|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
50-223 |
5.63e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 152.03 E-value: 5.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIySREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDC 129
Cdd:COG0666 90 LLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 130 VYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSADAQAV 209
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
170
....*....|....
gi 2785094811 210 QVSSSARRPAHKKK 223
Cdd:COG0666 249 DKDGLTALLLAAAA 262
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
50-208 |
9.71e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 9.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIYSREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDC 129
Cdd:COG0666 56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2785094811 130 VYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSADAQA 208
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
50-208 |
6.04e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 125.84 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIysrEHH--VDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNT 127
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLL---EAGadVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 128 DCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSADAQ 207
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
.
gi 2785094811 208 A 208
Cdd:COG0666 280 A 280
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
78-205 |
1.81e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.82 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASR 157
Cdd:COG0666 51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2785094811 158 GNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSAD 205
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
85-176 |
5.49e-25 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 99.42 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 85 LHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHnANPNLTDfHGNTAFHHAASRGNIKIVK 164
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 2785094811 165 LLLKYNVDFEAK 176
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
50-184 |
8.16e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 93.48 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIysrEH--HVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNT 127
Cdd:COG0666 156 PLHLAAANGNLEIVKLLL---EAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2785094811 128 DCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPL 184
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
118-205 |
5.06e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 118 LIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYnVDFEAKTkYGLTPLQLATYENHTEMIK 197
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*...
gi 2785094811 198 FLESKSAD 205
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
74-220 |
1.90e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 88.87 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 74 VDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHH 153
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2785094811 154 AASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSADAQAVQVSSsarrPAH 220
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGST----PLH 259
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
85-205 |
6.32e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 85.01 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 85 LHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVK 164
Cdd:COG0666 25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2785094811 165 LLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSAD 205
Cdd:COG0666 105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
51-144 |
2.63e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 51 LQRAASVGDLVTTESMIYSrEHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNsNINIQDDeGCTPLIKAVQCQNTDCV 130
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 2785094811 131 YILLRHNANPNLTD 144
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
67-205 |
1.31e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 82.79 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 67 IYSREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPL-----IKAVQCQNTDCVYILLRHNANPN 141
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2785094811 142 LTDFHGNTAFHHAASR--GNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENH--TEMIKFLESKSAD 205
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
55-209 |
1.70e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 82.41 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 55 ASVGDLVTTESMIYSREHHVDEYDRRGRTSLHYACVH--NHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDC--- 129
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkil 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 130 ---------------VYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTE 194
Cdd:PHA03100 160 kllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
170
....*....|....*
gi 2785094811 195 MIKFLESKSADAQAV 209
Cdd:PHA03100 240 IFKLLLNNGPSIKTI 254
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
80-209 |
5.72e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.00 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 80 RGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASR-G 158
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2785094811 159 NIKIVKLLLKYNVDFEAK-TKYGLTPLQLATYENhtEMIKFLESKSADAQAV 209
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSL 296
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
78-226 |
6.07e-15 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 79.14 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLR--HNANPNLtdfhGNTAFHHAA 155
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHA----AGDLLCTAA 630
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 156 SRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFLESKSADAQAVQV-----SSSARRPAHKKKVKH 226
Cdd:PLN03192 631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdddfsPTELRELLQKRELGH 706
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
47-264 |
6.79e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.92 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 47 PVGPLQRAASVGDLVTTESMIySREHHVDEYDRRGRTSLHYACVH-----------------------------NHPDV- 96
Cdd:PHA02878 37 PFIPLHQAVEARNLDVVKSLL-TRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafNNRNVe 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 97 ----------------------------------VTLLLEYNSNINIQD-DEGCTPLIKAVQCQNTDCVYILLRHNANPN 141
Cdd:PHA02878 116 ifkiiltnrykniqtidlvyidkkskddiieaeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 142 LTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLAT-YENHTEMIKFLESKSADaqaVQVSSSARrpah 220
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVD---VNAKSYIL---- 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2785094811 221 kkkvkhvrfnkevfvfnNERPLSRRVRSPRQLKSILKTSIQHNS 264
Cdd:PHA02878 269 -----------------GLTALHSSIKSERKLKLLLEYGADINS 295
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
71-209 |
1.69e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 71 EHHVDEYdrrGRTSLHYaCVHNH----PDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNT-DCVYILLRHNANPNLTDF 145
Cdd:PHA03095 40 VNFRGEY---GKTPLHL-YLHYSsekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDK 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2785094811 146 HGNTAFHHAASRGNI--KIVKLLLKYNVDFEAKTKYGLTPLQlATYENHT---EMIKFLESKSADAQAV 209
Cdd:PHA03095 116 VGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADVYAV 183
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
50-209 |
3.75e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.95 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIYSREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDC 129
Cdd:PHA02875 71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 130 VYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYG-LTPLQLATYENHTEMIKFLESKSADAQA 208
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
|
.
gi 2785094811 209 V 209
Cdd:PHA02875 231 M 231
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
133-187 |
4.52e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 61.21 E-value: 4.52e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 133 LLRH-NANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLA 187
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-201 |
5.86e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 65.43 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 74 VDEYDRRGRTSLH-YACVHN-HPDVVTLLLEYNSNINIQDDEGCTPLikAVQCQNTDC----VYILLRHNANPNLTDFHG 147
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRF 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2785094811 148 NTAFHHAA--SRGNIKIVKLLLKYNVDFEAKTKYGLTPLQ-LATYEN--HTEMIKFLES 201
Cdd:PHA03095 188 RSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSSckRSLVLPLLIA 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
81-134 |
6.14e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 6.14e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2785094811 81 GRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILL 134
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
95-209 |
2.58e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.51 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 95 DVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDC---VYILLRHNANPNLTDFHGNTAFHHAASRGN-IKIVKLLLKYN 170
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2785094811 171 VDFEAKTKYGLTPLQ--LATYENHTEMIKFLESKSADAQAV 209
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNAL 148
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
82-205 |
4.15e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.70 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 82 RTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIK 161
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2785094811 162 IVKLLLKYN--VDfEAKTKYGLTPLQLATYENHTEMIKFLESKSAD 205
Cdd:PHA02875 83 AVEELLDLGkfAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
147-199 |
5.66e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 5.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2785094811 147 GNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFL 199
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
92-179 |
6.52e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.99 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 92 NHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNV 171
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
....*...
