|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
514-805 |
8.82e-121 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 366.62 E-value: 8.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 514 NCILKADIAILRQEICTMKNDNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQQELNDLKAENTRLNAELL 593
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 594 KEKESKKRLEADIESYQSRLAAAISKHSESVKTERNLKLALERTRD--VSVQVEMSSAISKVKAENEFLTEQLSETQIKF 671
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDewLRLQDKMNFDVSNLRDENEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 672 NALKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQRENAWLVQQLDDV 751
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156104901 752 HQKEDHKE-IVTNIQRGF--------IESGKKDLVLEEKSKKLMNECDHLKESLFQYEREKTE 805
Cdd:pfam14915 241 QNKADAKEkTVIDIQDQFqdivkklqAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAE 303
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
31-247 |
6.20e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 155.11 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 31 DSELQKIHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHC 110
Cdd:COG0666 51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 111 QEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKA 190
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156104901 191 SSHAVDRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAISHHLTKI 247
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
29-298 |
5.15e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.56 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 29 IRDSELQKIHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAV 108
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 109 HCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKK 188
Cdd:COG0666 96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 189 KASSHAVDRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAISHHLTKIQQQILEHKKKILKKEKSDVGS 268
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|
gi 156104901 269 SDESAVSIFHELRVDSLPASDDKDLNVATK 298
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
37-235 |
2.75e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 141.63 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERCLARRsGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACA 116
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 117 VILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVD 196
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190
....*....|....*....|....*....|....*....
gi 156104901 197 RLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDA 235
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
37-203 |
1.61e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.21 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERCLARRsGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACA 116
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 117 VILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVD 196
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 156104901 197 RLRRSAL 203
Cdd:COG0666 283 LDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
59-247 |
4.02e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.50 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 59 DLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALH 138
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 139 YAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDRLRRSALMLAVYYDSPGIVNIL 218
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180
....*....|....*....|....*....
gi 156104901 219 LKQNIDVFAQDMCGRDAEDYAISHHLTKI 247
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEI 201
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
71-163 |
1.34e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 71 LHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHgANPNLKDiYGNTALHYAVYSESTSLAE 150
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 156104901 151 KLLSHGAHIEALD 163
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-247 |
1.25e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.54 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 47 AEVERCLARRSGDLDALDKQHRTALHlACTSG---HVQVVTLLVNRKCQIDVCDKENRTPLiqAVHCQEEACAV----IL 119
Cdd:PHA03095 97 LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVellrLL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 120 LEHGANPNLKDIYGNTALHY-AVYS-ESTSLAEKLLSHGAHIEALDKDNNTPLLFAII---CKKEKMVEFLLKKkASSHA 194
Cdd:PHA03095 174 IDAGADVYAVDDRFRSLLHHhLQSFkPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLLIAG-ISINA 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156104901 195 VDRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAISHHLTKI 247
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
37-130 |
8.92e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERcLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNrKCQIDVCDkENRTPLIQAVHCQEEACA 116
Cdd:pfam12796 1 LHLAAKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 156104901 117 VILLEHGANPNLKD 130
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
137-229 |
1.00e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 137 LHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDrlRRSALMLAVYYDSPGIVN 216
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 156104901 217 ILLKQNIDVFAQD 229
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
100-244 |
8.12e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 100 NRTPLIQAVHCQEEACAVI---LLEHGANPNLKDIYGNTALHYAVYSEST-SLAEKLLSHGAHIEALDKDNNTPLL---- 171
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHvyls 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156104901 172 -FAIickKEKMVEFLLKKKASSHAVDRLRRSAlmLAVYYDSPG----IVNILLKQNIDVFAQDMCGRDAEDyaisHHL 244
Cdd:PHA03095 127 gFNI---NPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLH----HHL 195
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
37-195 |
4.23e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.03 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACA 116
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 117 VILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLL-FAIICKKEKMVEFLLKKKASSHAV 195
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
29-210 |
1.32e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.06 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 29 IRDSELQKIhRAAVKGDAAEVE--RCLARRSGDLDALDKQH-RTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLI 105
Cdd:PHA02878 128 IQTIDLVYI-DKKSKDDIIEAEitKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 106 QAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAV-YSESTSLAEKLLSHGAHIEALDKDNN-TPLLFAIicKKEKMVE 183
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSI--KSERKLK 284
|
170 180
....*....|....*....|....*....
