|
Name |
Accession |
Description |
Interval |
E-value |
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
6-354 |
1.42e-104 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 309.06 E-value: 1.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 6 ARLQQTFEELKIDAFLVSSEANLHYLTGM-ADMAGDGYLLVLADD-AYLITDARYQTAfagqyddehlvitrdylgavcq 83
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGFrGSPERLAALLVTADGePVLFVDELEAER---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 84 liattqtgvmgfeddlpyvaysyldenlvsDLVALPTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREID 163
Cdd:COG0006 59 ------------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTERE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 164 VSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQ 243
Cdd:COG0006 109 VAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 244 AVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLAIHEAPLISKNTANRLVANSVVTVEPGVYFP 323
Cdd:COG0006 189 AVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIP 268
|
330 340 350
....*....|....*....|....*....|.
gi 1655161503 324 GLGGMRIEDDVLVTATGHERLTKATRDLLIL 354
Cdd:COG0006 269 GIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
134-341 |
1.08e-100 |
|
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: 295.96 E-value: 1.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 134 IEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLA 293
Cdd:cd01092 81 FGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGHGVGLE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655161503 294 IHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGH 341
Cdd:cd01092 161 VHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
4-353 |
3.17e-80 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 249.08 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 4 RIARLQQTFEELKIDAFLVSSEANLHYLTGMAdmAGDGYLLVLADDAYLITDARYQT---AFAGQYDDEHLVITRDYLGA 80
Cdd:PRK09795 3 LLASLRDWLKAQQLDAVLLSSRQNKQPHLGIS--TGSGYVVISRESAHILVDSRYYAdveARAQGYQLHLLDATNTLTTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 81 VCQLIATTQTGVMGFED-----DLPYVAYSYLDENLVSdlvalpTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIV 155
Cdd:PRK09795 81 VNQIIADEQLQTLGFEGqqvswETAHRWQSELNAKLVS------ATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 156 RPGMREIDVSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPD 235
Cdd:PRK09795 155 QAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 236 AK-----LKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLAIHEAPLISKNTANRLVA 310
Cdd:PRK09795 235 VSaeshpLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQP 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1655161503 311 NSVVTVEPGVYFPGLGGMRIEDDVLVTATGHERLTKATRDLLI 353
Cdd:PRK09795 315 GMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLL 357
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
135-338 |
3.19e-74 |
|
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: 228.28 E-value: 3.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 135 EKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAY-MRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FG-YFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGL 292
Cdd:pfam00557 81 VGaEYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGHGIGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655161503 293 AIHEAPLIS-KNTANRLVANSVVTVEPGVYF-PGLGGMRIEDDVLVTA 338
Cdd:pfam00557 161 EVHEGPYISrGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
129-320 |
2.43e-25 |
|
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: 102.43 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 129 KSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKA-----SFTTIVVGGARAALPHGTASTAL 203
Cdd:TIGR00500 4 KSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAflgyyGFPGSVCISVNEVVIHGIPDKKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 204 LEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFN 283
Cdd:TIGR00500 84 LKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVRE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1655161503 284 HGmGHGIGLAIHEAPLI----SKNTANRLVANSVVTVEPGV 320
Cdd:TIGR00500 164 YC-GHGIGRKFHEEPQIpnygKKFTNVRLKEGMVFTIEPMV 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
6-354 |
1.42e-104 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 309.06 E-value: 1.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 6 ARLQQTFEELKIDAFLVSSEANLHYLTGM-ADMAGDGYLLVLADD-AYLITDARYQTAfagqyddehlvitrdylgavcq 83
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGFrGSPERLAALLVTADGePVLFVDELEAER---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 84 liattqtgvmgfeddlpyvaysyldenlvsDLVALPTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREID 163
Cdd:COG0006 59 ------------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTERE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 164 VSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQ 243
Cdd:COG0006 109 VAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 244 AVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLAIHEAPLISKNTANRLVANSVVTVEPGVYFP 323
Cdd:COG0006 189 AVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIP 268
|
330 340 350
....*....|....*....|....*....|.