gi 2785094811 172 DFEAKTKY 179
Cdd:PHA03100 250 SIKTIIET 257
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
99-154 |
1.58e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 54.27 E-value: 1.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 99 LLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHA 154
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
78-121 |
1.50e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.58 E-value: 1.50e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKA 121
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
50-172 |
2.96e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.90 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIySREHHVDEYDRRGRTSLHYACVHNHpDVVTLLLEyNSNINIQDDEGCTPLIKAVQ--CqNT 127
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLI-DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINppC-DI 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2785094811 128 DCVYILLRHNANPNLTDFHG----NTAFHHAASRGNIK--IVKLLLKYNVD 172
Cdd:PHA02874 269 DIIDILLYHKADISIKDNKGenpiDTAFKYINKDPVIKdiIANAVLIKEAD 319
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
59-208 |
3.17e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.00 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 59 DLVTTESMIYSREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNA 138
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 139 NPNLTDF-----------------------------HGNTAFHHAASRGNI-KIVKLLLKYNVDFEAKTKYGLTPLQLAT 188
Cdd:PHA02876 236 NINKNDLsllkairnedletslllydagfsvnsiddCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180
....*....|....*....|.
gi 2785094811 189 YENH-TEMIKFLESKSADAQA 208
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNA 336
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
50-111 |
4.48e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 4.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2785094811 50 PLQRAASVGDLVTTESMIysREHHVDEYDRrGRTSLHYACVHNHPDVVTLLLEYNSNINIQD 111
Cdd:pfam12796 33 ALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
50-211 |
8.08e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.84 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIYSREHHVDEYDRRGRTSLhYACVHNHPDV--VTLLLEYNSNINIQDDEGCTPLIKAVQC-QN 126
Cdd:PHA02876 276 PLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPL-YLMAKNGYDTenIRTLIMLGADVNAADRLYITPLHQASTLdRN 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 127 TDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEA------------------------------- 175
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAlsqkigtalhfalcgtnpymsvktlidrgan 434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2785094811 176 ---KTKYGLTPLQLATYEN-HTEMIKFLESKSADAQAVQV 211
Cdd:PHA02876 435 vnsKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
51-197 |
1.24e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.97 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 51 LQRAASVGDLVTTEsMIYSREHHVDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCV 130
Cdd:PHA02874 128 LHYAIKKGDLESIK-MLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 131 YILLRH-------------------------------NANPNLTDFHGNTAFHHAASRG-NIKIVKLLLKYNVDFEAKTK 178
Cdd:PHA02874 207 KLLIDHgnhimnkckngftplhnaiihnrsaiellinNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDN 286
|
170 180
....*....|....*....|
gi 2785094811 179 YGLTPLQLA-TYENHTEMIK 197
Cdd:PHA02874 287 KGENPIDTAfKYINKDPVIK 306
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
85-191 |
1.71e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 52.51 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 85 LHYACVHN---HPDVVTLLLEYNSNINIQDDEGCTPL-IKAVQCQ-NTDCVYILLRHNANPNLTDFHGNTAFH-HAASRG 158
Cdd:PHA02859 91 LHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLhMYMCNFNvRINVIKLLIDSGVSFLNKDFDNNNILYsYILFHS 170
|
90 100 110
....*....|....*....|....*....|...
gi 2785094811 159 NIKIVKLLLKYNVDFEAKTKYGLTPLQLATYEN 191
Cdd:PHA02859 171 DKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
50-201 |
2.50e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 54.25 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 50 PLQRAASVGDLVTTESMIYSreHHVDEYDR--RGRTSLHYACVHNHPDVVTLLLE-----YNSNINIQDDEGCTPLIKAV 122
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLKC--PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 123 QCQNTDCVYILLRHNA---NPNLTD-----------FHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQ-LA 187
Cdd:cd22192 98 VNQNLNLVRELIARGAdvvSPRATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLV 177
|
170
....*....|....*..
gi 2785094811 188 TYENHT---EMIKFLES 201
Cdd:cd22192 178 LQPNKTfacQMYDLILS 194
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
78-175 |
2.90e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 78 DRRGRTSLHYACVHN---HPDVVTLLLEyNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHA 154
Cdd:PHA03095 219 DMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
90 100
....*....|....*....|.
gi 2785094811 155 ASRGNIKIVKLLLKYNVDFEA 175
Cdd:PHA03095 298 VRNNNGRAVRAALAKNPSAET 318
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
93-204 |
5.25e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 93 HPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVD 172
Cdd:PHA02874 70 HPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
|
90 100 110
....*....|....*....|....*....|..
gi 2785094811 173 FEAKTKYGLTPLQLATYENHTEMIKFLESKSA 204
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
99-205 |
6.63e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 51.88 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 99 LLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTK 178
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100
....*....|....*....|....*..
