|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
6-438 |
0e+00 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 562.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 6 KSEFKARRERLLAQMDKNSVAIIPAASEVTRSRDTEYAFRQDSDFFYLTGFNEPDAVLVLCNNSDAP--STLFCLDKDKL 83
Cdd:PRK10879 3 QQEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHnhSVLFNRVRDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 84 AEIWHGRRVGFDKAKSDYLFDEAYPLSELNDKLLDILNEKDAIYFAQGAYTSFDTKVFTLLGTLRSGARKGLKAPSTLKE 163
Cdd:PRK10879 83 AEIWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYHAQGEYAYADEIVFSALEKLRKGSRQNLTAPATLTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 164 IRGLIHEMRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHY 243
Cdd:PRK10879 163 WRPWVHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 244 TQNSDVLKNGDLVLIDSGCELQGYAADITRTFPVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQG 323
Cdd:PRK10879 243 TENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEVVRIMVSG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 324 LLDLGILTGDFDELMAKGACKEYYMHGLGHWLGLDVHDVGDYKVNNvERAFEPGMVLTIEPGLYISEDSSAPQKYKGIGI 403
Cdd:PRK10879 323 LVKLGILKGDVDQLIAENAHRPFFMHGLSHWLGLDVHDVGVYGQDR-SRILEPGMVLTVEPGLYIAPDADVPEQYRGIGI 401
|
410 420 430
....*....|....*....|....*....|....*
gi 639319551 404 RIEDNLLVTETGHENLTLSVPKKISDIEALMQSAK 438
Cdd:PRK10879 402 RIEDDIVITETGNENLTASVVKKPDEIEALMAAAR 436
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
180-420 |
7.91e-119 |
|
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: 346.48 E-value: 7.91e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPhPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLID 259
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGAR-LAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 260 SGCELQGYAADITRTFPVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQGLLDLGILTGDFDELMA 339
Cdd:cd01087 80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGDVDEIVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 340 KGACKEYYMHGLGHWLGLDVHDVGDYKV-NNVERAFEPGMVLTIEPGLYISED-SSAPQKYKGIGIRIEDNLLVTETGHE 417
Cdd:cd01087 160 SGAYAKFFPHGLGHYLGLDVHDVGGYLRyLRRARPLEPGMVITIEPGIYFIPDlLDVPEYFRGGGIRIEDDVLVTEDGPE 239
|
...
gi 639319551 418 NLT 420
Cdd:cd01087 240 NLT 242
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
154-430 |
3.28e-99 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 298.66 E-value: 3.28e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 154 GLKAPSTLKEIRGLIHEMRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVG 233
Cdd:COG0006 53 ELEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAEGPSFDTIVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 234 SGDNANILHYTQNSDVLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHAN 313
Cdd:COG0006 133 SGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAV-GEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 314 KLAMEVMTQGLLdlgiltgdfdelmakgacKEYYMHGLGHWLGLDVHDVGDYKVNNvERAFEPGMVLTIEPGLYIsedss 393
Cdd:COG0006 212 AAARDVLAEAGY------------------GEYFPHGTGHGVGLDVHEGPQISPGN-DRPLEPGMVFTIEPGIYI----- 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 639319551 394 aPQKYkgiGIRIEDNLLVTETGHENLTlSVPKKISDI 430
Cdd:COG0006 268 -PGIG---GVRIEDTVLVTEDGAEVLT-RLPRELLEL 299
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
183-413 |
8.58e-72 |
|
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: 225.20 E-value: 8.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 183 MREGCEISARGHMRAMRFSHPGATEFQLEAELHHH-YAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLIDSG 261
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 262 CELQ-GYAADITRTFpVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQGLLDlgiltgdfdelmak 340
Cdd:pfam00557 83 AEYDgGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639319551 341 gackEYYMHGLGHWLGLDVHDVGDYKVNNVERAFEPGMVLTIEPGLYISEDSSapqkykgiGIRIEDNLLVTE 413