gi 1655161503 324 GLGGMRIEDDVLVTATGHERLTKATRDLLIL 354
Cdd:COG0006 269 GIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
134-341 |
1.08e-100 |
|
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: 295.96 E-value: 1.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 134 IEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLA 293
Cdd:cd01092 81 FGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGHGVGLE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655161503 294 IHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGH 341
Cdd:cd01092 161 VHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
4-353 |
3.17e-80 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 249.08 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 4 RIARLQQTFEELKIDAFLVSSEANLHYLTGMAdmAGDGYLLVLADDAYLITDARYQT---AFAGQYDDEHLVITRDYLGA 80
Cdd:PRK09795 3 LLASLRDWLKAQQLDAVLLSSRQNKQPHLGIS--TGSGYVVISRESAHILVDSRYYAdveARAQGYQLHLLDATNTLTTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 81 VCQLIATTQTGVMGFED-----DLPYVAYSYLDENLVSdlvalpTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIV 155
Cdd:PRK09795 81 VNQIIADEQLQTLGFEGqqvswETAHRWQSELNAKLVS------ATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 156 RPGMREIDVSNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPD 235
Cdd:PRK09795 155 QAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 236 AK-----LKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLAIHEAPLISKNTANRLVA 310
Cdd:PRK09795 235 VSaeshpLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQP 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1655161503 311 NSVVTVEPGVYFPGLGGMRIEDDVLVTATGHERLTKATRDLLI 353
Cdd:PRK09795 315 GMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLL 357
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
135-338 |
3.19e-74 |
|
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: 228.28 E-value: 3.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 135 EKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAY-MRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FG-YFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGL 292
Cdd:pfam00557 81 VGaEYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGHGIGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655161503 293 AIHEAPLIS-KNTANRLVANSVVTVEPGVYF-PGLGGMRIEDDVLVTA 338
Cdd:pfam00557 161 EVHEGPYISrGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
134-341 |
1.24e-57 |
|
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: 185.74 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 134 IEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGAsKASFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGG-YPAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFNHGMGHGIGLA 293
Cdd:cd01066 80 LGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFGHRTGHGIGLE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655161503 294 IHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGH 341
Cdd:cd01066 160 IHEPPVLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP 207
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
134-346 |
4.45e-42 |
|
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: 146.56 E-value: 4.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 134 IEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAsFTTIVVGGARAALPHGTASTALLEAGQMVTLD 213
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARLA-YSYIVAAGSNAAILHYVHNDQPLKDGDLVLID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 214 FGYFLDDYTSDMTRTFAL-GEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEV----DAVGRDYLTKAG----------- 277
Cdd:cd01087 80 AGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGilkgdvdeive 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 278 ---YGEAFNHGMGHGIGLAIH--EAPLISKNTANRLVANSVVTVEPGVYFP----------GLGGMRIEDDVLVTATGHE 342
Cdd:cd01087 160 sgaYAKFFPHGLGHYLGLDVHdvGGYLRYLRRARPLEPGMVITIEPGIYFIpdlldvpeyfRGGGIRIEDDVLVTEDGPE 239
|
....
gi 1655161503 343 RLTK 346
Cdd:cd01087 240 NLTR 243
|
|
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
161-342 |
2.13e-31 |
|
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: 118.05 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 161 EIDVSNLLDAYMRSHGASKA-SFTTIVVGGARAALPH---GTASTALLEAGQMVTLDFG--YFldDYTSDMTRTFALGEP 234
Cdd:cd01085 32 ELSAADKLEEFRRQQKGYVGlSFDTISGFGPNGAIVHyspTEESNRKISPDGLYLIDSGgqYL--DGTTDITRTVHLGEP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 235 DAKLKAAYQAVLTAQqLVVDQVH--AGANSAEVDAVGRDYLTKAGYGeaFNHGMGHGIG--LAIHEAPL-ISKNTAN-RL 308
Cdd:cd01085 110 TAEQKRDYTLVLKGH-IALARAKfpKGTTGSQLDALARQPLWKAGLD--YGHGTGHGVGsfLNVHEGPQsISPAPNNvPL 186
|
170 180 190
....*....|....*....|....*....|....