gi 2785094811 179 YGLTPLQLATYENHTEMIKFLESKSAD 205
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGAD 112
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
146-175 |
1.88e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.89 E-value: 1.88e-06
10 20 30
....*....|....*....|....*....|
gi 2785094811 146 HGNTAFHHAASRGNIKIVKLLLKYNVDFEA 175
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
130-209 |
1.96e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 130 VYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLATYENHTEMIKFL-----ESKSA 204
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqCHFEL 177
|
....*
gi 2785094811 205 DAQAV 209
Cdd:PTZ00322 178 GANAK 182
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
80-112 |
1.97e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.97 E-value: 1.97e-06
10 20 30
....*....|....*....|....*....|....
gi 2785094811 80 RGRTSLHYACVH-NHPDVVTLLLEYNSNINIQDD 112
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
342-524 |
2.23e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 51.19 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 342 FHSVPSEAAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSlTAVEPAQTKSTIATdsLTAVEPAL 421
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEV-VVVETTHPEVIAAP--VTEQPQVI 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 422 TKSTKDAASLTAAEPAPTKsTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTA 501
Cdd:PRK10811 932 TESDVAVAQEVAEHAEPVV-EPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEAT 1010
|
170 180
....*....|....*....|....*....
gi 2785094811 502 VE------PMptksTTAadsltavePAPT 524
Cdd:PRK10811 1011 VEhnhataPM----TRA--------PAPE 1027
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
78-136 |
2.74e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 2.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRH 136
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
78-170 |
3.57e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 49.27 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEgcTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASR 157
Cdd:PHA02791 27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104
|
90
....*....|...
gi 2785094811 158 GNIKIVKLLLKYN 170
Cdd:PHA02791 105 GNMQTVKLFVKKN 117
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
80-109 |
3.70e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.12 E-value: 3.70e-06
10 20 30
....*....|....*....|....*....|
gi 2785094811 80 RGRTSLHYACVHNHPDVVTLLLEYNSNINI 109
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
89-199 |
3.84e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.96 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 89 CVHNhpDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLK 168
Cdd:PHA02874 101 CIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
|
90 100 110
....*....|....*....|....*....|.
gi 2785094811 169 YNVDFEAKTKYGLTPLQLATYENHTEMIKFL 199
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
82-197 |
4.00e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 49.21 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 82 RTSLHYACVHNH-PDVVTLLLEYNSNINIQ----DDEGCTPLIKAVQCQNTDCVYILLRHNANPN-LTDFHGNTAFHHAA 155
Cdd:PHA02884 33 IANILYSSIKFHyTDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISV 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2785094811 156 SRGNIKIVKLLLKYNVDFEAKTKYGLTPLQLAT---YENHTEMIK 197
Cdd:PHA02884 113 LHGCLKCLEILLSYGADINIQTNDMVTPIELALmicNNFLAFMIC 157
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
328-672 |
4.10e-06 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 49.96 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 328 ENTSATDEKTKMENFHSVPSEAAADVGPSTSTAdsldAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPA---- 403
Cdd:pfam17823 45 DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTS----AAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAaaas 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 404 QTKSTIATDSLTAVE--PALTKSTKDA----ASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTI 477
Cdd:pfam17823 121 SSPSSAAQSLPAAIAalPSEAFSAPRAaacrANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 478 AADS-LIAAEPAPT------------------KSTTAADSLTAVEPMPTKSTTAADSLTAVEPAPTKSTTAAASLTAAEP 538
Cdd:pfam17823 201 SAPAtLTPARGISTaatatghpaagtalaavgNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 539 APTKSTTAadGLTADEPAPTKSTTAadgltadepelsltyaadstvsgdSGPASHIgldyVVDLPLYKEStrykPHADPE 618
Cdd:pfam17823 281 SPAKHMPS--DTMARNPAAPMGAQA------------------------QGPIIQV----STDQPVHNTA----GEPTPS 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 619 PTPGSCTCYSLDSIQMTNLTLLISFSEEEIFYTASSDE--ESSFIPDIEEGLPATQ 672
Cdd:pfam17823 327 PSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPvlHTSMIPEVEATSPTTQ 382
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
146-175 |
4.42e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 43.79 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|
gi 2785094811 146 HGNTAFHHAASRGNIKIVKLLLKYNVDFEA 175
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PRK10118 |
PRK10118 |
flagellar hook length control protein FliK; |
340-523 |
6.52e-06 |
|
flagellar hook length control protein FliK;
Pssm-ID: 236652 [Multi-domain] Cd Length: 408 Bit Score: 49.09 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 340 ENFHSVPSEAAADVGPSTSTADSLdaaEPAQTKSTKEAASLTAVEPEPTKST----IAADS-LTAVEPAQTKSTIATDsl 414
Cdd:PRK10118 87 ANLLIPVDETLPVITDEQSLSSPL---TPALKTSALAALSKNAQKDEKADDLsdedLASLSaLFAMLPGQDNTTPVAD-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 415 tavEPALTKSTKDAASLTAAEPAP--TKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAAdsliaaEPAPTKS 492
Cdd:PRK10118 162 ---APSTVLPAEKPTLLTKDMPSApqDETHTLSSDEHEKGLTSAQLTTAQPDDAPGTPAQPLTPLAA------EAQAKAE 232
|
170 180 190
....*....|....*....|....*....|.
