|
Name |
Accession |
Description |
Interval |
E-value |
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
1-388 |
0e+00 |
|
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: 637.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 1 MSGEEEA--AELTIAEDLVVTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKIFKKEKEMKKGIAFPT 78
Cdd:TIGR00495 1 MSGKDEQqeQAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEKEMEKGIAFPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 79 SISVNNCVCHFSPLKSDQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKENPVSGRKADVIKAAHLCAEAALRLVK 158
Cdd:TIGR00495 81 CISVNNCVGHFSPLKSDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 159 PGNQNTQVTDAWNKIAHSFHCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAK 238
Cdd:TIGR00495 161 PGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDSQKKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 239 DAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDTMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQ 318
Cdd:TIGR00495 241 DADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPFTLRNFEDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 319 FKFTVLLMPNGPMRITSGPFEPELYKSEFEVQDGELKALLQSSASRKTQKKKKKKASKNAENATTGETAE 388
Cdd:TIGR00495 321 FKFTVLLMPNGPMRITSGEFEPDLYKSEMEVQDPEIKALLASPIKRKKQKKKAKKASKTGEAATEGETME 390
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
18-334 |
1.53e-122 |
|
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: 353.56 E-value: 1.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 18 VTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQD 97
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 98 YILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKENPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAHSF 177
Cdd:cd01089 81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 178 HCTPIEGMLSHQLKQhvidgektiiqnptdqqkkdhekaefevhevyavdvLVSSGEGKAKdagqrttiykrdpskqygl 257
Cdd:cd01089 161 GCTPVEGVLSHQLKR------------------------------------VVSSGEGKAK------------------- 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201877459 258 kmktsraffseverrfdtmpftlrafedekkarmgVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRIT 334
Cdd:cd01089 186 -----------------------------------LVECVKHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
42-329 |
1.17e-20 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 93.24 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 42 GASVLCLCEKGDAMIMEETGkifkkEKEMKKGIAFPTSISVNNCVCHFSPLKSDqDYILKDGDLVKIDLGVHVDGFIANV 121
Cdd:PTZ00053 182 GVKLIDICERIESKSRELIE-----ADGLKCGWAFPTGCSLNHCAAHYTPNTGD-KTVLTYDDVCKLDFGTHVNGRIIDC 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 122 AHSF--------VIDASKENPVSGrkadvIKAAHLCAeaalRLVKPGNQNTQVTDAW-----NKIahsFHCTPIEGMLSH 188
Cdd:PTZ00053 256 AFTVafnpkydpLLQATKDATNTG-----IKEAGIDV----RLSDIGAAIQEVIESYeveikGKT---YPIKSIRNLNGH 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 189 QLKQHVIDGEKTI-IQNPTDQQKkdhekaeFEVHEVYAVDVLVSSGEGKAKDAGQrTTIYKRDPSKQYG-LKMKTSRAFF 266
Cdd:PTZ00053 324 SIGPYIIHGGKSVpIVKGGENTR-------MEEGELFAIETFASTGRGYVNEDLE-CSHYMKDPGAEFVpLRLPKAKQLL 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201877459 267 SEVERRFDTMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 329
Cdd:PTZ00053 396 KHINTNFGTLAFCRRWLDRlgQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTC 460
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
25-174 |
2.90e-16 |
|
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: 76.90 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 25 GDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKifkkekemkKGIAFPTSI--SVNNCVCHFSPLksdqDYILKD 102
Cdd:pfam00557 7 ARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA---------RGPAFPPIVasGPNAAIPHYIPN----DRVLKP 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201877459 103 GDLVKIDLGVHVD-GFIANVAHSFVIDaskenPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIA 174
Cdd:pfam00557 74 GDLVLIDVGAEYDgGYCSDITRTFVVG-----KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVL 141
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
76-161 |
1.62e-13 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 69.65 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 76 FPTSI--SVNNCVCHFSPlksdQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAA 153
Cdd:COG0024 62 FPKSIctSVNEVVVHGIP----SDRVLKDGDIVNIDVGAILDGYHGDSARTFVV-----GEVSPEARRLVEVTEEALYAG 132
|
....*...
