGVMKPGMVFTIEPMINEG-----------------------------------TW 335
Cdd:TIGR00501 153 TGHSMAPYrLHGGKSIPNV-KERDTTKLEEGDVVAIEPFATDGvgyvtdggevsiyaflaerpvrldsarnllktideNY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323273 336 KDMTWPDDWTSTTQD--------------------------GKLSAQFEHTLLVTEHGVEILT 372
Cdd:TIGR00501 232 GTLPFARRWLDKLGDekylfalnnlirhgliydypvlneisGGYVAQWEHTILVEEHGKEVTT 294
|
|
| zf-C6H2 |
pfam15801 |
zf-MYND-like zinc finger, mRNA-binding; zf-C6H2 is an unusual zinc-finger similar to zf-MYND, ... |
22-66 |
9.49e-17 |
|
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: 73.42 E-value: 9.49e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6323273 22 CSGLQCGRETSSqMKCPVCLKQGI-VSIFCDTSCYENNYKAHKALH 66
Cdd:pfam15801 1 CAGPGCGKEASS-LQCPTCLKLGIkGSFFCSQDCFKKNWKSHKAIH 45
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
135-373 |
1.72e-13 |
|
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: 69.52 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSplnyYNFPkSLCTSvNEVICHGVPDKTVLKEGD 214
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARLA----YSYI-VAAGS-NAAILHYVHNDQPLKDGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 215 IVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATEN----------- 283
Cdd:cd01087 75 LVLIDAGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGlkelgilkgdv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 284 ----KCSVVRTYCGHGVGEFF----HCSPNIPHYakNRTPGVMKPGMVFTIEP---MINEGTWKDMTWP-------DDwt 345
Cdd:cd01087 155 deivESGAYAKFFPHGLGHYLgldvHDVGGYLRY--LRRARPLEPGMVITIEPgiyFIPDLLDVPEYFRgggirieDD-- 230
|
250 260
....*....|....*....|....*...
gi 6323273 346 sttqdgklsaqfehtLLVTEHGVEILTA 373
Cdd:cd01087 231 ---------------VLVTEDGPENLTR 243
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
146-379 |
1.37e-12 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 68.60 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 146 REVLDIAA-AHVR------PGITTDELDEIVHNETIKRGA-YPSplnyYNfpkslcTSV----NEVICHGVPDKTVLKEG 213
Cdd:PRK10879 183 RRAGEISAlAHTRamekcrPGMFEYQLEGEIHHEFNRHGArYPS----YN------TIVgsgeNGCILHYTENESEMRDG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 214 DIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDH------------------ 275
Cdd:PRK10879 253 DLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEvvrimvsglvklgilkgd 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 276 IEKHATENKcsvVRTYCGHGVGEFF----HcspNIPHYAKNRTPgVMKPGMVFTIEPMINEGTWKDMtwPDDWTSttqdg 351
Cdd:PRK10879 333 VDQLIAENA---HRPFFMHGLSHWLgldvH---DVGVYGQDRSR-ILEPGMVLTVEPGLYIAPDADV--PEQYRG----- 398
|
250 260
....*....|....*....|....*...
gi 6323273 352 kLSAQFEHTLLVTEHGVEILTARNKKSP 379
Cdd:PRK10879 399 -IGIRIEDDIVITETGNENLTASVVKKP 425
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
137-373 |
1.73e-12 |
|
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: 66.20 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 137 KIRKACMLGREVLDIAAAHVRPGITTDEL----DEIVHNET---------IKRG-AYPSplnyynfpkslCTSVNEVICH 202
Cdd:cd01089 3 KYKTAGQIANKVLKQVISLCVPGAKVVDLcekgDKLILEELgkvykkekkLEKGiAFPT-----------CISVNNCVCH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 203 GVPDK----TVLKEGDIVNLDVSLYYQGYHADLNETYYVGE----NISKEALNTTETSRECLKLAIKMCKPGTTFQELGD 274
Cdd:cd01089 72 FSPLKsdatYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAeaetPVTGKKADVIAAAHYALEAALRLLRPGNQNSDITE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 275 HIEKHATENKCSVVRTYCGHGVGEFFHCSPNiphyaKNRTPGVMKPGMVFTIEPMInegtwkdmtwpddwtstTQDGKLS 354
Cdd:cd01089 152 AIQKVIVDYGCTPVEGVLSHQLKRVVSSGEG-----KAKLVECVKHGLLFPYPVLY-----------------EKEGEVV 209
|
250
....*....|....*....