gi 1655161503 309 VANSVVTVEPGVYFPGLGGMRIEDDVLVTATGHE 342
Cdd:cd01085 187 KAGMILSNEPGYYKEGKYGIRIENLVLVVEAETT 220
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
127-346 |
9.17e-26 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 103.55 E-value: 9.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 127 ITKSADEIEKLRASAKLADAGFQYVTSIVRPGM--REIDvsNLLDAYMRSHGAsKASFttIVVGGARAAL--------PH 196
Cdd:COG0024 2 EIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVttLELD--RIAEEFIRDHGA-IPAF--LGYYGFPKSIctsvnevvVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 197 GTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAK----LKAAYQAVLTAqqlvVDQVHAGANSAEV-DAVGRd 271
Cdd:COG0024 77 GIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEarrlVEVTEEALYAG----IAAAKPGNRLGDIgHAIQS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 272 YLTKAGYG--EAFnhgMGHGIGLAIHEAPLIS----KNTANRLVANSVVTVEPGVyfpGLGG--MRIEDD---------- 333
Cdd:COG0024 152 YAESNGYSvvREF---VGHGIGREMHEEPQVPnygrPGRGPRLKPGMVLAIEPMI---NAGTpeVKVLDDgwtvvtkdgs 225
|
250 260
....*....|....*....|.
gi 1655161503 334 --------VLVTATGHERLTK 346
Cdd:COG0024 226 lsaqfehtVAVTEDGPEILTL 246
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
129-320 |
2.43e-25 |
|
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: 102.43 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 129 KSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKA-----SFTTIVVGGARAALPHGTASTAL 203
Cdd:TIGR00500 4 KSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAflgyyGFPGSVCISVNEVVIHGIPDKKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 204 LEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFN 283
Cdd:TIGR00500 84 LKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVRE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1655161503 284 HGmGHGIGLAIHEAPLI----SKNTANRLVANSVVTVEPGV 320
Cdd:TIGR00500 164 YC-GHGIGRKFHEEPQIpnygKKFTNVRLKEGMVFTIEPMV 203
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
114-352 |
9.65e-25 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 102.49 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 114 DLVALPTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-FTTIVVGG--A 190
Cdd:PRK15173 81 DFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSrFHLISVGAdfS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 191 RAALPHGTASTAlleaGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGR 270
Cdd:PRK15173 161 PKLIPSNTKACS----GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 271 DYLTKAGYGEaFNHG-MGHGIG--LAIHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGHERLTKA 347
Cdd:PRK15173 237 EVIKKSGLPN-YNRGhLGHGNGvfLGLEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKL 315
|
....*
gi 1655161503 348 TRDLL 352
Cdd:PRK15173 316 PRDLV 320
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
114-352 |
4.86e-24 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 101.71 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 114 DLVALPTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-FTTIVVGG--A 190
Cdd:PRK14575 164 DFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSrFHLISVGAdfS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 191 RAALPHGTASTAlleaGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGR 270
Cdd:PRK14575 244 PKLIPSNTKACS----GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTM 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 271 DYLTKAGYGEaFNHG-MGHGIG--LAIHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGHERLTKA 347
Cdd:PRK14575 320 EVIKKSGLPN-YNRGhLGHGNGvfLGLEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKL 398
|
....*
gi 1655161503 348 TRDLL 352
Cdd:PRK14575 399 PRDLV 403
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
91-345 |
8.98e-23 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 98.64 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 91 GVMGFEDDLPYVAYSYLDENLVSDLVALPTVVD------TLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDV 164
Cdd:PRK10879 130 GEYAYADEIVFSALEKLRKGSRQNLTAPATLTDwrpwvhEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 165 SNLLDAYMRSHGASKASFTTIVVGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFAL-GEPDAKLKAAYQ 243
Cdd:PRK10879 210 EGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYD 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 244 AVLTAQQLVVDQVHAGANSAEV-DAVGR---DYLTKAG--------------YGEAFNHGMGHGIGLAIHEAPLISKNTA 305
Cdd:PRK10879 290 IVLESLETSLRLYRPGTSIREVtGEVVRimvSGLVKLGilkgdvdqliaenaHRPFFMHGLSHWLGLDVHDVGVYGQDRS 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1655161503 306 NRLVANSVVTVEPGVY----------FPGLgGMRIEDDVLVTATGHERLT 345
Cdd:PRK10879 370 RILEPGMVLTVEPGLYiapdadvpeqYRGI-GIRIEDDIVITETGNENLT 418
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
134-346 |
1.48e-22 |
|
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: 94.48 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 134 IEKLRASAKLADAGFQYVTSIVRPGM--REIDvsNLLDAYMRSHGAsKASF-----------TTI---VVggaraalpHG 197
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVttKELD--QIAHEFIEEHGA-YPAPlgyygfpksicTSVnevVC--------HG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 198 TASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAG 277
Cdd:cd01086 70 IPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 278 YG--EAFnhgMGHGIGLAIHEAPLI----SKNTANRLVANSVVTVEPGVyFPGLGGMRIEDD------------------ 333
Cdd:cd01086 150 YSvvREF---GGHGIGRKFHEEPQIpnygRPGTGPKLKPGMVFTIEPMI-NLGTYEVVTLPDgwtvvtkdgslsaqfeht 225
|
250
....*....|...