gi 156104901 184 FLLKKKASSHAVDRLRRSALMLAV--YYD 210
Cdd:PHA02878 285 LLLEYGADINSLNSYKLTPLSSAVkqYLC 313
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-197 |
2.72e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.67 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 47 AEVERCLARRSGDLDALDKQHRTALHLACTSGHV--QVVTLLVNRKCQIDVCDKENRTPL-IQAVHCQEEACAVI-LLEH 122
Cdd:PHA03095 167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVLpLLIA 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156104901 123 GANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDR 197
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
41-197 |
3.79e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.31 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 41 AVKGDAAEVERCLARRSGDLDALDKQHRTALHLACT--SGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVI 118
Cdd:PHA03100 80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 119 ------------------LLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEK 180
Cdd:PHA03100 160 kllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
|
170
....*....|....*..
gi 156104901 181 MVEFLLKKKASSHAVDR 197
Cdd:PHA03100 240 IFKLLLNNGPSIKTIIE 256
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
64-225 |
8.17e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.15 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 64 DKQHRTALHLACTSGHVQ-----VVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVI--LLEHGANPNLKDIYGNTA 136
Cdd:PHA03100 65 TKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 137 LHYAVYSESTSL--AEKLLSHGAHIEALD--------------KDN--NTPLLFAIICKKEKMVEFLLKKKASSHAVDRL 198
Cdd:PHA03100 145 LHLYLESNKIDLkiLKLLIDKGVDINAKNrvnyllsygvpiniKDVygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
|
170 180
....*....|....*....|....*..
gi 156104901 199 RRSALMLAVYYDSPGIVNILLKQNIDV 225
Cdd:PHA03100 225 GDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
59-242 |
1.29e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.38 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 59 DLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAV-----ILLEHGANPNLKDIYG 133
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVkeivkLLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 134 NTALHYAVY--SESTSLAEKLLSHGAHIEALDKDNNTPL-LFAIICKKE-KMVEFLLKKKASSHAVDRlrrsalmlavyy 209
Cdd:PHA03100 107 ITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLhLYLESNKIDlKILKLLIDKGVDINAKNR------------ 174
|
170 180 190
....*....|....*....|....*....|...
gi 156104901 210 dspgiVNILLKQNIDVFAQDMCGRDAEDYAISH 242
Cdd:PHA03100 175 -----VNYLLSYGVPINIKDVYGFTPLHYAVYN 202
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
59-242 |
1.45e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.30 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 59 DLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALH 138
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 139 YAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEkMVEFLLKKkASSHAVDRLRRSALMLAVYYD-SPGIVNI 217
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDI 273
|
170 180
....*....|....*....|....*
gi 156104901 218 LLKQNIDVFAQDMCGRDAEDYAISH 242
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFKY 298
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
53-219 |
1.84e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 53 LARRSGDLDALDKQHRTALHLACTSGH-VQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVI-LLEHGANPNLKD 130
Cdd:PHA02876 293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARD 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 131 IYGNTALHYAVYSESTSLAEKLLSHGAHIEAL----------------------------------DKDNNTPLLFAiiC 176
Cdd:PHA02876 373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALsqkigtalhfalcgtnpymsvktlidrganvnskNKDLSTPLHYA--C 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156104901 177 KKE---KMVEFLLKKKASSHAVDRLRRSALMLAVYYDspGIVNILL 219
Cdd:PHA02876 451 KKNcklDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
86-229 |
2.66e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 86 LVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSEST-----SLAEKLLSHGAHIE 160
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156104901 161 ALDKDNNTPLLFAIICKKE--KMVEFLLKKKASSHAVDRLRRSALMLAVYYDSP--GIVNILLKQNIDVFAQD 229
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN 173
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
67-247 |
4.74e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 62.70 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 67 HRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSEST 146
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 147 SLAEKLLSHGAHI-EALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDRLRRSALMLAVYYDSPGIVNILLKQNIDV 225
Cdd:PHA02875 82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
|
170 180
....*....|....*....|..