gi 6323273 355 AQFEHTLLVTEHGVEILTA 373
Cdd:cd01089 210 AQFKLTVLLTPNGVTVLTG 228
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
135-294 |
4.91e-10 |
|
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: 60.67 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 135 IKKIRKACMLGREVLDIAaahvrpgittDELDEIVHNETIKrgAYPSPLNYYN---FPKslCTSVNEVICHGVPDKT--- 208
Cdd:TIGR00495 34 LKSVVEACSPGAKVVDIC----------EKGDAFIMEETAK--IFKKEKEMEKgiaFPT--CISVNNCVGHFSPLKSdqd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 209 -VLKEGDIVNLDVSLYYQGYHADLNETYYVG----ENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATEN 283
Cdd:TIGR00495 100 yILKEGDVVKIDLGCHIDGFIALVAHTFVVGvaqeEPVTGRKADVIAAAHLAAEAALRLVKPGNTNTQVTEAINKVAHSY 179
|
170
....*....|.
gi 6323273 284 KCSVVRTYCGH 294
Cdd:TIGR00495 180 GCTPVEGMLSH 190
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
129-376 |
5.36e-09 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 57.25 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 129 IYKKDQIKKIRKACmlgrEVLDIAAAHVR----PGITTDELDEIVHNETIKRGAYPSplnyyNFPKSLCTSVNEVICHGV 204
Cdd:PRK09795 127 IKTPEEVEKIRLAC----GIADRGAEHIRrfiqAGMSEREIAAELEWFMRQQGAEKA-----SFDTIVASGWRGALPHGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 205 PDKTVLKEGDIVNLDVSLYYQGYHADLNETYYV-GENISKEA---LNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHA 280
Cdd:PRK09795 198 ASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVnGEGVSAEShplFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 281 TENKCSVVRTY-CGHGVGEFFHCSPNIphyaKNRTPGVMKPGMVFTIEPMInegtwkdmtwpddwtstTQDGKLSAQFEH 359
Cdd:PRK09795 278 TEAGYGDYFGHnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGI-----------------YLPGQGGVRIED 336
|
250
....*....|....*..
gi 6323273 360 TLLVTEHGVEILTARNK 376
Cdd:PRK09795 337 VVLVTPQGAEVLYAMPK 353
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
60-327 |
9.07e-07 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 50.48 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 60 KAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLT----PRRYVPEDIPKPdwaangLPVSEQRNDR---LNNIPIYKK 132
Cdd:PTZ00053 63 KKKKKKKNLGEAYDLAYDLPVVWSSAAFQDNSHIRKlgnwPEQEWKQTQPPT------IPVSKQFKDGeypVGEIQEYPG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 133 D-------------------QIKKIRKACMLGREVLDIAAAHVRPGIT----TDELD----EIVHNETIKRGaypsplny 185
Cdd:PTZ00053 137 EnssrtsseekreleklseeQYQDLRRAAEVHRQVRRYAQSVIKPGVKlidiCERIEsksrELIEADGLKCG-------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 186 YNFPKSLctSVNEVICHGVP---DKTVLKEGDIVNLDVSLYYQGYHAD------LNETYYVGENISKEALNTTetsrecL 256
Cdd:PTZ00053 209 WAFPTGC--SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDcaftvaFNPKYDPLLQATKDATNTG------I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 257 KLA---IKMCKPGTTFQELgdhIEKHATENKCSV-----VRTYCGHGVGEF-FHCSPNIPHYAKNRTpGVMKPGMVFTIE 327
Cdd:PTZ00053 281 KEAgidVRLSDIGAAIQEV---IESYEVEIKGKTypiksIRNLNGHSIGPYiIHGGKSVPIVKGGEN-TRMEEGELFAIE 356
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
134-376 |
9.53e-07 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 50.40 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 134 QIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIkrgAYPSPlnyyNFPKSLCTSVNEVICHGV-PDKTVLKE 212
Cdd:PRK14576 182 EIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVM---SFPET----NFSRFNLISVGDNFSPKIiADTTPAKV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 213 GDIVNLDVSLYYQGYHADLNETYYVGE--NISKEALNTTETSRECLklaIKMCKPGTTFQELGDH-IEKHATENKCSVVR 289
Cdd:PRK14576 255 GDLIKFDCGIDVAGYGADLARTFVLGEpdKLTQQIYDTIRTGHEHM---LSMVAPGVKLKAVFDStMAVIKTSGLPHYNR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 290 TYCGHGVGEFFHCSPniPHYAKNRTPGVMKPGMVFTIEpminegtwkdmtwpddwTSTTQDGKLSAQFEHTLLVTEHGVE 369
Cdd:PRK14576 332 GHLGHGDGVFLGLEE--VPFVSTQATETFCPGMVLSLE-----------------TPYYGIGVGSIMLEDMILITDSGFE 392
|
....*..