Cdd:pfam00557 148 ----EYFPHGLGHGIGLEVHEGPYISRGGDDRVLEPGMVFTIEPGIYFIPGWG--------GVRIEDTVLVTE 208
|
|
| AMP_N |
smart01011 |
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ... |
6-137 |
2.97e-55 |
|
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
Pssm-ID: 198079 Cd Length: 135 Bit Score: 179.74 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 6 KSEFKARRERLLAQMDKNSVAIIPAASEVTRSRDTEYAFRQDSDFFYLTGFNEPDAVLVL-CNNSDAPSTLFCLDKDKLA 84
Cdd:smart01011 3 AAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLdPSGGGGKSTLFVPPRDPED 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 639319551 85 EIWHGRRVGFDKAKSDYLFDEAYPLSELNDKLLDILNEKDAIYFAQGAYTSFD 137
Cdd:smart01011 83 ELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLLGRDPDLD 135
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
175-421 |
4.53e-15 |
|
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: 74.69 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGA---PHPAYG---TIVGSgDNANILHYTQNSD 248
Cdd:TIGR00500 4 KSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAkpaFLGYYGfpgSVCIS-VNEVVIHGIPDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 249 VLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGgymshanklamevMTQGllDLG 328
Cdd:TIGR00500 83 VLKDGDIVNIDVGVIYDGYHGDTAKTFLV-GKISPEAEKLLECTEESLYKAIEEAKPG-------------NRIG--EIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 329 ILTGDFDELMAKGACKEYYMHGLGHWLGLDVHdVGDYKVNNVERAFEPGMVLTIEPGLYI--SEDSSAPQKY------KG 400
Cdd:TIGR00500 147 AAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQ-IPNYGKKFTNVRLKEGMVFTIEPMVNTgtEEITTAADGWtvktkdGS 225
|
250 260
....*....|....*....|.
gi 639319551 401 IGIRIEDNLLVTETGHENLTL 421
Cdd:TIGR00500 226 LSAQFEHTIVITDNGPEILTE 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
6-438 |
0e+00 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 562.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 6 KSEFKARRERLLAQMDKNSVAIIPAASEVTRSRDTEYAFRQDSDFFYLTGFNEPDAVLVLCNNSDAP--STLFCLDKDKL 83
Cdd:PRK10879 3 QQEFQRRRQALLAKMQPGSAALIFAAPEATRSADSEYPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHnhSVLFNRVRDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 84 AEIWHGRRVGFDKAKSDYLFDEAYPLSELNDKLLDILNEKDAIYFAQGAYTSFDTKVFTLLGTLRSGARKGLKAPSTLKE 163
Cdd:PRK10879 83 AEIWFGRRLGQDAAPEKLGVDRALPFSEINQQLYQLLNGLDVVYHAQGEYAYADEIVFSALEKLRKGSRQNLTAPATLTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 164 IRGLIHEMRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHY 243
Cdd:PRK10879 163 WRPWVHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 244 TQNSDVLKNGDLVLIDSGCELQGYAADITRTFPVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQG 323
Cdd:PRK10879 243 TENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVTGEVVRIMVSG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 324 LLDLGILTGDFDELMAKGACKEYYMHGLGHWLGLDVHDVGDYKVNNvERAFEPGMVLTIEPGLYISEDSSAPQKYKGIGI 403
Cdd:PRK10879 323 LVKLGILKGDVDQLIAENAHRPFFMHGLSHWLGLDVHDVGVYGQDR-SRILEPGMVLTVEPGLYIAPDADVPEQYRGIGI 401
|
410 420 430
....*....|....*....|....*....|....*
gi 639319551 404 RIEDNLLVTETGHENLTLSVPKKISDIEALMQSAK 438
Cdd:PRK10879 402 RIEDDIVITETGNENLTASVVKKPDEIEALMAAAR 436
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
180-420 |
7.91e-119 |
|
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: 346.48 E-value: 7.91e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPhPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLID 259
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGAR-LAYSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 260 SGCELQGYAADITRTFPVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQGLLDLGILTGDFDELMA 339
Cdd:cd01087 80 AGAEYGGYASDITRTFPVNGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLKELGILKGDVDEIVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 340 KGACKEYYMHGLGHWLGLDVHDVGDYKV-NNVERAFEPGMVLTIEPGLYISED-SSAPQKYKGIGIRIEDNLLVTETGHE 417
Cdd:cd01087 160 SGAYAKFFPHGLGHYLGLDVHDVGGYLRyLRRARPLEPGMVITIEPGIYFIPDlLDVPEYFRGGGIRIEDDVLVTEDGPE 239
|
...