gi 156104901 226 FAQDMCGRDAEDYAISHHLTKI 247
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAI 183
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
37-239 |
1.01e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.00 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERCLARrSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDvcdkENRTPLIQAVHCQEEACA 116
Cdd:PHA02876 182 IHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 117 VILLEHGANPNLKDIYGNTALHYAVYSESTS-LAEKLLSHGAHIEALDKDNNTPL-LFAIICKKEKMVEFLLKKKASSHA 194
Cdd:PHA02876 257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNA 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156104901 195 VDRLRRSALMLAVYYD-SPGIVNILLKQNIDVFAQDMCGRDAEDYA 239
Cdd:PHA02876 337 ADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA 382
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
119-233 |
2.63e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.42 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 119 LLEHGANPNLKDIYGNTALHYAVYSESTSLAE---KLLSHGAHIEALDKDNNTPlLFAIIC--KKEKMVEFLLKKKASSH 193
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTP-LHLYLYnaTTLDVIKLLIKAGADVN 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 156104901 194 AVDRLRRSAL--MLAVYYDSPGIVNILLKQNIDVFAQDMCGR 233
Cdd:PHA03095 112 AKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGM 153
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
68-224 |
6.31e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.85 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 68 RTALHLACTSGHVQVVTLLVNRKCQI-DVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSEST 146
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156104901 147 SLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVDRLRRSALM-LAVYYDSPGIVNILLKQNID 224
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
29-209 |
6.72e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 29 IRDSELQKIHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAV 108
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 109 HCQEEACAVILLEHGANPNLKDIYGNTALHYAV-YSEStslAEKLLSHGAHIEALDKDNNTPLLFAI--ICKKEkMVEFL 185
Cdd:PHA02874 199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIiHNRS---AIELLINNASINDQDIDGSTPLHHAInpPCDID-IIDIL 274
|
170 180
....*....|....*....|....
gi 156104901 186 LKKKASSHAVDRLRRSALMLAVYY 209
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTAFKY 298
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
133-186 |
1.42e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 156104901 133 GNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLL 186
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
100-153 |
5.66e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 5.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 156104901 100 NRTPLIQAV-HCQEEACAViLLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLL 153
Cdd:pfam13637 1 ELTALHAAAaSGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
119-173 |
3.25e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.73 E-value: 3.25e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 156104901 119 LLEHG-ANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFA 173
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
118-196 |
4.41e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 4.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156104901 118 ILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAVD 196
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
74-225 |
5.34e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.33 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 74 ACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAeKLL 153
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156104901 154 SHGAHIealdkdNNTPLLFAIICKKEK-----MVEFLLKKKASSHAVDRLRRSALMLAVYYDSPGIVNILLKQNIDV 225
Cdd:PLN03192 611 YHFASI------SDPHAAGDLLCTAAKrndltAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
40-191 |
7.20e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.95 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 40 AAVKGDAAEVERCLaRRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVIL 119
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156104901 120 --LEHGANPNLkdiyGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKAS 191
Cdd:PLN03192 611 yhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
41-169 |
1.19e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 41 AVKGDAAEVeRCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLlvnrkcqidvcdkenrtpliqavhcqeeacaviLL 120
Cdd:PTZ00322 90 AASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRV---------------------------------LL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 156104901 121 EHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGahIEALDKDNNTP 169
Cdd:PTZ00322 136 EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS--QCHFELGANAK 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
85-140 |
1.62e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 156104901 85 LLVNRKCQIDVCDKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYA 140
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
116-247 |
2.12e-06 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 50.34 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 116 AVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASSHAV 195
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 156104901 196 DRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAISHHLTKI 247
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
37-87 |
2.17e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 156104901 37 IHRAAVKGDAAEVERCLARRSgDLDALDKQHRTALHLACTSGHVQVVTLLV 87
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
91-242 |