gi 2785094811 493 TTAADSLTAVEPMPTKSTTAADSLTAVePAP 523
Cdd:PRK10118 233 VISTPSPVTAAASPTITPHQTQPLPTA-AAP 262
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
96-204 |
9.54e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 48.97 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 96 VVTLLLEYNSNINIQDDEGCTPL---IKAVQCQNTDCVYILLRHNANPN-LTDFHGNTAFHHAASRGNIK--IVKLLLKY 169
Cdd:PHA02989 90 IVKLLLKFGADINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSF 169
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2785094811 170 NVD-FEAKTKYGLTPLQLatYENHT------EMIKFLESKSA 204
Cdd:PHA02989 170 GVNlFEKTSLYGLTPMNI--YLRNDidvisiKVIKYLIKKGV 209
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
345-590 |
1.31e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.69 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 345 VPSEAAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEPePTKSTIAADSLTAVEPAQTKSTIATDSLTAVEPALTKS 424
Cdd:PRK07003 386 RAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP-PAAPAPPATADRGDDAADGDAPVPAKANARASADSRCD 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 425 TKDAASLTAAEP--APTKSTNAAdslTAVEPVPTkSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTAV 502
Cdd:PRK07003 465 ERDAQPPADSGSasAPASDAPPD---AAFEPAPR-AAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAA 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 503 EPmPTKSTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTADEPELSLTYAADS 582
Cdd:PRK07003 541 AP-AARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAEQA 619
|
....*...
gi 2785094811 583 TVSGDSGP 590
Cdd:PRK07003 620 AESRGAPP 627
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
80-109 |
2.29e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.86 E-value: 2.29e-05
10 20 30
....*....|....*....|....*....|
gi 2785094811 80 RGRTSLHYACVHNHPDVVTLLLEYNSNINI 109
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
146-178 |
2.66e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.51 E-value: 2.66e-05
10 20 30
....*....|....*....|....*....|....
gi 2785094811 146 HGNTAFHHAASR-GNIKIVKLLLKYNVDFEAKTK 178
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
346-574 |
4.07e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.18 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 346 PSEAAADVGPSTSTADSLDAAEPAqtkstkeAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAVEPALTKST 425
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPA-------AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAAR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 426 KDAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAAdsltAVEPVPTKSTIAADSLIAAEPAP----TKSTTAADSLTA 501
Cdd:PRK12323 438 QASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAA----AAAAAPARAAPAAAPAPADDDPPpweeLPPEFASPAPAQ 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2785094811 502 VEPMPtksttaADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGL----TADEPEL 574
Cdd:PRK12323 514 PDAAP------AGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLpdmfDGDWPAL 584
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-171 |
4.75e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.56 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 74 VDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDfhgnTAFHH 153
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
90 100
....*....|....*....|.
gi 2785094811 154 AASRGNIKIV---KLLLKYNV 171
Cdd:PHA03095 326 ASVAGGDIPSdatRLCVAKVV 346
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
344-559 |
6.19e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 46.28 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 344 SVPSEAAADVGPSTSTADSLDAA----EPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAVEP 419
Cdd:COG3469 3 SVSTAASPTAGGASATAVTLLGAaataASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 420 ALTKSTKDAASLTAAEPAPTKSTNAADSltavePVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSL 499
Cdd:COG3469 83 TAAAAAATSTSATLVATSTASGANTGTS-----TVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 500 TAVEPMPTKSTTAADSLTAvePAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTK 559
Cdd:COG3469 158 TATGGTTTTSTTTTTTSAS--TTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKH 215
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
356-564 |
1.26e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.68 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 356 STSTADSLDAAEPAQTKSTKEAASLTAVEPEPT----KSTIAADSLTAvePAQTKSTIATDSLTAVEPALTKStkdAASL 431
Cdd:pfam05109 413 TTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTtglpSSTHVPTNLTA--PASTGPTVSTADVTSPTPAGTTS---GASP 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 432 TAAEPAPTKS---TNAADSLTAVEPVPTKSTNAADSLTAV-EPVP--TKSTIAADSLIAAEPAPT-KSTTAADSLTAVEP 504
Cdd:pfam05109 488 VTPSPSPRDNgteSKAPDMTSPTSAVTTPTPNATSPTPAVtTPTPnaTSPTLGKTSPTSAVTTPTpNATSPTPAVTTPTP 567
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2785094811 505 MPTKSTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAadGLTADEP---APTKSTTAA 564
Cdd:pfam05109 568 NATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTL--GGTSSTPvvtSPPKNATSA 628
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
95-205 |
1.41e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 45.21 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 95 DVVTLLLEYNSNINIQDDEGCTPL------IKAVQcQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRG---NIKIVKL 165
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLctilsnIKDYK-HMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2785094811 166 LLKYNVDFEAKTKYGLTPLQLATYENHT---EMIKFLESKSAD 205
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVD 173
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
325-472 |
2.74e-04 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 43.35 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 325 VWEENTSATDEKTKMENFHSVPSEAAADVGPST-------STADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSL 397
Cdd:PHA03255 23 IWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTnqsttltTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 398 TAVEPAQTKStiATDSLTAVEPALTKSTKDAASLTAAepAPTKSTNAadslTAVEPVPT-KSTNAADSLTAVEPVP 472