gi 6323273 370 ILTARNK 376
Cdd:PRK14576 393 FLSKLDR 399
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
134-327 |
1.47e-05 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 46.63 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 134 QIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRgaypSPLNYYNFpkSLCTSVNEVICHGVPDKTVLKEG 213
Cdd:PRK15173 100 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRF--HLISVGADFSPKLIPSNTKACSG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 214 DIVNLDVSLYYQGYHADLNETYYVGE--NISKEALNTTETSRECLklaIKMCKPGTTFQELGDH----IEKHATENkcsV 287
Cdd:PRK15173 174 DLIKFDCGVDVDGYGADIARTFVVGEppEITRKIYQTIRTGHEHM---LSMVAPGVKMKDVFDStmevIKKSGLPN---Y 247
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323273 288 VRTYCGHGVGEFFHC--SPNIPHYAKNRtpgvMKPGMVFTIE 327
Cdd:PRK15173 248 NRGHLGHGNGVFLGLeeSPFVSTHATES----FTSGMVLSLE 285
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
134-327 |
2.63e-05 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 45.85 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 134 QIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRgaypSPLNYYNFpkSLCTSVNEVICHGVPDKTVLKEG 213
Cdd:PRK14575 183 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK----SETHFSRF--HLISVGADFSPKLIPSNTKACSG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 214 DIVNLDVSLYYQGYHADLNETYYVGE--NISKEALNTTETSRECLklaIKMCKPGTTFQELGDH----IEKHATENkcsV 287
Cdd:PRK14575 257 DLIKFDCGVDVDGYGADIARTFVVGEppEITRKIYQTIRTGHEHM---LSMVAPGVKMKDVFDStmevIKKSGLPN---Y 330
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323273 288 VRTYCGHGVGEFFHC--SPNIPHYAKNRtpgvMKPGMVFTIE 327
Cdd:PRK14575 331 NRGHLGHGNGVFLGLeeSPFVSTHATES----FTSGMVLSLE 368
|
|
| Creatinase |
cd01090 |
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea. |
209-330 |
2.27e-04 |
|
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
Pssm-ID: 238523 [Multi-domain] Cd Length: 228 Bit Score: 42.14 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323273 209 VLKEGDIVNLDVSLYYQGYHADLNETYYVGEnISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVV 288
Cdd:cd01090 76 KVQRGDILSLNCFPMIAGYYTALERTLFLDE-VSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRY 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6323273 289 RTY-CGHGVGEFFHcspnipHYAknRTPG---------VMKPGMVFTIEPMI 330
Cdd:cd01090 155 RTFgYGHSFGVLSH------YYG--REAGlelredidtVLEPGMVVSMEPMI 198
|
|
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
293-328 |
2.24e-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: 39.08 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|....*...
gi 6323273 293 GHGVGEFF--HCSPNIPHYAKNRTPgvMKPGMVFTIEP 328
Cdd:cd01085 161 GHGVGSFLnvHEGPQSISPAPNNVP--LKAGMILSNEP 196
|
|
| |