3.10e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 50.35 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 91 CQIDVC--DKENRTPLIQAVHCQEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNT 168
Cdd:PHA02874 113 CGIDVNikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156104901 169 PLLFAIICKKEKMVEFLLKKkaSSHAVDRLRR--SALMLAVYYDSPGIVniLLKQNIDVFAQDMCGRDAEDYAISH 242
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDH--GNHIMNKCKNgfTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINP 264
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
442-785 |
3.76e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 442 LKQENEEKTNVNMLYKKNREELERKEKQYKKEVEAKQLeptvQSLEMKSKTARNTPNWDFHNHEEMKGLMDENCILKADI 521
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL----KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 522 AILRQEICTMKNDNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITE------TAFRYQQELNDLKAENTRLNAELLKE 595
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllklerRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 596 KESKKRLEADIESYQSRLAAAisKHSESVKTERNLKLALERTRDVSVQVEMSSAISKVKAENEFLTEQLSETQIKFNALK 675
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAE--EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 676 DKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQRENAWLVQQLDDVHQKE 755
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350
....*....|....*....|....*....|
gi 156104901 756 DHKEIVTNIQRGFIESGKKDLVLEEKSKKL 785
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-241 |
4.81e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.88 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 41 AVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRtpLIQAVHCQE-EACAVIL 119
Cdd:PHA02878 44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA--IKDAFNNRNvEIFKIIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 120 LEHGANPNLKDIYGNTALHYAVYSEsTSLAEKLLSHGAHIEALDKDN-NTPLLFAIICKKEKMVEFLLKKKASSHAVDRL 198
Cdd:PHA02878 122 TNRYKNIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 156104901 199 RRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYAIS 241
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-814 |
6.77e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 360 AEQALPVASEEEQERHERSEKKQPQVKEGNNTNKSEKIQLSENICDSTSSAAAGRLTQQRKIGKTYPQQFPKKLKEEHDR 439
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 440 CTLKQENEEKTNVNMLyKKNREELERKEKQYKKEVEAKQLEPTVQSLEMKSKTarntpnwdfhnhEEMKGLMDENciLKA 519
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA------------DEAKKKAEEA--KKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 520 DIAILRQEICTMKNDNLEK---ENKYLKDIKIVKETNAALEkyIKLNEEMITETAFRYQQELNdlKAENTRLNAELLKEK 596
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAE 1561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 597 ESKKRLEADIESYQSRLA---AAISKHSESVKTERNLKLALERTRDVSVQVEMSSAiSKVKAENEFLTEQLSETQIKFNA 673
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMAlrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 674 LKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEE---RICHLQRENAWLVQQLDD 750
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAEEKKKAEE 1720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156104901 751 VHQKEDHKEI-VTNIQRGFIESGKK--DLVLEEKSKKLMNECDHLKESLFQYEREKTEGVVSIKEDK 814
Cdd:PTZ00121 1721 LKKAEEENKIkAEEAKKEAEEDKKKaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
504-805 |
7.59e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 504 HEEMKGLMDENCILKADIAILRQEIctmknDNLEKENKYLKD-IKIVKETNAALEKYIKLNEEMITEtafrYQQELNDLK 582
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERL-----EELEEDLSSLEQeIENVKSELKELEARIEELEEDLHK----LEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 583 AentRLNAELLKEKESKKRleaDIESYQSRLAAAISkHSESVKTERNLKLAL---ERTRDVSVQVEMSSAISKVKAENEF 659
Cdd:TIGR02169 786 A---RLSHSRIPEIQAELS---KLEEEVSRIEARLR-EIEQKLNRLTLEKEYlekEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 660 LTEQLSETQIKFNALKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQR 739
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 740 ENAWLVQQLDDVHQKEDHKEIVTNIQRG--------------FIESGKKDLVLEEKSKKLMNECDHLKESLFQYEREKTE 805
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEiralepvnmlaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
44-219 |
1.34e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.42 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 44 GDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVH-------------- 109
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidng 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 110 ---------CQEEACAVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAIICKKEK 180
Cdd:PHA02874 92 vdtsilpipCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 156104901 181 MVEFLLKKKASSHAVDRLRRSALMLAVYYDSPGIVNILL 219
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
53-107 |
1.43e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 1.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 156104901 53 LARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQA 107
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
514-763 |
1.46e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 514 NCILKADIAILRQEI--CTMKNDNLEKE----NKYLKDIKivKETNAALEKYiklnEEMITETAfryqQELNDLKAENTR 587
Cdd:PHA02562 169 DKLNKDKIRELNQQIqtLDMKIDHIQQQiktyNKNIEEQR--KKNGENIARK----QNKYDELV----EEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 588 LNAELLKEKESKKRLEADIESYQSRLAAAISKHSESVKTERNLKLALE---RTRDVSVQVEMssaISKVKAENEFLTEQL 664
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptCTQQISEGPDR---ITKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 665 SETQIKFNALKDKFrktrDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQRENAWL 744
Cdd:PHA02562 316 EKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
250
....*....|....*....