Cdd:PHA03255 103 TTKVTAQNIT--ATEAGTGTSTGVTSNVTTRSSSTTS--ATTRITNA----TTLAPTLSsKGTSNATKTTAELPTV 170
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
76-203 |
3.35e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 76 EYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQ----------DDEGC----TPLIKAVqCQNTDCVYILLRHNANPN 141
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAA-CTNQPEIVQLLMEKESTD 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2785094811 142 LT--DFHGNTAFHHAA-----SRGNIKIVK-----LLLKY-NVDFEA-KTKYGLTPLQLATYENHTEMIKFLESKS 203
Cdd:cd22194 215 ITsqDSRGNTVLHALVtvaedSKTQNDFVKrmydmILLKSeNKNLETiRNNEGLTPLQLAAKMGKAEILKYILSRE 290
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
426-566 |
4.00e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 426 KDAASLTAAEPAPTKS-TNAADSLTAVEPVPTKSTNAAdsltAVEPVPTKSTIAADSLIAAEPAPTKSTTAAdsltAVEP 504
Cdd:PRK14951 365 KPAAAAEAAAPAEKKTpARPEAAAPAAAPVAQAAAAPA----PAAAPAAAASAPAAPPAAAPPAPVAAPAAA----APAA 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2785094811 505 MPTKSTTAAdsltAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADG 566
Cdd:PRK14951 437 APAAAPAAV----ALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
344-489 |
4.46e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.70 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 344 SVPSEAAADVGPSTSTADSLDAAEPAQ-TKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQTKStiATDSLTAVEPALT 422
Cdd:PRK07994 369 EVPPQSAAPAASAQATAAPTAAVAPPQaPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQ--GATKAKKSEPAAA 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2785094811 423 KSTKDAAS----LTAAEPAPTKSTNAADSltaVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAP 489
Cdd:PRK07994 447 SRARPVNSalerLASVRPAPSALEKAPAK---KEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAA 514
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
460-581 |
4.77e-04 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 43.09 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 460 NAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTAVEPMPTKSTTAADSLTAVEPAPTksttaaasltAAEPA 539
Cdd:PRK10856 151 SAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQA----------NVDTA 220
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2785094811 540 PTKSTTAADGLTADEPAPTKSTTAADGlTADEPELSLTYAAD 581
Cdd:PRK10856 221 ATPAPAAPATPDGAAPLPTDQAGVSTP-AADPNALVMNFTAD 261
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
98-212 |
6.99e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.21 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 98 TLLLEYNSNINIQDDEGCTPLIKAVQcqNTDCVYILLrhNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKT 177
Cdd:cd22194 96 TCLMKALLNINENTKEIVRILLAFAE--ENGILDRFI--NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHA 171
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2785094811 178 K--------------YGLTPLQLATYENHTEMIKFLESKSADAQAVQVS 212
Cdd:cd22194 172 KgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
251-517 |
7.03e-04 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 42.87 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 251 QLKSILKTSIQHNSEAGMQLTGRSPwcVNVDNvSSTSSVKGesGRKIHIKPKKSqNSFRK-----------SGVY----- 314
Cdd:PRK13914 70 QVNEVAAAEKTEKSVSATWLNVRSG--AGVDN-SIITSIKG--GTKVTVETTES-NGWHKityndgktgfvNGKYltdkv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 315 VSSRVAPILEVWEENTS---ATDEKTKMENFHSVPSEAAADVGPSTSTADSLDaaEPAQTKSTKEAASLTAVEpepTKST 391
Cdd:PRK13914 144 TSTPVAPTQEVKKETTTqqaAPAAETKTEVKQTTQATTPAPKVAETKETPVVD--QNATTHAVKSGDTIWALS---VKYG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 392 IAADSLTAVEPAQTKSTIATDSLTAVEPALTKSTKdaASLTAAEPAPTKSTnaadsltavEPVPTKSTNAADSLTAVEPV 471
Cdd:PRK13914 219 VSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPK--AEVKTEAPAAEKQA---------APVVKENTNTNTATTEKKET 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2785094811 472 PT-KSTIAADSLIAAEPAPTKSTTAADSLTAVEPMPTKSTTAADSLT 517
Cdd:PRK13914 288 TTqQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPS 334
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
113-144 |
7.88e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 7.88e-04
10 20 30
....*....|....*....|....*....|...
gi 2785094811 113 EGCTPLIKAV-QCQNTDCVYILLRHNANPNLTD 144
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
365-580 |
8.43e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.91 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 365 AAEPAQTKSTKEAASLTAVEPEptkstiAADSLTAVEPAQTKSTIATDSLTAVEPALTKSTKDAASLTAAEPAPTKstna 444
Cdd:PRK07003 357 AFEPAVTGGGAPGGGVPARVAG------AVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 445 adsltAVEPVPTKSTNAADSlTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTAVEPMPTKSTTAADsltavEPAPT 524
Cdd:PRK07003 427 -----PAAPAPPATADRGDD-AADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF-----EPAPR 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2785094811 525 K-STTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGltADEPELSLTYAA 580
Cdd:PRK07003 496 AaAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPA--AAAPAARAGGAA 550
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
327-592 |
9.45e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 42.69 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 327 EENTSATDEKTKMENFHSVPSEAAADVGPST-STADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQT 405
Cdd:COG5271 448 EADSLADEEEEAEAELDTEEDTESAEEDADGdEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAAD 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 406 KSTIATDSLT-AVEPALTKSTKDAASLTAAEPAPTKSTNAADSLTAvEPVPTKSTNAADSlTAVEPVPTKSTIAADSLIA 484
Cdd:COG5271 528 PEDSDEDALEdETEGEENAPGSDQDADETDEPEATAEEDEPDEAEA-ETEDATENADADE-TEESADESEEAEASEDEAA 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 485 AEPAPTKSTTAADSLTAVEPMPTKSTTAADSLTAVEPAPTKsTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAA 564
Cdd:COG5271 606 EEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASE-AADEDADAETEAEASADESEEEAEDESETSSEDAEEDA 684
|
250 260 270
....*....|....*....|....*....|..