gi 639319551 418 NLT 420
Cdd:cd01087 240 NLT 242
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
154-430 |
3.28e-99 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 298.66 E-value: 3.28e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 154 GLKAPSTLKEIRGLIHEMRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVG 233
Cdd:COG0006 53 ELEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAEGPSFDTIVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 234 SGDNANILHYTQNSDVLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHAN 313
Cdd:COG0006 133 SGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAV-GEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 314 KLAMEVMTQGLLdlgiltgdfdelmakgacKEYYMHGLGHWLGLDVHDVGDYKVNNvERAFEPGMVLTIEPGLYIsedss 393
Cdd:COG0006 212 AAARDVLAEAGY------------------GEYFPHGTGHGVGLDVHEGPQISPGN-DRPLEPGMVFTIEPGIYI----- 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 639319551 394 aPQKYkgiGIRIEDNLLVTETGHENLTlSVPKKISDI 430
Cdd:COG0006 268 -PGIG---GVRIEDTVLVTEDGAEVLT-RLPRELLEL 299
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
183-413 |
8.58e-72 |
|
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: 225.20 E-value: 8.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 183 MREGCEISARGHMRAMRFSHPGATEFQLEAELHHH-YAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLIDSG 261
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 262 CELQ-GYAADITRTFpVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQGLLDlgiltgdfdelmak 340
Cdd:pfam00557 83 AEYDgGYCSDITRTF-VVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639319551 341 gackEYYMHGLGHWLGLDVHDVGDYKVNNVERAFEPGMVLTIEPGLYISEDSSapqkykgiGIRIEDNLLVTE 413
Cdd:pfam00557 148 ----EYFPHGLGHGIGLEVHEGPYISRGGDDRVLEPGMVFTIEPGIYFIPGWG--------GVRIEDTVLVTE 208
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
180-416 |
3.27e-56 |
|
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: 184.63 E-value: 3.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLID 259
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 260 SGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMT-QGLldlgiltgdfdelm 338
Cdd:cd01092 81 FGAIYDGYCSDITRTVAV-GEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEeAGY-------------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639319551 339 akgacKEYYMHGLGHWLGLDVHDvGDYKVNNVERAFEPGMVLTIEPGLYIsedssaPQKYkgiGIRIEDNLLVTETGH 416
Cdd:cd01092 146 -----GEYFIHRTGHGVGLEVHE-APYISPGSDDVLEEGMVFTIEPGIYI------PGKG---GVRIEDDVLVTEDGC 208
|
|
| AMP_N |
smart01011 |
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ... |
6-137 |
2.97e-55 |
|
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain. However, little or no sequence similarity exists between the two families.
Pssm-ID: 198079 Cd Length: 135 Bit Score: 179.74 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 6 KSEFKARRERLLAQMDKNSVAIIPAASEVTRSRDTEYAFRQDSDFFYLTGFNEPDAVLVL-CNNSDAPSTLFCLDKDKLA 84
Cdd:smart01011 3 AAEYAARRRRLAAKLFPGSVAVLPAGPEKVRSNDTDYPFRQDSDFYYLTGFDEPDAVLVLdPSGGGGKSTLFVPPRDPED 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 639319551 85 EIWHGRRVGFDKAKSDYLFDEAYPLSELNDKLLDILNEKDAIYFAQGAYTSFD 137
Cdd:smart01011 83 ELWDGPRLGLEEAKEKFGVDEVYPIDELDAVLPGLLAGAGTVYYLLGRDPDLD 135
|
|
| AMP_N |
pfam05195 |
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the ... |
9-127 |
4.12e-52 |
|
Aminopeptidase P, N-terminal domain; This domain is structurally very similar to the creatinase N-terminal domain (pfam01321). However, little or no sequence similarity exists between the two families.