gi 156104901 745 VQQLDDVHQKEDHKEIVTN 763
Cdd:PHA02562 392 VKTKSELVKEKYHRGIVTD 410
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
553-722 |
1.76e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 553 NAALEKYIKLNEEMITETAFR----YQQELNDLKAENTRLNAEL--LKEK-------ESKKRLEADIESYQSRLAAAISK 619
Cdd:COG3206 155 NALAEAYLEQNLELRREEARKalefLEEQLPELRKELEEAEAALeeFRQKnglvdlsEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 620 HSESVKTERNLKLALERTRDVSVQVEMSSAISKVKAENEFLTEQLSETQIKFN-------ALKDKFRKTRDSLRK-KSLA 691
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQeAQRI 314
|
170 180 190
....*....|....*....|....*....|.
gi 156104901 692 LETVQNDLSQTQQQTQEMKEMYQNAEAKVNN 722
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
37-174 |
1.78e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.52 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 37 IHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNRKCQIDVCDKENRTPLIQAVHCQEEACA 116
Cdd:PHA02876 345 LHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 117 V-ILLEHGANPNLKDIYGNTALHYAVYSE-STSLAEKLLSHGAHIEALDKDNNTPLLFAI 174
Cdd:PHA02876 425 VkTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL 484
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
461-710 |
3.13e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 461 EELERKEKQYKKEVEAKQLE-PTVQSLEMKSKTARNTPNwdfhnhEEMKGLMDENCILKADIAILRQEICTMKND--NLE 537
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKElKNLDKNLNKDEEKINNSN------NKIKILEQQIKDLNDKLKKNKDKINKLNSDlsKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 538 KENKYLKDIKIVKETN-AALEKYIKLNEEMITETA---FRYQQELNDLKAENTRLNAELLKEKESKKRLEADIESYQSRL 613
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVElNKLEKQKKENKKNIDKFLteiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 614 AAAISKHSESVKTERNLKLALERTRDVSVQV--------EMSSAISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSL 685
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQIselkkqnnQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260
....*....|....*....|....*
gi 156104901 686 RKKSLALETVQNDLSQTQQQTQEMK 710
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLK 294
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
537-722 |
3.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 537 EKENKY--LKDIKIVKETNAALEKYIKLNEEM--ITETAFRYQQELNDLKAENTRLNAELLKEKESKKRLEADIESYQSR 612
Cdd:COG1196 210 EKAERYreLKEELKELEAELLLLKLRELEAELeeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 613 LAAAISKHSEsvkTERNLKLALERTRDVSVQ-VEMSSAISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSLRKKSLA 691
Cdd:COG1196 290 EYELLAELAR---LEQDIARLEERRRELEERlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190
....*....|....*....|....*....|.
gi 156104901 692 LETVQNDLSQTQQQTQEMKEMYQNAEAKVNN 722
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
574-811 |
3.99e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 574 YQQELNDLKAENTRLNAELLKEKESKKRLEADIESYQSRLAAAISKhseSVKTERNLKLALERTRDVSVQVE-MSSAISK 652
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---LDELAEELAELEEKLEELKEELEsLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 653 VKAENEFLTEQLSETQIKFNALKDKFRKTR---DSLRKKSLALETVQNDLSQTQQQTQEmkemyQNAEAKVNNSTGKWNC 729
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLElqiASLNNEIERLEARLERLEDRRERLQQ-----EIEELLKKLEEAELKE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 730 VEERICHLQRENAWLVQQLDDVHQKEDhkeivtNIQRGFIESGKKDLVLEEKSKKLMNECDHLkESLFQYEREKTEGVVS 809
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALE------ELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKA 510
|
..
