|
Name |
Accession |
Description |
Interval |
E-value |
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
26-411 |
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: 658.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 26 MSGEDEQQEQ--TIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDSMIMEETGKIFKKEKEMKKGIAFPT 103
Cdd:TIGR00495 1 MSGKDEQQEQaySLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEKEMEKGIAFPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 104 SISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDVVQGTQVTGRKADVIKAAHLCAEAALRLVK 183
Cdd:TIGR00495 81 CISVNNCVGHFSPLKSDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 184 PGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAK 263
Cdd:TIGR00495 161 PGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDSQKKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 264 DAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQ 343
Cdd:TIGR00495 241 DADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPFTLRNFEDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQ 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076552070 344 FKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTAENATSGET 411
Cdd:TIGR00495 321 FKFTVLLMPNGPMRITSGEFEPDLYKSEMEVQDPEIKALLASPIKRKKQKKKAKKASKTGEAATEGET 388
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
43-359 |
1.03e-115 |
|
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: 353.94 E-value: 1.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 43 VTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDSMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQD 122
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 123 YILKEGDLVKIDLGVHVDGFIANVAHTFVVDVVQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSF 202
Cdd:cd01089 81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 203 NCTPIEGMLSHQLKQhvidgektiiqnptdqqkkdhekaefevhevyavdvLVSSGEGKAKdagqrttiykrdpskqygl 282
Cdd:cd01089 161 GCTPVEGVLSHQLKR------------------------------------VVSSGEGKAK------------------- 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076552070 283 kmktsraffseverrfdampftlrafedekkarmgVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRIT 359
Cdd:cd01089 186 -----------------------------------LVECVKHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
77-354 |
1.38e-20 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 96.32 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 77 GDSMImEETGKIFKKEKEM------KKGIAFPTSISVNNCVCHFSPLKSDqDYILKEGDLVKIDLGVHVDGFIANVAHTF 150
Cdd:PTZ00053 182 GVKLI-DICERIESKSRELieadglKCGWAFPTGCSLNHCAAHYTPNTGD-KTVLTYDDVCKLDFGTHVNGRIIDCAFTV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 151 VVD-----VVQGTQ---VTGrkadvIKAAHLCAeaalRLVKPGNQNTQVTEAW-----NKVahsFNCTPIEGMLSHQLKQ 217
Cdd:PTZ00053 260 AFNpkydpLLQATKdatNTG-----IKEAGIDV----RLSDIGAAIQEVIESYeveikGKT---YPIKSIRNLNGHSIGP 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 218 HVIDGEKTI-IQNPTDQQKkdhekaeFEVHEVYAVDVLVSSGEGKAKDAGQrTTIYKRDPSKQYG-LKMKTSRAFFSEVE 295
Cdd:PTZ00053 328 YIIHGGKSVpIVKGGENTR-------MEEGELFAIETFASTGRGYVNEDLE-CSHYMKDPGAEFVpLRLPKAKQLLKHIN 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076552070 296 RRFDAMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 354
Cdd:PTZ00053 400 TNFGTLAFCRRWLDRlgQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTC 460
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
89-199 |
2.78e-14 |
|
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: 72.66 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 89 FKKEKEMKKGIAFPTSI--SVNNCVCHFSPLksdqDYILKEGDLVKIDLGVHVD-GFIANVAHTFVVDvvqgtQVTGRKA 165
Cdd:pfam00557 37 ARLRRGGARGPAFPPIVasGPNAAIPHYIPN----DRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG-----KPSPEQR 107
|
90 100 110
....*....|....*....|....*....|....