gi 1201877459 154 LRLVKPGN 161
Cdd:COG0024 133 IAAAKPGN 140
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
1-388 |
0e+00 |
|
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: 637.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 1 MSGEEEA--AELTIAEDLVVTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKIFKKEKEMKKGIAFPT 78
Cdd:TIGR00495 1 MSGKDEQqeQAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEKEMEKGIAFPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 79 SISVNNCVCHFSPLKSDQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKENPVSGRKADVIKAAHLCAEAALRLVK 158
Cdd:TIGR00495 81 CISVNNCVGHFSPLKSDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 159 PGNQNTQVTDAWNKIAHSFHCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAK 238
Cdd:TIGR00495 161 PGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDSQKKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 239 DAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDTMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQ 318
Cdd:TIGR00495 241 DADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPFTLRNFEDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 319 FKFTVLLMPNGPMRITSGPFEPELYKSEFEVQDGELKALLQSSASRKTQKKKKKKASKNAENATTGETAE 388
Cdd:TIGR00495 321 FKFTVLLMPNGPMRITSGEFEPDLYKSEMEVQDPEIKALLASPIKRKKQKKKAKKASKTGEAATEGETME 390
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
18-334 |
1.53e-122 |
|
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: 353.56 E-value: 1.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 18 VTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQD 97
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 98 YILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKENPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAHSF 177
Cdd:cd01089 81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 178 HCTPIEGMLSHQLKQhvidgektiiqnptdqqkkdhekaefevhevyavdvLVSSGEGKAKdagqrttiykrdpskqygl 257
Cdd:cd01089 161 GCTPVEGVLSHQLKR------------------------------------VVSSGEGKAK------------------- 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201877459 258 kmktsraffseverrfdtmpftlrafedekkarmgVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRIT 334
Cdd:cd01089 186 -----------------------------------LVECVKHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
20-329 |
1.21e-49 |
|
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: 168.97 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 20 KYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGkifkkekemkkGIAFPTSISVNNCVCHFSPLKSDqDYI 99
Cdd:cd01088 3 KYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA-----------GPAFPVNLSINECAAHYTPNAGD-DTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 100 LKDGDLVKIDLGVHVDGFIANVAhsFVIDaskenpVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAHSFHC 179
Cdd:cd01088 71 LKEGDVVKLDFGAHVDGYIADSA--FTVD------FDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 180 TPIEGMLSHQLKQHVIDGEKTIiqnPTDqqkKDHEKAEFEVHEVYAVDVLVSSGEGKAKDaGQRTTIYKRDPSKQYGLKM 259
Cdd:cd01088 143 KPIRNLTGHSIERYRLHAGKSI---PNV---KGGEGTRLEEGDVYAIEPFATTGKGYVHD-GPECSIYMLNRDKPLRLPR 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201877459 260 ktSRAFFSEVERRFDTMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 329
Cdd:cd01088 216 --ARKLLDVIYENFGTLPFARRWLDRlgETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDG 285
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
42-329 |
1.17e-20 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 93.24 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 42 GASVLCLCEKGDAMIMEETGkifkkEKEMKKGIAFPTSISVNNCVCHFSPLKSDqDYILKDGDLVKIDLGVHVDGFIANV 121
Cdd:PTZ00053 182 GVKLIDICERIESKSRELIE-----ADGLKCGWAFPTGCSLNHCAAHYTPNTGD-KTVLTYDDVCKLDFGTHVNGRIIDC 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 122 AHSF--------VIDASKENPVSGrkadvIKAAHLCAeaalRLVKPGNQNTQVTDAW-----NKIahsFHCTPIEGMLSH 188
Cdd:PTZ00053 256 AFTVafnpkydpLLQATKDATNTG-----IKEAGIDV----RLSDIGAAIQEVIESYeveikGKT---YPIKSIRNLNGH 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 189 QLKQHVIDGEKTI-IQNPTDQQKkdhekaeFEVHEVYAVDVLVSSGEGKAKDAGQrTTIYKRDPSKQYG-LKMKTSRAFF 266
Cdd:PTZ00053 324 SIGPYIIHGGKSVpIVKGGENTR-------MEEGELFAIETFASTGRGYVNEDLE-CSHYMKDPGAEFVpLRLPKAKQLL 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201877459 267 SEVERRFDTMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 329
Cdd:PTZ00053 396 KHINTNFGTLAFCRRWLDRlgQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTC 460
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
25-188 |
8.18e-17 |
|
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: 79.07 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 25 GDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKI-FKKEKemkkgiAFPTSI--SVNNCVCHFSPlksdQDYILK 101
Cdd:cd01086 8 GRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPaPLGYY------GFPKSIctSVNEVVCHGIP----DDRVLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 102 DGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAHSFHCTP 181
Cdd:cd01086 78 DGDIVNIDVGVELDGYHGDSARTFIV-----GEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSV 152
|
....*..