gi 1655161503 334 VLVTATGHERLTK 346
Cdd:cd01086 226 VLITEDGPEILTL 238
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
129-346 |
1.11e-20 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 89.81 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 129 KSADEIEKLRASAKLADAGFQYVTSIVRPGM--REIDvsNLLDAYMRSHGAsKASF-----------TTI---VVggara 192
Cdd:PRK05716 6 KTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVttKELD--RIAEEYIRDQGA-IPAPlgyhgfpksicTSVnevVC----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 193 alpHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLK----AAYQAVLTAqqlvVDQVHAGANSAEVDAV 268
Cdd:PRK05716 78 ---HGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKrlceVTKEALYLG----IAAVKPGARLGDIGHA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 269 GRDYLTKAGYGEAFNHGmGHGIGLAIHEAPLI----SKNTANRLVANSVVTVEPGVYfPGLGGMRIEDD----------- 333
Cdd:PRK05716 151 IQKYAEAEGFSVVREYC-GHGIGRKFHEEPQIphygAPGDGPVLKEGMVFTIEPMIN-AGKREVKTLKDgwtvvtkdgsl 228
|
250 260
....*....|....*....|
gi 1655161503 334 -------VLVTATGHERLTK 346
Cdd:PRK05716 229 saqyehtVAVTEDGPEILTL 248
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
115-351 |
4.71e-20 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 90.46 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 115 LVALPTVVDTLRITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-FTTIVVGGARAa 193
Cdd:PRK14576 164 LVDSTALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMSFPETNFSrFNLISVGDNFS- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 194 lPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYL 273
Cdd:PRK14576 243 -PKIIADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 274 TKAGYGEAFNHGMGHGIG--LAIHEAPLISKNTANRLVANSVVTVEPGVYFPGLGGMRIEDDVLVTATGHERLTKATRDL 351
Cdd:PRK14576 322 KTSGLPHYNRGHLGHGDGvfLGLEEVPFVSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILITDSGFEFLSKLDRDL 401
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
4-127 |
4.29e-16 |
|
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.
Pssm-ID: 460159 Cd Length: 128 Bit Score: 73.88 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 4 RIARLQQTFEELKIDAFLVSSEANLHYLTGMADMAGdGYLLVLADDAYLITDA-RYQTAFAGQYDDEHLVITRDY---LG 79
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGFTGSRG-LLLLVTADGALLLVDAlEYERAAAESAPDFDVVPYRDYealAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655161503 80 AVCQLIATTQTgvMGFEDD-LPYVAYSYLDENL-VSDLVALPTVVDTLRI 127
Cdd:pfam01321 80 LLKELGAGGKR--VGFEADaLTVAFYEALKEALpGAELVDVSGLIERLRM 127
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
127-347 |
8.00e-16 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 76.03 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 127 ITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKA-------------SFTTIVVggaraa 193
Cdd:PRK12896 9 EIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSpegyygfpgstciSVNEEVA------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 194 lpHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYL 273
Cdd:PRK12896 83 --HGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 274 TKAGYG--EAFnhgMGHGIGLAIHEAPLI-------SKNTanRLVANSVVTVEPgvyFPGLGG--MRIEDD--------- 333
Cdd:PRK12896 161 KKNGYSvvRDL---TGHGVGRSLHEEPSViltytdpLPNR--LLRPGMTLAVEP---FLNLGAkdAETLDDgwtvvtpdk 232
|
250 260
....*....|....*....|...