gi 2785094811 565 DGLTA----DEPELSLTYAADSTVSGDSGPAS 592
Cdd:COG5271 685 DAAAAeasdDEEETEEADEDAETASEEADAEE 716
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
346-625 |
9.47e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 346 PSEAAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAVE---PALT 422
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPaagPPRR 2782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 423 KSTKDAASLTAAEPAPTKSTNAADSlTAVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAA-----D 497
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADP-PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 498 SLTAVEPMPTKSTTAADSLTAV----EPAPTKSTTAAAS-LTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTADEP 572
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARPPVrrlaRPAVSRSTESFALpPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2785094811 573 ELSLTyAADSTVSGDSGPASHIGLDYVVDLPLYKESTRYKPHADPEPTPGSCT 625
Cdd:PHA03247 2942 PLAPT-TDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASST 2993
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
68-214 |
1.46e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 41.79 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 68 YSREHHVDEYDRR---GRTSLHYACVHNHP---DVVTLLLEYNsniniQDDEGCTPLIKAvqcQNTDCVYIllrhnanpn 141
Cdd:cd21882 10 CLRWYLTDSAYQRgatGKTCLHKAALNLNDgvnEAIMLLLEAA-----PDSGNPKELVNA---PCTDEFYQ--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 142 ltdfhGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTK-------------YGLTPLQLATYENHTEMIKFLESKSADAQA 208
Cdd:cd21882 73 -----GQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAA 147
|
....*.
gi 2785094811 209 VQVSSS 214
Cdd:cd21882 148 LEAQDS 153
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
416-591 |
1.65e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 416 AVEPALTKSTKDAASLTAAEP------APTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAAdsliAAEPAP 489
Cdd:PRK07003 357 AFEPAVTGGGAPGGGVPARVAgavpapGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP----PAAPAP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 490 TKSTTAADSlTAVEPMPTKSTTAADSLTAVEPAPtksttaaaslTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTA 569
Cdd:PRK07003 433 PATADRGDD-AADGDAPVPAKANARASADSRCDE----------RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSA 501
|
170 180
....*....|....*....|..
gi 2785094811 570 DEPELSLTYAADSTVSGDSGPA 591
Cdd:PRK07003 502 ATPAAVPDARAPAAASREDAPA 523
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
443-549 |
1.73e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 41.17 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 443 NAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTAVEPMPTKSTTAADSLTAVEPA 522
Cdd:PRK10856 151 SAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPAT 230
|
90 100 110
....*....|....*....|....*....|.
gi 2785094811 523 PTKSTtaaasltaaePAPTK----STTAADG 549
Cdd:PRK10856 231 PDGAA----------PLPTDqagvSTPAADP 251
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
349-498 |
1.82e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 349 AAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEpepTKSTIAADSLTAVEPAQTKSTIATDSltAVEPALTK--STK 426
Cdd:PRK13108 304 AAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAE---VTDEVAAESVVQVADRDGESTPAVEE--TSEADIEReqPGD 378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2785094811 427 DAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPV-----PTKSTIAADSLIAAEPAPTKSTTAADS 498
Cdd:PRK13108 379 LAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIpdpakPDELAVAGPGDDPAEPDGIRRQDDFSS 455
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
113-142 |
1.83e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|
gi 2785094811 113 EGCTPLIKAVQCQNTDCVYILLRHNANPNL 142
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
74-136 |
1.93e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 41.52 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2785094811 74 VDEYDRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQDDEGCTPLIKAV-QCQNTDCVYILLRH 136
Cdd:PHA02917 445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCH 508
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
350-516 |
2.06e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 41.33 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 350 AADVGPSTSTADSLD--AAEPAqtkstkeaASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLtavePALTKSTKD 427
Cdd:PRK12373 170 AAGKGPVVKPGPQIGryASEPA--------GGLTSLTEEAGKARYNASKALAEDIGDTVKRIDGTEV----PLLAPWQGD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 428 AASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSlTAVEPVPTKSTIAADSLiAAEPAPTKSTTAADSLT-AVEPMP 506
Cdd:PRK12373 238 AAPVPPSEAARPKSADAETNAALKTPATAPKAAAKNA-KAPEAQPVSGTAAAEPA-PKEAAKAAAAAAKPALEdKPRPLG 315
|
170
....*....|
gi 2785094811 507 TKSTTAADSL 516
Cdd:PRK12373 316 IARPGGADDL 325
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
400-565 |
2.08e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.56 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 400 VEPAQTKSTIATDSLTAVEPALTKSTKDAAslTAAEPAPTKSTNAADSLTAVEPVPTkstnAADSLTAVEPVPTKSTIAA 479
Cdd:PRK10811 847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVA--AAVEPVVSAPVVEAVAEVVEEPVVV----AEPQPEEVVVVETTHPEVI 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 480 DSLIAAEPAP-TKSTTAADSLTAVEPMPTksTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPT 558
Cdd:PRK10811 921 AAPVTEQPQViTESDVAVAQEVAEHAEPV--VEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
|
....*..
gi 2785094811 559 KSTTAAD 565
Cdd:PRK10811 999 PEVAPAQ 1005
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
345-550 |
2.21e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 345 VPSEAAADVGPSTSTadsldaAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAVEPALTKS 424
Cdd:PRK12323 382 VAQPAPAAAAPAAAA------PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 425 TKDAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPtkSTIAADSLIAAEPAPtksttaADSLTAVEP 504
Cdd:PRK12323 456 AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELP--PEFASPAPAQPDAAP------AGWVAESIP 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2785094811 505 MPTKSTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGL 550
Cdd:PRK12323 528 DPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
427-524 |
2.48e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 40.78 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 427 DAASL--TAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTKSTTAAdslTAVEP 504
Cdd:PRK10856 150 SSAELsqNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAA---TPAPA 226
|
90 100
....*....|....*....|
gi 2785094811 505 MPTKSTTAADSLTAVEPAPT 524
Cdd:PRK10856 227 APATPDGAAPLPTDQAGVST 246
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
348-586 |
2.52e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 41.25 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 348 EAAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSL----TAVEPAQTKSTIATDSLTAVEPALTK 423
Cdd:PRK14949 369 DDPAEISLPEGQTPSALAAAVQAPHANEPQFVNAAPAEKKTALTEQTTAQqqvqAANAEAVAEADASAEPADTVEQALDD 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 424 STKDAASLTaAEPA------------PTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPtkSTIAADSLIAAEPAPTK 491
Cdd:PRK14949 449 ESELLAALN-AEQAvilsqaqsqgfeASSSLDADNSAVPEQIDSTAEQSVVNPSVTDTQVD--DTSASNNSAADNTVDDN 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 492 StTAADSLTAVEPMPTKSTTAADSLTAVEP-APTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTAD 570
Cdd:PRK14949 526 Y-SAEDTLESNGLDEGDYAQDSAPLDAYQDdYVAFSSESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAA 604
|
250 260
....*....|....*....|.