Pssm-ID: 461581 [Multi-domain] Cd Length: 121 Bit Score: 171.15 E-value: 4.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 9 FKARRERLLAQMDKNSVAIIPAASEVTRSRDTEYAFRQDSDFFYLTGFNEPDAVLVLCNNSDAP--STLFCLDKDKLAEI 86
Cdd:pfam05195 1 YAERRARLLAKLPPNSVAILPGAPEKYRNGDVFYPFRQDSDFYYLTGFNEPDAVLVLEGGDIDSgkETLFVPPKDPEDEI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 639319551 87 WHGRRVGFDKAKSDYLFDEAYPLSELNDKLLDILNEKDAIY 127
Cdd:pfam05195 81 WDGPRLGPEEAKELFGVDEVYPIDELDEVLPKLLKGRDTVY 121
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
180-416 |
1.83e-50 |
|
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: 169.94 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHhYAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLKNGDLVLID 259
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQ-ALRAAGGYPAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 260 SGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQGLLdlgiltgdfdelma 339
Cdd:cd01066 80 LGGVYDGYHADLTRTFVI-GEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGL-------------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639319551 340 kgacKEYYMHGLGHWLGLDVHDVGDYKVNNVERaFEPGMVLTIEPGLYIsedssapqkYKGIGIRIEDNLLVTETGH 416
Cdd:cd01066 145 ----GPNFGHRTGHGIGLEIHEPPVLKAGDDTV-LEPGMVFAVEPGLYL---------PGGGGVRIEDTVLVTEDGP 207
|
|
| PRK13607 |
PRK13607 |
proline dipeptidase; Provisional |
168-420 |
2.03e-45 |
|
proline dipeptidase; Provisional
Pssm-ID: 237444 [Multi-domain] Cd Length: 443 Bit Score: 163.14 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 168 IHEMRLFKSPSEIDVMREGCEISARGHM--RAMRFShpGATEFqleaELHHHYAM------NGAPhpaYGTIVGSGDNAN 239
Cdd:PRK13607 155 LHYHRAYKTDYELACMREAQKIAVAGHRaaKEAFRA--GMSEF----DINLAYLTatgqrdNDVP---YGNIVALNEHAA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 240 ILHYTQnSDVLKNGDL--VLIDSGCELQGYAADITRTFPVNGQfsEEQAALYNIVLKAQEVAFDEVKPG-GYMS-----H 311
Cdd:PRK13607 226 VLHYTK-LDHQAPAEMrsFLIDAGAEYNGYAADITRTYAAKED--NDFAALIKDVNKEQLALIATMKPGvSYVDlhiqmH 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 312 AnKLAmevmtQGLLDLGILTG-DFDELMAKGACKEYYMHGLGHWLGLDVHDVG----DYKVNNVE-----------RAFE 375
Cdd:PRK13607 303 Q-RIA-----KLLRKFQIVTGlSEEAMVEQGITSPFFPHGLGHPLGLQVHDVAgfmqDDRGTHLAapekhpylrctRVLE 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639319551 376 PGMVLTIEPGLYISEDSSAPQKY----KGI------------GIRIEDNLLVTETGHENLT 420
Cdd:PRK13607 377 PGMVLTIEPGLYFIDSLLAPLREgpfsKHFnwqkidalkpfgGIRIEDNVVVHENGVENMT 437
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
171-427 |
1.51e-37 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 140.07 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 171 MRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHYTQNSDVL 250
Cdd:PRK09795 124 LRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 251 KNGDLVLIDSGCELQGYAADITRTFPVNGQFSEEQA----ALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQglld 326
Cdd:PRK09795 204 AAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITE---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 327 lgiltgdfdelmakGACKEYYMHGLGHWLGLDVHDVGDYKVNNVERaFEPGMVLTIEPGLYISEDSsapqkykgiGIRIE 406
Cdd:PRK09795 280 --------------AGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTT-LQPGMLLTVEPGIYLPGQG---------GVRIE 335
|
250 260
....*....|....*....|.