gi 1655161503 334 ---------VLVTATGHERLTKA 347
Cdd:PRK12896 233 slsaqfehtVVVTRDGPEILTDR 255
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
127-329 |
1.58e-13 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 69.68 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 127 ITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-----FTTIVVGGARAALPHGTAST 201
Cdd:PRK12897 3 TIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQkgyngYPYAICASVNDEMCHAFPAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 202 ALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEA 281
Cdd:PRK12897 83 VPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1655161503 282 FNHgMGHGIGLAIHEAPLI----SKNTANRLVANSVVTVEPGVYFpglgGMR 329
Cdd:PRK12897 163 RDF-TGHGIGKEIHEEPAIfhfgKQGQGPELQEGMVITIEPIVNV----GMR 209
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
129-346 |
4.90e-07 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 50.99 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 129 KSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-----FTTIVVGGARAALPHGTASTAL 203
Cdd:PLN03158 138 KTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATIAAGGYPSPlnyhfFPKSCCTSVNEVICHGIPDARK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 204 LEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYGEAFN 283
Cdd:PLN03158 218 LEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 284 HgMGHGIGLAIHEAPLISKNTANRLV----ANSVVTVEP----GVY----FP---------GLGGMRIEDDVLVTATGHE 342
Cdd:PLN03158 298 Y-CGHGIGELFHCAPNIPHYARNKAVgvmkAGQVFTIEPminaGVWrdrmWPdgwtavtadGKRSAQFEHTLLVTETGVE 376
|
....
gi 1655161503 343 RLTK 346
Cdd:PLN03158 377 VLTA 380
|
|
| COG5406 |
COG5406 |
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and ... |
128-300 |
7.06e-06 |
|
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and repair, Chromatin structure and dynamics];
Pssm-ID: 227693 [Multi-domain] Cd Length: 1001 Bit Score: 48.08 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 128 TKSADEIEKLRASAKLADAGFQYVT---SIVRPGMREIDVSNLLD-----------AYMRSHGASKASF-------TTIV 186
Cdd:COG5406 170 TKDAEEIANCRASSAASSVLMRYFVkemEMLWDGAFKITHGKLSDlmesliddvefFQTKSLKLGDIDLdqlewcyTPII 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 187 VGGARAALPHGTASTALLEAGQMVTLDFGYFLDDYTSDMTRTFaLGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVD 266
Cdd:COG5406 250 QSGGSIDLTPSAFSFPMELTGDVVLLSIGIRYNGYCSNMSRTI-LTDPDSEQQKNYEFLYMLQKYILGLVRPGTDSGIIY 328
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655161503 267 AVGRDYLTKAG--YGEAFNHGMGHGIGLAIHEAPLI 300
Cdd:COG5406 329 SEAEKYISSNGpeLGPNFIYNVGLMIGIEFRSSQKP 364
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
127-345 |
7.14e-06 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 47.12 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 127 ITKSADEIEKLRASAKLADAGFQYVTSIVRPGMREIDVSNLLDAYMRSHGASKAS-------FTTIVVGGARAALPHGTA 199
Cdd:PRK12318 42 IIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPlnygsppFPKTICTSLNEVICHGIP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 200 STALLEAGQMVTLDFGYFLDDYTSDMTRTFALGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAGYg 279
Cdd:PRK12318 122 NDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGF- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 280 EAFNHGMGHGIGLAIHEAPLIS--KNTAN-RLVANSVVTVEP--------GVYFP----------GLGGMRIEDDVLVTA 338
Cdd:PRK12318 201 SVVDQFVGHGVGIKFHENPYVPhhRNSSKiPLAPGMIFTIEPminvgkkeGVIDPinhweartcdNQPSAQWEHTILITE 280
|
....*..
gi 1655161503 339 TGHERLT 345
Cdd:PRK12318 281 TGYEILT 287
|
|
| CDC68-like |
cd01091 |
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ... |
221-320 |
2.21e-05 |
|
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: 45.03 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655161503 221 YTSDMTRTFaLGEPDAKLKAAYQAVLTAQQLVVDQVHAGANSAEVDAVGRDYLTKAG--YGEAFNHGMGHGIGLAIHEAP 298
Cdd:cd01091 105 YCSNIARTF-LIDPTSEQQKNYNFLLALQEEILKELKPGAKLSDVYQKTLDYIKKKKpeLEPNFTKNLGFGIGLEFRESS 183
|
90 100
....*....|....*....|...
gi 1655161503 299 L-ISKNTANRLVANSVVTVEPGV 320
Cdd:cd01091 184 LiINAKNDRKLKKGMVFNLSIGF 206
|
|
| |