gi 2785094811 571 EPE----LSLTYAA-DSTVSG 586
Cdd:PRK14949 605 SLAdddiLDAVLAArDSLLSD 625
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
338-547 |
2.60e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 338 KMENFHSVPSEAAADVGPSTSTAdSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQtkSTIATDSLTAV 417
Cdd:PRK07003 354 RMLAFEPAVTGGGAPGGGVPARV-AGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA--ATRAEAPPAAP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 418 EPAltkSTKDAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTkstiaADSLIAAEPAPtkstTAAD 497
Cdd:PRK07003 431 APP---ATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASD-----APPDAAFEPAP----RAAA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2785094811 498 SLTAVEPMPTKSTTAADSLTAVEPAPTKSTTAAASLtaaePAPTKSTTAA 547
Cdd:PRK07003 499 PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARP----PTPAAAAPAA 544
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
354-560 |
2.82e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 40.69 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 354 GPSTSTADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVE----------PAQTKSTIATDSLTAVE----- 418
Cdd:PRK10905 22 APSTSSSDQTASGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQdvslppisstPTQGQTPVATDGQQRVEvqgdl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 419 -PALTKSTKD-------AASLTAAEPA---PTKSTNAADSLTAVEPVPTKSTNAADSLTAV-EPVPTKSTIAADSLIAAE 486
Cdd:PRK10905 102 nNALTQPQNQqqlnnvaVNSTLPTEPAtvaPVRNGNASRQTAKTQTAERPATTRPARKQAViEPKKPQATAKTEPKPVAQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2785094811 487 PaPTKSTTAADSLTAVEPMPTkSTTAADSLTAVEPAPTksttaaasltaAEPAPTKSTTAADGLTADEPAPTKS 560
Cdd:PRK10905 182 T-PKRTEPAAPVASTKAPAAT-STPAPKETATTAPVQT-----------ASPAQTTATPAAGGKTAGNVGSLKS 242
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
348-621 |
2.85e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.07 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 348 EAAADVGPSTSTADSLDAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAV--EPAQTKSTIATD-SLTAVEPALTKS 424
Cdd:PLN03209 304 EVIAETTAPLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIeeEPPQPKAVVPRPlSPYTAYEDLKPP 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 425 TKDAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTiaadsliaaepAPTKSTTAADSL---TA 501
Cdd:PLN03209 384 TSPIPTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKT-----------RPLSPYARYEDLkppTS 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 502 VEPMPTKSTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTADEPELSLTYAAD 581
Cdd:PLN03209 453 PSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKV 532
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2785094811 582 STVSGDSGPASHIGLDYVVDLPLyKESTRY---KPHADPEPTP 621
Cdd:PLN03209 533 GNSAPPTALADEQHHAQPKPRPL-SPYTMYedlKPPTSPTPSP 574
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
97-178 |
2.86e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 97 VTLLLEYNSNINIQDDEGCTPLIKAVQCQNTDCVYILLRHNANPNLTDFHGNTAFHHAASRGNIKIVKLLLKYNV---DF 173
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfEL 177
|
....*
gi 2785094811 174 EAKTK 178
Cdd:PTZ00322 178 GANAK 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
344-617 |
3.31e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 344 SVPSEAAAdvgPSTSTADSLDAAEPAQTKSTKEAAslTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAV------ 417
Cdd:PHA03247 2590 DAPPQSAR---PRAPVDDRGDPRGPAPPSPLPPDT--HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvsrp 2664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 418 EPALTKSTKDAASLTAAEPAPTKSTNAADSLTAV------EPVPTKSTNAADSLTAVEPVPTKSTIAADSLIA--AEPAP 489
Cdd:PHA03247 2665 RRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAapAPPAV 2744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 490 TKSTTAADSLTAVEPMPTKSTTAADSLTAVEPAP----TKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAAD 565
Cdd:PHA03247 2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2785094811 566 GlTADEPELSLTYAADSTVSGDSGPASHIGLDYVVDLPLYKESTRYKPHADP 617
Cdd:PHA03247 2825 A-GPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
427-587 |
3.51e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 40.62 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 427 DAASLTAAEPAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPVPTKSTiAADSLIAAEPAPTKSTTAADSLTAVEPMP 506
Cdd:PRK07994 368 PEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPE-TTSQLLAARQQLQRAQGATKAKKSEPAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 507 TKSTTAADSLTAVEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAAdgLTADEPELSLTYAADSTVSG 586
Cdd:PRK07994 447 SRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKAL--EHEKTPELAAKLAAEAIERD 524
|
.