gi 639319551 407 DNLLVTETGHENLtLSVPKKI 427
Cdd:PRK09795 336 DVVLVTPQGAEVL-YAMPKTV 355
|
|
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
206-418 |
1.56e-23 |
|
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: 98.02 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 206 TEFQLEAELHHHYAMN-GAPHPAYGTIVGSGDNANILHY--TQNSD-VLKNGDLVLIDSGCELQGYAADITRTFPVnGQF 281
Cdd:cd01085 31 TELSAADKLEEFRRQQkGYVGLSFDTISGFGPNGAIVHYspTEESNrKISPDGLYLIDSGGQYLDGTTDITRTVHL-GEP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 282 SEEQAALYNIVLKAQeVAFDEVKpggYMSHANKLAMEVMT-QGLLDLGIltgDFDelmakgackeyymHGLGHWLG--LD 358
Cdd:cd01085 110 TAEQKRDYTLVLKGH-IALARAK---FPKGTTGSQLDALArQPLWKAGL---DYG-------------HGTGHGVGsfLN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639319551 359 VHD--VGDYKVNNVErAFEPGMVLTIEPGLYIsedssaPQKYkgiGIRIEDNLLVTETGHEN 418
Cdd:cd01085 170 VHEgpQSISPAPNNV-PLKAGMILSNEPGYYK------EGKY---GIRIENLVLVVEAETTE 221
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
180-421 |
2.32e-16 |
|
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: 77.92 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGA---PHPAYG------TIVgsgdNANILHYTQNSDVL 250
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAypaPLGYYGfpksicTSV----NEVVCHGIPDDRVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 251 KNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYmshanklamevmtqgLLDLGIL 330
Cdd:cd01086 77 KDGDIVNIDVGVELDGYHGDSARTFIV-GEVSEEAKKLVEVTEEALYKGIEAVKPGNR---------------IGDIGHA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 331 TGDFDELMAKGACKEYymhgLGHWLGLDVH---DVGDYKVNNVERAFEPGMVLTIEPglYISEDSSAP-QKYKGIGIRIE 406
Cdd:cd01086 141 IEKYAEKNGYSVVREF----GGHGIGRKFHeepQIPNYGRPGTGPKLKPGMVFTIEP--MINLGTYEVvTLPDGWTVVTK 214
|
250 260
....*....|....*....|....
gi 639319551 407 DN---------LLVTETGHENLTL 421
Cdd:cd01086 215 DGslsaqfehtVLITEDGPEILTL 238
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
175-422 |
9.23e-16 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 76.58 E-value: 9.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGApHPAY-------GTI---VgsgdNANILHYT 244
Cdd:COG0024 4 KTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGA-IPAFlgyygfpKSIctsV----NEVVVHGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 245 QNSDVLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMShanklamevmtqgl 324
Cdd:COG0024 79 PSDRVLKDGDIVNIDVGAILDGYHGDSARTFVV-GEVSPEARRLVEVTEEALYAGIAAAKPGNRLG-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 325 lDLGILTGDFdelmAKGA----CKEYYMHGLGHwlglDVH---DVGDYKVNNVERAFEPGMVLTIEPGL-------YISE 390
Cdd:COG0024 144 -DIGHAIQSY----AESNgysvVREFVGHGIGR----EMHeepQVPNYGRPGRGPRLKPGMVLAIEPMInagtpevKVLD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 639319551 391 DssapqkykGIGIRIEDN---------LLVTETGHENLTLS 422
Cdd:COG0024 215 D--------GWTVVTKDGslsaqfehtVAVTEDGPEILTLP 247
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
175-421 |
4.53e-15 |
|
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: 74.69 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGA---PHPAYG---TIVGSgDNANILHYTQNSD 248
Cdd:TIGR00500 4 KSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAkpaFLGYYGfpgSVCIS-VNEVVIHGIPDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 249 VLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGgymshanklamevMTQGllDLG 328
Cdd:TIGR00500 83 VLKDGDIVNIDVGVIYDGYHGDTAKTFLV-GKISPEAEKLLECTEESLYKAIEEAKPG-------------NRIG--EIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 329 ILTGDFDELMAKGACKEYYMHGLGHWLGLDVHdVGDYKVNNVERAFEPGMVLTIEPGLYI--SEDSSAPQKY------KG 400
Cdd:TIGR00500 147 AAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQ-IPNYGKKFTNVRLKEGMVFTIEPMVNTgtEEITTAADGWtvktkdGS 225
|
250 260
....*....|....*....|.