gi 2076552070 166 DVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVA 199
Cdd:pfam00557 108 ELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVL 141
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
101-213 |
3.04e-14 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 73.50 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTSI--SVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVdvvqGTqVTGRKADVIKAAHLCAEAA 178
Cdd:COG0024 62 FPKSIctSVNEVVVHGIP----SDRVLKDGDIVNIDVGAILDGYHGDSARTFVV----GE-VSPEARRLVEVTEEALYAG 132
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:COG0024 133 IAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGH 167
|
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
669-693 |
6.31e-05 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 40.69 E-value: 6.31e-05
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
675-693 |
1.13e-04 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 39.71 E-value: 1.13e-04
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
575-597 |
1.67e-04 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 39.53 E-value: 1.67e-04
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
577-595 |
1.11e-03 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 37.01 E-value: 1.11e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
26-411 |
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: 658.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 26 MSGEDEQQEQ--TIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDSMIMEETGKIFKKEKEMKKGIAFPT 103
Cdd:TIGR00495 1 MSGKDEQQEQaySLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEKEMEKGIAFPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 104 SISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDVVQGTQVTGRKADVIKAAHLCAEAALRLVK 183
Cdd:TIGR00495 81 CISVNNCVGHFSPLKSDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 184 PGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAK 263
Cdd:TIGR00495 161 PGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDSQKKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 264 DAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQ 343
Cdd:TIGR00495 241 DADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPFTLRNFEDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQ 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076552070 344 FKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTAENATSGET 411
Cdd:TIGR00495 321 FKFTVLLMPNGPMRITSGEFEPDLYKSEMEVQDPEIKALLASPIKRKKQKKKAKKASKTGEAATEGET 388
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
43-359 |
1.03e-115 |
|
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: 353.94 E-value: 1.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 43 VTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDSMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQD 122
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 123 YILKEGDLVKIDLGVHVDGFIANVAHTFVVDVVQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSF 202
Cdd:cd01089 81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 203 NCTPIEGMLSHQLKQhvidgektiiqnptdqqkkdhekaefevhevyavdvLVSSGEGKAKdagqrttiykrdpskqygl 282
Cdd:cd01089 161 GCTPVEGVLSHQLKR------------------------------------VVSSGEGKAK------------------- 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076552070 283 kmktsraffseverrfdampftlrafedekkarmgVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRIT 359
Cdd:cd01089 186 -----------------------------------LVECVKHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
45-354 |
3.71e-44 |
|
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: 161.65 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 45 KYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDSMIMEETGkifkkekemkkGIAFPTSISVNNCVCHFSPLKSDqDYI 124
Cdd:cd01088 3 KYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA-----------GPAFPVNLSINECAAHYTPNAGD-DTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 125 LKEGDLVKIDLGVHVDGFIANVAhtFVVDVVQGTQvtgrkaDVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNC 204
Cdd:cd01088 71 LKEGDVVKLDFGAHVDGYIADSA--FTVDFDPKYD------DLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 205 TPIEGMLSHQLKQHVIDGEKTIiqnPTDqqkKDHEKAEFEVHEVYAVDVLVSSGEGKAKDaGQRTTIYKRDPSKQYGLKM 284
Cdd:cd01088 143 KPIRNLTGHSIERYRLHAGKSI---PNV---KGGEGTRLEEGDVYAIEPFATTGKGYVHD-GPECSIYMLNRDKPLRLPR 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076552070 285 ktSRAFFSEVERRFDAMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 354
Cdd:cd01088 216 --ARKLLDVIYENFGTLPFARRWLDRlgETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDG 285
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
77-354 |
1.38e-20 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 96.32 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 77 GDSMImEETGKIFKKEKEM------KKGIAFPTSISVNNCVCHFSPLKSDqDYILKEGDLVKIDLGVHVDGFIANVAHTF 150
Cdd:PTZ00053 182 GVKLI-DICERIESKSRELieadglKCGWAFPTGCSLNHCAAHYTPNTGD-KTVLTYDDVCKLDFGTHVNGRIIDCAFTV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 151 VVD-----VVQGTQ---VTGrkadvIKAAHLCAeaalRLVKPGNQNTQVTEAW-----NKVahsFNCTPIEGMLSHQLKQ 217
Cdd:PTZ00053 260 AFNpkydpLLQATKdatNTG-----IKEAGIDV----RLSDIGAAIQEVIESYeveikGKT---YPIKSIRNLNGHSIGP 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 218 HVIDGEKTI-IQNPTDQQKkdhekaeFEVHEVYAVDVLVSSGEGKAKDAGQrTTIYKRDPSKQYG-LKMKTSRAFFSEVE 295
Cdd:PTZ00053 328 YIIHGGKSVpIVKGGENTR-------MEEGELFAIETFASTGRGYVNEDLE-CSHYMKDPGAEFVpLRLPKAKQLLKHIN 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076552070 296 RRFDAMPFTLRAFED--EKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNG 354