gi 2785094811 587 D 587
Cdd:PRK07994 525 P 525
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
376-572 |
3.85e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 40.75 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 376 EAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIATDSLTAVEPALTKSTKDAASLTAAEPAPTkSTNAADSLTAVEPVP 455
Cdd:PHA03369 345 NEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQ-FCGDPGLVSPYNPQS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 456 TKSTNAADSLTAVEPVPTKSTIAADSlIAAEPAPTKSTTAA------------DSLTaVEPMPTKSTTAADSLTAVEPAP 523
Cdd:PHA03369 424 PGTSYGPEPVGPVPPQPTNPYVMPIS-MANMVYPGHPQEHGherkrkrggelkEELI-ETLKLVKKLKEEQESLAKELEA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2785094811 524 TKSTTAAASLTAAEPAPTKSTTAAdgltadePAPTKSTTAADGLTADEP 572
Cdd:PHA03369 502 TAHKSEIKKIAESEFKNAGAKTAA-------ANIEPNCSADAAAPATKR 543
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
116-223 |
3.85e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 40.77 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 116 TPLIKAVQCQNTDCVYILLR-HNANPNLTDFHGNTAFHHAASRGNIKIVKLLLK-----YNVDFEAKTKYGLTPLQLATY 189
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVV 98
|
90 100 110
....*....|....*....|....*....|....
gi 2785094811 190 ENHTEMIKFLESKSADAQAVQVSSSARRPAHKKK 223
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPRATGTFFRPGPKNL 132
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
71-202 |
3.99e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 40.63 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 71 EHHVDEYdRRGRTSLHYACVHNHPDVVTLLLEYNSNINIQ------DDEGCT-------PLIKAVQCQNTDCVYILLRHN 137
Cdd:cd21882 64 APCTDEF-YQGQTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 138 ANP---NLTDFHGNTAFHHAASRGN---------IKIVKLLLKYNVDF-------EAKTKYGLTPLQLATYENHTEMIKF 198
Cdd:cd21882 143 AQPaalEAQDSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQH 222
|
....
gi 2785094811 199 LESK 202
Cdd:cd21882 223 ILQR 226
|
|
| PRK11907 |
PRK11907 |
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; |
425-553 |
6.48e-03 |
|
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
Pssm-ID: 237019 [Multi-domain] Cd Length: 814 Bit Score: 39.84 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 425 TKDAASLTAAEpAPTKSTNAADSLTAVEPVPTKSTNAADSLTAVEPvptkstiaadsliAAEPAPTKST--TAADSLTAv 502
Cdd:PRK11907 7 SKSAVALTLAL-LTASNPKLAQAEEIVTTTPATSTEAEQTTPVESD-------------ATEEADNTETpvAATTAAEA- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2785094811 503 epmPTKSTTAADSltavEPAPTKSTTAAASLTAAEPAPTKSTTAADGLTAD 553
Cdd:PRK11907 72 ---PSSSETAETS----DPTSEATDTTTSEARTVTPAATETSKPVEGQTVD 115
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
50-101 |
6.69e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.33 E-value: 6.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2785094811 50 PLQRAASVGDLVTTESMIYSReHHVDEYDRRGRTSLHYACVHNHPDVVTLLL 101
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
375-507 |
7.17e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 39.70 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 375 KEAASLTAVEPePTKSTIAADSLTAVEPAQTKSTIATDSLTAVEPALTKSTkdAASLTAAEPAPTKSTNAADSLTAVEPV 454
Cdd:PRK14951 365 KPAAAAEAAAP-AEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAP--AAPPAAAPPAPVAAPAAAAPAAAPAAA 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2785094811 455 PTKSTNAADSltavEPVPTKSTIAADSLIAAEPAPTKSTTAADSLTAVEPMPT 507
Cdd:PRK14951 442 PAAVALAPAP----PAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
112-208 |
7.47e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 39.78 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 112 DEGCTPLIKAV---QCQNTDCVYILL---RHNANPN------LTD--FHGNTAFHHAASRGNIKIVKLLLKYNVDFEAKT 177
Cdd:cd22193 27 STGKTCLMKALlnlNPGTNDTIRILLdiaEKTDNLKrfinaeYTDeyYEGQTALHIAIERRQGDIVALLVENGADVHAHA 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2785094811 178 K--------------YGLTPLQLATYENHTEMIKFL---ESKSADAQA 208
Cdd:cd22193 107 KgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
78-208 |
7.64e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 39.68 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 78 DRRGRTSLHYACVHNHPDVVTLLLEYNSNiniQDDEGCTPLIKAVQcQNTDCVYILLRHN------------AN-PNLTD 144
Cdd:TIGR00870 49 DRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISL-EYVDAVEAILLHLlaafrksgplelANdQYTSE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2785094811 145 F-HGNTAFHHAASRGNIKIVKLLLKYNVDFEAKTK--------------YGLTPLQLATYENHTEMIKFLESKSADAQA 208
Cdd:TIGR00870 125 FtPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILT 203
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
345-577 |
9.91e-03 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 39.39 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 345 VPSEAAADVGPSTSTADsldAAEPAQTKSTKEAASLTAVEPEPTKSTIAADSLTAVEPAQTKSTIA-----------TDS 413
Cdd:COG3170 117 AAAPAPAPAAPAAAAAA---ADQPAAEAAPAASGEYYPVRPGDTLWSIAARPVRPSSGVSLDQMMValyranpdafiDGN 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 414 LTAVEPALTKSTKDAASLTAAEPAPTKSTNAA--DSLTAVEPVPTKSTNAADSLTAVEPVPTKSTIAADSLIAAEPAPTK 491
Cdd:COG3170 194 INRLKAGAVLRVPAAEEVAALSPAEARQEVQAqsADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVPAAAEDTLSP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785094811 492 STTAADSLTAVEPMPTKSTTAADSLTAVEPAPTKsttAAASLTAAEPAPTKSTTAADGLTADEPAPTKSTTAADGLTADE 571
Cdd:COG3170 274 EVTAAAAAEEADALPEAAAELAERLAALEAQLAE---LQRLLALKNPAPAAAVSAPAAAAAAATVEAAAPAAAAQPAAAA 350
|
....*.
gi 2785094811 572 PELSLT 577
Cdd:COG3170 351 PAPALD 356
|
|
| |