gi 639319551 401 IGIRIEDNLLVTETGHENLTL 421
Cdd:TIGR00500 226 LSAQFEHTIVITDNGPEILTE 246
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
175-422 |
1.49e-14 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 73.24 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHmRAMR-FSHPGATEFQLEAELHHHYAMNGApHPA----YG------TIVgsgdNANILHY 243
Cdd:PRK05716 6 KTPEEIEKMRVAGRLAAEVL-DEIEpHVKPGVTTKELDRIAEEYIRDQGA-IPAplgyHGfpksicTSV----NEVVCHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 244 TQNSDVLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGgymshaNKLAmevmtqg 323
Cdd:PRK05716 80 IPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGV-GEISPEDKRLCEVTKEALYLGIAAVKPG------ARLG------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 324 llDLGILTGDFdelmAKGA----CKEYYMHGLGHWLgldvHD---VGDYKVNNVERAFEPGMVLTIEP-------GLYIS 389
Cdd:PRK05716 146 --DIGHAIQKY----AEAEgfsvVREYCGHGIGRKF----HEepqIPHYGAPGDGPVLKEGMVFTIEPminagkrEVKTL 215
|
250 260 270
....*....|....*....|....*....|....
gi 639319551 390 EDS-SAPQKYKGIGIRIEDNLLVTETGHENLTLS 422
Cdd:PRK05716 216 KDGwTVVTKDGSLSAQYEHTVAVTEDGPEILTLR 249
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
175-421 |
6.55e-14 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 71.41 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGApHPAY-------GTIVGSgDNANILHYTQNS 247
Cdd:PRK12896 11 KSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGA-IPSPegyygfpGSTCIS-VNEEVAHGIPGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 248 DVLKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYmshanklamevmtqgLLDL 327
Cdd:PRK12896 89 RVIKDGDLVNIDVSAYLDGYHGDTGITFAV-GPVSEEAEKLCRVAEEALWAGIKQVKAGRP---------------LNDI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 328 GILTGDFDELMAKGACKEYYMHGLGHWLGLDVHDVGDYKVNNVERAFEPGMVLTIEPGL---------------YISEDS 392
Cdd:PRK12896 153 GRAIEDFAKKNGYSVVRDLTGHGVGRSLHEEPSVILTYTDPLPNRLLRPGMTLAVEPFLnlgakdaetlddgwtVVTPDK 232
|
250 260
....*....|....*....|....*....