gi 1201877459 182 IEGMLSH 188
Cdd:cd01086 153 VREFGGH 159
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
25-174 |
2.90e-16 |
|
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: 76.90 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 25 GDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGKifkkekemkKGIAFPTSI--SVNNCVCHFSPLksdqDYILKD 102
Cdd:pfam00557 7 ARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA---------RGPAFPPIVasGPNAAIPHYIPN----DRVLKP 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201877459 103 GDLVKIDLGVHVD-GFIANVAHSFVIDaskenPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIA 174
Cdd:pfam00557 74 GDLVLIDVGAEYDgGYCSDITRTFVVG-----KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVL 141
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
18-181 |
2.04e-14 |
|
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: 71.72 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 18 VTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGkifkkekemkkGIAFPTSISVNN--CVCHFSPlksd 95
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGG-----------YPAGPTIVGSGArtALPHYRP---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 96 QDYILKDGDLVKIDLGVHVDGFIANVAHSFVIDaskenPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAH 175
Cdd:cd01066 66 DDRRLQEGDLVLVDLGGVYDGYHADLTRTFVIG-----EPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLE 140
|
....*.
gi 1201877459 176 SFHCTP 181
Cdd:cd01066 141 EHGLGP 146
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
76-188 |
2.17e-14 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 72.47 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 76 FPTSI--SVNNCVCHFSPlksdQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAA 153
Cdd:PRK05716 64 FPKSIctSVNEVVCHGIP----SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGV-----GEISPEDKRLCEVTKEALYLG 134
|
90 100 110
....*....|....*....|....*....|....*
gi 1201877459 154 LRLVKPGNQNTQVTDAWNKIAHSFHCTPIEGMLSH 188
Cdd:PRK05716 135 IAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGH 169
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
76-161 |
1.62e-13 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 69.65 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 76 FPTSI--SVNNCVCHFSPlksdQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAA 153
Cdd:COG0024 62 FPKSIctSVNEVVVHGIP----SDRVLKDGDIVNIDVGAILDGYHGDSARTFVV-----GEVSPEARRLVEVTEEALYAG 132
|
....*...
gi 1201877459 154 LRLVKPGN 161
Cdd:COG0024 133 IAAAKPGN 140
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
18-188 |
4.06e-12 |
|
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: 65.45 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 18 VTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAMIMEETGK-IFKKEKEMKKGIAfptsISVNNCVCHFSPlksdQ 96
Cdd:TIGR00500 9 IEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKpAFLGYYGFPGSVC----ISVNEVVIHGIP----D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 97 DYILKDGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKIAHS 176
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLV-----GKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEA 155
|
170
....*....|..
gi 1201877459 177 FHCTPIEGMLSH 188
Cdd:TIGR00500 156 KGFSVVREYCGH 167
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
6-188 |
1.33e-11 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 64.09 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 6 EAAELTIAEDLVVTKYKMGGDIANRVLRAVVEEANSGASVLCLCEKGDAmIMEETGKI--FKKEKemkkgiAFPTS--IS 81
Cdd:PRK12896 4 EGRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEK-RLEEHGAIpsPEGYY------GFPGStcIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 82 VNNCVCHFSPlkSDQdyILKDGDLVKIDLGVHVDGFIANVAHSFVIDaskenPVSGRKADVIKAAHLCAEAALRLVKPGN 161
Cdd:PRK12896 77 VNEEVAHGIP--GPR--VIKDGDLVNIDVSAYLDGYHGDTGITFAVG-----PVSEEAEKLCRVAEEALWAGIKQVKAGR 147
|
170 180
....*....|....*....|....*..