Cdd:PTZ00053 400 TNFGTLAFCRRWLDRlgQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTC 460
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
101-213 |
4.55e-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: 81.77 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTSI--SVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVdvvqGTqVTGRKADVIKAAHLCAEAA 178
Cdd:cd01086 54 FPKSIctSVNEVVCHGIP----DDRVLKDGDIVNIDVGVELDGYHGDSARTFIV----GE-VSEEAKKLVEVTEEALYKG 124
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:cd01086 125 IEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGH 159
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
101-213 |
4.02e-16 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 79.02 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTSI--SVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVdvvqGTqVTGRKADVIKAAHLCAEAA 178
Cdd:PRK05716 64 FPKSIctSVNEVVCHGIP----SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGV----GE-ISPEDKRLCEVTKEALYLG 134
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:PRK05716 135 IAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGH 169
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
43-206 |
2.44e-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: 72.87 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 43 VTKYKMGGDIANRVLRSLVEAsssgvsvlslCEKGDSMImEETGKIFKKEKEMKKGIAFPTSISVNN--CVCHFSPlksd 120
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEA----------IRPGVTEA-EVAAAIEQALRAAGGYPAGPTIVGSGArtALPHYRP---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 121 QDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvqgtQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAH 200
Cdd:cd01066 66 DDRRLQEGDLVLVDLGGVYDGYHADLTRTFVIG-----EPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLE 140
|
....*.
gi 2076552070 201 SFNCTP 206
Cdd:cd01066 141 EHGLGP 146
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
89-199 |
2.78e-14 |
|
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: 72.66 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 89 FKKEKEMKKGIAFPTSI--SVNNCVCHFSPLksdqDYILKEGDLVKIDLGVHVD-GFIANVAHTFVVDvvqgtQVTGRKA 165
Cdd:pfam00557 37 ARLRRGGARGPAFPPIVasGPNAAIPHYIPN----DRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG-----KPSPEQR 107
|
90 100 110
....*....|....*....|....*....|....
gi 2076552070 166 DVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVA 199
Cdd:pfam00557 108 ELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVL 141
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
101-213 |
3.04e-14 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 73.50 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTSI--SVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVdvvqGTqVTGRKADVIKAAHLCAEAA 178
Cdd:COG0024 62 FPKSIctSVNEVVVHGIP----SDRVLKDGDIVNIDVGAILDGYHGDSARTFVV----GE-VSPEARRLVEVTEEALYAG 132
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:COG0024 133 IAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGH 167
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
101-213 |
1.18e-11 |
|
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: 65.83 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTS--ISVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvqgtQVTGRKADVIKAAHLCAEAA 178
Cdd:TIGR00500 62 FPGSvcISVNEVVIHGIP----DKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVG-----KISPEAEKLLECTEESLYKA 132
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:TIGR00500 133 IEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGH 167
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
31-213 |
3.52e-10 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 61.78 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 31 EQQEQTIAEDLVVTKYKMGGDIANRVLR---SLVEASSSGVSVLSLCEKgdsmIMEETGKI--FKKEKemkkgiAFPTS- 104
Cdd:PRK12896 4 EGRGMEIKSPRELEKMRKIGRIVATALKemgKAVEPGMTTKELDRIAEK----RLEEHGAIpsPEGYY------GFPGSt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 105 -ISVNNCVCHFSPlkSDQdyILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvqgtQVTGRKADVIKAAHLCAEAALRLVK 183
Cdd:PRK12896 74 cISVNEEVAHGIP--GPR--VIKDGDLVNIDVSAYLDGYHGDTGITFAVG-----PVSEEAEKLCRVAEEALWAGIKQVK 144
|
170 180 190
....*....|....*....|....*....|
gi 2076552070 184 PGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:PRK12896 145 AGRPLNDIGRAIEDFAKKNGYSVVRDLTGH 174
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
101-213 |
2.30e-07 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 53.67 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 101 FPTSI--SVNNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHtfvvdVVQGTQVTGRKADVIKAAHLCAEAA 178
Cdd:PRK12318 104 FPKTIctSLNEVICHGIP----NDIPLKNGDIMNIDVSCIVDGYYGDCSR-----MVMIGEVSEIKKKVCQASLECLNAA 174
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 179 LRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSH 213
Cdd:PRK12318 175 IAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGH 209
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
92-198 |
5.82e-06 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 49.43 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 92 EKEMKK----GIAFPTSISV--NNCVCHFSPlksdQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDVVQGTQvtgRKA 165
Cdd:COG0006 114 EAAMRRrgaeGPSFDTIVASgeNAAIPHYTP----TDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQ---REI 186
|
90 100 110
....*....|....*....|....*....|....