gi 639319551 393 SAPQKYkgigiriEDNLLVTETGHENLTL 421
Cdd:PRK12896 233 SLSAQF-------EHTVVVTRDGPEILTD 254
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
108-420 |
1.53e-13 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 71.29 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 108 PLSELNDKLLDILNEKDAIyfaqgaytsfDTKVFTLLGTLRSGARKGLKA--PST-LKEIRGLIHEMRLFKSPSEIDVMR 184
Cdd:PRK15173 36 PIESVCNILKDALNDARVL----------NKKIAIDLNIMSNGGKRVIDAvmPNVdFVDSSSIFNELRVIKSPWEIKRLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 185 EGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLkNGDLVLIDSGCEL 264
Cdd:PRK15173 106 KSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLIPSNTKAC-SGDLIKFDCGVDV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 265 QGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQ-GLLDLGiltgdfdelmakgac 343
Cdd:PRK15173 185 DGYGADIARTFVV-GEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKsGLPNYN--------------- 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639319551 344 KEYYMHGLGHWLGLdvhDVGDYKVNNVERAFEPGMVLTIEPGLYisedssapqKYKGIGIRIEDNLLVTETGHENLT 420
Cdd:PRK15173 249 RGHLGHGNGVFLGL---EESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIMIEDMILINKEGIEFLS 313
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
108-420 |
3.90e-13 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 70.51 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 108 PLSELNDKLLDILNEKDAIyfaqgaytsfDTKVFTLLGTLRSGARKGLKA--PST-LKEIRGLIHEMRLFKSPSEIDVMR 184
Cdd:PRK14575 119 PIESVCNILKDALNDARVL----------NKKIAIDLNIMSNGGKRVIDAvmPNVdFVDSSSIFNELRVIKSPWEIKRLR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 185 EGCEISARGHMRAMRFSHPGATEFQLEAELHHHYAMNGAPHPAYGTIVGSGDNANILHYTQNSDVLkNGDLVLIDSGCEL 264
Cdd:PRK14575 189 KSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLIPSNTKAC-SGDLIKFDCGVDV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 265 QGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVMTQ-GLLDLGiltgdfdelmakgac 343
Cdd:PRK14575 268 DGYGADIARTFVV-GEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKsGLPNYN--------------- 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639319551 344 KEYYMHGLGHWLGLdvhDVGDYKVNNVERAFEPGMVLTIEPGLYisedssapqKYKGIGIRIEDNLLVTETGHENLT 420
Cdd:PRK14575 332 RGHLGHGNGVFLGL---EESPFVSTHATESFTSGMVLSLETPYY---------GYNLGSIMIEDMILINKEGIEFLS 396
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
166-420 |
2.45e-12 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 68.12 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 166 GLIHEMRLFKSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHhyAMNGAPHPAYG--TIVGSGDNANILHY 243
Cdd:PRK14576 169 ALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKA--AVMSFPETNFSrfNLISVGDNFSPKII 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 244 TQNSDVlKNGDLVLIDSGCELQGYAADITRTFpVNGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHANKLAMEVM-TQ 322
Cdd:PRK14576 247 ADTTPA-KVGDLIKFDCGIDVAGYGADLARTF-VLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIkTS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 323 GLLDLGiltgdfdelmakgacKEYYMHGLGHWLGLdvhDVGDYKVNNVERAFEPGMVLTIEpglyisedssapQKYKGIG 402
Cdd:PRK14576 325 GLPHYN---------------RGHLGHGDGVFLGL---EEVPFVSTQATETFCPGMVLSLE------------TPYYGIG 374
|
250 260
....*....|....*....|.
gi 639319551 403 ---IRIEDNLLVTETGHENLT 420
Cdd:PRK14576 375 vgsIMLEDMILITDSGFEFLS 395
|
|
| CDC68-like |
cd01091 |
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ... |
228-417 |
2.10e-10 |
|
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.
Pssm-ID: 238524 [Multi-domain] Cd Length: 243 Bit Score: 60.82 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 228 YGTIVGSGDNANILHYTQNSDVLKNGDLVLIDS-GCELQGYAADITRTFPVNGqfSEEQAALYNIVLKAQEVAFDEVKPG 306
Cdd:cd01091 65 YPPIIQSGGNYDLLKSSSSSDKLLYHFGVIICSlGARYKSYCSNIARTFLIDP--TSEQQKNYNFLLALQEEILKELKPG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 307 GYMSHANKLAMEVMTQGLLDLgiltgdfdelmakgacKEYYMHGLGHWLGLDVHDVGDYKVNNVERAFEPGMVLTIEPGL 386
Cdd:cd01091 143 AKLSDVYQKTLDYIKKKKPEL----------------EPNFTKNLGFGIGLEFRESSLIINAKNDRKLKKGMVFNLSIGF 206
|
170 180 190
....*....|....*....|....*....|..