gi 1201877459 162 QNTQVTDAWNKIAHSFHCTPIEGMLSH 188
Cdd:PRK12896 148 PLNDIGRAIEDFAKKNGYSVVRDLTGH 174
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
76-188 |
1.77e-07 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 52.13 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 76 FPTSI--SVNNCVCHFSPlksdQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIdaskeNPVSGRKADVIKAAHLCAEAA 153
Cdd:PRK12318 104 FPKTIctSLNEVICHGIP----NDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMI-----GEVSEIKKKVCQASLECLNAA 174
|
90 100 110
....*....|....*....|....*....|....*
gi 1201877459 154 LRLVKPGNQNTQVTDAWNKIAHSFHCTPIEGMLSH 188
Cdd:PRK12318 175 IAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGH 209
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
20-173 |
4.76e-05 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 44.81 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 20 KYKMGGDIANRVLRAVVEEANSGASvlclcEKGDAMIMEETGKifkkeKEMKKGIAFPTSISV--NNCVCHFSPlksdQD 97
Cdd:COG0006 81 LMRKAARIADAAHEAALAALRPGVT-----EREVAAELEAAMR-----RRGAEGPSFDTIVASgeNAAIPHYTP----TD 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201877459 98 YILKDGDLVKIDLGVHVDGFIANVAHSFVIDaskenPVSGRKADVIKAAHLCAEAALRLVKPGNQNTQVTDAWNKI 173
Cdd:COG0006 147 RPLKPGDLVLIDAGAEYDGYTSDITRTVAVG-----EPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDV 217
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
77-190 |
6.51e-05 |
|
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: 44.10 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 77 PTSIS-VNNCVCHFSPLksdqDYILKDGDLVKIDLGVHVDGFIANVAHSFvidaskenPVSGRK----ADVIKAAHLCAE 151
Cdd:cd01087 50 YIVAAgSNAAILHYVHN----DQPLKDGDLVLIDAGAEYGGYASDITRTF--------PVNGKFtdeqRELYEAVLAAQK 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 1201877459 152 AALRLVKPGNQNTQVTDAWNKIAHsfhctpiEGMLSHQL 190
Cdd:cd01087 118 AAIAACKPGVSYEDIHLLAHRVLA-------EGLKELGI 149
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
89-169 |
2.95e-04 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 42.40 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 89 FSPLKSDQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKEnpVSGRKADVIKAAHlcaEAALRLVKPGNQNTQVTD 168
Cdd:PRK15173 159 FSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPE--ITRKIYQTIRTGH---EHMLSMVAPGVKMKDVFD 233
|
.
gi 1201877459 169 A 169
Cdd:PRK15173 234 S 234
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
89-169 |
4.08e-04 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 42.39 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 89 FSPLKSDQDYILKDGDLVKIDLGVHVDGFIANVAHSFVIDASKEnpVSGRKADVIKAAHlcaEAALRLVKPGNQNTQVTD 168
Cdd:PRK14575 242 FSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPE--ITRKIYQTIRTGH---EHMLSMVAPGVKMKDVFD 316
|
.
gi 1201877459 169 A 169
Cdd:PRK14575 317 S 317
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
83-169 |
3.27e-03 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 39.32 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 83 NNCVCHFSPLKSDqdyiLKDGDLVKIDLGVHVDGFIANVAHSFvidaskenPVSGRKA-------DVIKAAhlcAEAALR 155
Cdd:PRK10879 236 NGCILHYTENESE----MRDGDLVLIDAGCEYKGYAGDITRTF--------PVNGKFTpaqreiyDIVLES---LETSLR 300
|
90
....*....|....
gi 1201877459 156 LVKPGNQNTQVTDA 169
Cdd:PRK10879 301 LYRPGTSIREVTGE 314
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
67-160 |
8.83e-03 |
|
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: 37.10 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201877459 67 EKEMKK----GIAFPTSIS--VNNCVCHFSPlkSDQdyILKDGDLVKIDLGVHVDGFIANVAHSFVI-DASKENpvsgRK 139
Cdd:cd01092 36 EYFMRKlgaeGPSFDTIVAsgPNSALPHGVP--SDR--KIEEGDLVLIDFGAIYDGYCSDITRTVAVgEPSDEL----KE 107
|
90 100
....*....|....*....|..
gi 1201877459 140 A-DVIKAAHlcaEAALRLVKPG 160
Cdd:cd01092 108 IyEIVLEAQ---QAAIKAVKPG 126
|
|
|