gi 2076552070 166 -DVIKAAHlcaEAALRLVKPGNQNTQVTEAWNKV 198
Cdd:COG0006 187 yEAVLEAQ---EAAIAALKPGVTGGEVDAAARDV 217
|
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
669-693 |
6.31e-05 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 40.69 E-value: 6.31e-05
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
675-693 |
1.13e-04 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 39.71 E-value: 1.13e-04
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
102-215 |
1.62e-04 |
|
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: 44.49 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 102 PTSIS-VNNCVCHFSPLksdqDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvqGtQVTGRKADVIKAAHLCAEAALR 180
Cdd:cd01087 50 YIVAAgSNAAILHYVHN----DQPLKDGDLVLIDAGAEYGGYASDITRTFPVN---G-KFTDEQRELYEAVLAAQKAAIA 121
|
90 100 110
....*....|....*....|....*....|....*
gi 2076552070 181 LVKPGNQNTQVTEAWNKVAHsfnctpiEGMLSHQL 215
Cdd:cd01087 122 ACKPGVSYEDIHLLAHRVLA-------EGLKELGI 149
|
|
| ZnF_C3H1 |
smart00356 |
zinc finger; |
575-597 |
1.67e-04 |
|
zinc finger;
Pssm-ID: 214632 [Multi-domain] Cd Length: 27 Bit Score: 39.53 E-value: 1.67e-04
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
92-185 |
4.13e-04 |
|
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: 42.50 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076552070 92 EKEMKK----GIAFPTSIS--VNNCVCHFSPlkSDQdyILKEGDLVKIDLGVHVDGFIANVAHTFVVdvvqgtqvtGRKA 165
Cdd:cd01092 36 EYFMRKlgaeGPSFDTIVAsgPNSALPHGVP--SDR--KIEEGDLVLIDFGAIYDGYCSDITRTVAV---------GEPS 102
|
90 100
....*....|....*....|....
gi 2076552070 166 DVIKAAH---LCA-EAALRLVKPG 185
Cdd:cd01092 103 DELKEIYeivLEAqQAAIKAVKPG 126
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
114-185 |
4.97e-04 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 43.55 E-value: 4.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076552070 114 FSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvQGTQVTGRKADVIKAAHlcaEAALRLVKPG 185
Cdd:PRK15173 159 FSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVG--EPPEITRKIYQTIRTGH---EHMLSMVAPG 225
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
114-185 |
7.17e-04 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 43.16 E-value: 7.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076552070 114 FSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDvvQGTQVTGRKADVIKAAHlcaEAALRLVKPG 185
Cdd:PRK14575 242 FSPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVG--EPPEITRKIYQTIRTGH---EHMLSMVAPG 308
|
|
| zf_CCCH_4 |
pfam18345 |
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ... |
577-595 |
1.11e-03 |
|
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.
Pssm-ID: 465719 [Multi-domain] Cd Length: 19 Bit Score: 37.01 E-value: 1.11e-03
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
673-695 |
1.54e-03 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 36.79 E-value: 1.54e-03
|
| zf-CCCH_4 |
pfam18044 |
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ... |
673-693 |
9.98e-03 |
|
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.
Pssm-ID: 465626 Cd Length: 22 Bit Score: 34.49 E-value: 9.98e-03
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