gi 639319551 387 Y-ISEDSSAPQKYKGIGIRIEDNLLVTETGHE 417
Cdd:cd01091 207 SnLQNPEPKDKESKTYALLLSDTILVTEDEPA 238
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
175-424 |
2.40e-09 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 58.70 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 175 KSPSEIDVMREGCEISARGHMRAMRFSHPGATEFQLEAELHHH-YAMNGAPHPA----YGTIVGSGDNANILHYTQNSDV 249
Cdd:PLN03158 138 KTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEAtIAAGGYPSPLnyhfFPKSCCTSVNEVICHGIPDARK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 250 LKNGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGgymshanklamevmtqglldlgI 329
Cdd:PLN03158 218 LEDGDIVNVDVTVYYKGCHGDLNETFFV-GNVDEASRQLVKCTYECLEKAIAIVKPG----------------------V 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 330 LTGDFDELMAKGACkeyyMHGL-------GHWLGLDVH---DVGDYKVNNVERAFEPGMVLTIEPGLY--ISEDSSAPQK 397
Cdd:PLN03158 275 RYREVGEVINRHAT----MSGLsvvksycGHGIGELFHcapNIPHYARNKAVGVMKAGQVFTIEPMINagVWRDRMWPDG 350
|
250 260 270
....*....|....*....|....*....|...
gi 639319551 398 YKGI---GIR---IEDNLLVTETGHENLTLSVP 424
Cdd:PLN03158 351 WTAVtadGKRsaqFEHTLLVTETGVEVLTARLP 383
|
|
| Creatinase |
cd01090 |
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea. |
180-420 |
1.49e-05 |
|
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
Pssm-ID: 238523 [Multi-domain] Cd Length: 228 Bit Score: 45.99 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 180 IDVMREGCEISARGHMRAMRFSHPGATEFqlEAELHHHYAMNGA-----PHPAYG---TIVGSGDNANILHYTQNSDVLK 251
Cdd:cd01090 1 IALIRHGARIADIGGAAVVEAIREGVPEY--EVALAGTQAMVREiaktfPEVELMdtwTWFQSGINTDGAHNPVTNRKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 252 NGDLVLIDSGCELQGYAADITRTFPVnGQFSEEQAALYNIVLKAQEVAFDEVKPGGYMSHanklamevmtqglldlgiLT 331
Cdd:cd01090 79 RGDILSLNCFPMIAGYYTALERTLFL-DEVSDAHLKIWEANVAVHERGLELIKPGARCKD------------------IA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 332 GDFDELMAKGACKEYYMHGLGHWLGLDVH----DVGDYKVNNVERAFEPGMVLTIEPGLYISEDSSAPQKYkgigiRIED 407
Cdd:cd01090 140 AELNEMYREHDLLRYRTFGYGHSFGVLSHyygrEAGLELREDIDTVLEPGMVVSMEPMIMLPEGQPGAGGY-----REHD 214
|
250
....*....|...
gi 639319551 408 NLLVTETGHENLT 420
Cdd:cd01090 215 ILVINENGAENIT 227
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
249-306 |
5.64e-04 |
|
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: 41.80 E-value: 5.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639319551 249 VLKNGDLVLIDSGCELQGYAADITRTFPVNGQFSEEQAALYNIVLKAQ----EVAFDEVKPG 306
Cdd:TIGR00495 101 ILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKADVIAAAhlaaEAALRLVKPG 162
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
237-307 |
4.27e-03 |
|
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: 38.47 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319551 237 NANILHYT----QNSDVLKNGDLVLIDSGCELQGYAADITRTF---PVNGQFSEEQAAlyNIVLKAQ---EVAFDEVKPG 306
Cdd:cd01089 66 NNCVCHFSplksDATYTLKDGDVVKIDLGCHIDGYIAVVAHTIvvgAEAETPVTGKKA--DVIAAAHyalEAALRLLRPG 143
|
.
gi 639319551 307 G 307
Cdd:cd01089 144 N 144
|
|
| |