gi 156104901 810 IK 811
Cdd:TIGR02168 511 LL 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
349-717 |
1.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 349 AVQRKNVQTLRAEQALPVASEEEQERHERSEKKQPQVKEGNNTNKSEKIQLSENICDSTSSAAAGRLTQQRKIGKTYPQQ 428
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 429 FPKKLKEEHDRCTLKQENEEKTNVNMLyKKNREELERKEKQYKKEVEAKQLEPTVQSLEMKSKTarntpnwdfhnhEEMK 508
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEA-KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA------------DEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 509 glmdencilKADIAILRQEICTMKNDNLEKENKYLKDIKIVKETNAALEKYiklNEEMITETAFRYQQELNDLKAENTRL 588
Cdd:PTZ00121 1529 ---------KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK---KAEEDKNMALRKAEEAKKAEEARIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 589 NAELLKEKESKKRLEADIESYQSRLAAAISKHSESVKTERNLKLALERTRDVSVQVEMSSAISKVKAENEFLTEQLSETQ 668
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 156104901 669 ikfnalKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAE 717
Cdd:PTZ00121 1677 ------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
118-190 |
1.18e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 43.33 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156104901 118 ILLEHGANPNLKD-IYGNTALHYAVYSESTSLAEKLLSH-GAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKA 190
Cdd:PHA02736 76 LLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
28-198 |
1.19e-04 |
|
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: 45.77 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 28 RIRDSELqkiHRAAVKGDAAEVERCLARRSGDLDALDKQHRTALHLACTSGHVQVVTLLVNrkcqidvCDKEnrtpLIQa 107
Cdd:cd22192 15 RISESPL---LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-------AAPE----LVN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 108 vhcqeeacavillehgaNPNLKDIY-GNTALHYAVYSESTSLAEKLLSHGAHIEA---------LDKDN-----NTPLLF 172
Cdd:cd22192 80 -----------------EPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNliyygEHPLSF 142
|
170 180
....*....|....*....|....*.
gi 156104901 173 AIICKKEKMVEFLLKKKASSHAVDRL 198
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSL 168
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
535-708 |
1.29e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 535 NLEKENKYLKDIKIVKETNAALEKYIKLNEEMITEtafrYQQELNDLKAENTRLNAELLkEKESKKRLEA-------DIE 607
Cdd:PRK11281 64 DLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQ----AQAELEALKDDNDEETRETL-STLSLRQLESrlaqtldQLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 608 SYQSRLAAAiskhsesvkterNLKLALERTRDVSVQVEMSSA------ISKVKAENEFLTEQLSETQIKFNALKDKFRKT 681
Cdd:PRK11281 139 NAQNDLAEY------------NSQLVSLQTQPERAQAALYANsqrlqqIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA 206
|
170 180 190
....*....|....*....|....*....|....
gi 156104901 682 RDSLRKKSLA-------LETVQNDLSQTQQQTQE 708
Cdd:PRK11281 207 QNDLQRKSLEgntqlqdLLQKQRDYLTARIQRLE 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-740 |
1.47e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 457 KKNREELER--KEKQYKKEVEAKQLEPTVQSLEMKSKTARNtpnwdfhnheEMKGLMDENCILKADIAILRQEiCTMKND 534
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKEAIER----------QLASLEEELEKLTEEISELEKR-LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 535 NLEKENKYLKD-----IKIVKETNAALEKYIKLNEEMITEtafrYQQELNDLKAENTRLNAELLKEKESKKRLEADIESY 609
Cdd:TIGR02169 273 LLEELNKKIKDlgeeeQLRVKEKIGELEAEIASLERSIAE----KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 610 QSRLAAAISKHSESvKTERNLKLA--------LERTRD--VSVQVEMSSAISK---VKAENEFLTEQLSETQIKFNALKD 676
Cdd:TIGR02169 349 RKRRDKLTEEYAEL-KEELEDLRAeleevdkeFAETRDelKDYREKLEKLKREineLKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156104901 677 KFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKWNCVEERICHLQRE 740
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
69-187 |
2.14e-04 |
|
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: 45.07 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 69 TALHLACTSGHVQVVTLLVNR------KCQIDVCDKENRTPL-------IQAVHC--QEEACAvILLEHGANPNLKDIYG 133
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSfyhgespLNAAAClgSPSIVA-LLSEDPADILTADSLG 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 134 NTALHYAV--------YSE-STSLAEKLLSHGAHI-------EALDKDNNTPLlfAIICKKEKMVEFLLK 187
Cdd:TIGR00870 209 NTLLHLLVmenefkaeYEElSCQMYNFALSLLDKLrdskeleVILNHQGLTPL--KLAAKEGRIVLFRLK 276
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
271-694 |
2.35e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 271 ESAVSIFHELRVDSLPASDD-KDLNVATKQCVPEKVSEPLPGSSHEKGNRIVNGQGEGPPAKHPSLKPSTEVEDPAVKGA 349
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTfRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 350 VQRKNVQTLRAEQALPVASEEEQERHERSEKKQPQVKEGNNTNKSEKIQLSENICDSTSSAAAGRLTQQRKIGKTYPQQF 429
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 430 PKKLKEEHDRCTLKQENEEKTNVNMLYKKNREELERKEK----QYKKEVEAkqlEPTVQSLEMKSKTARNTPNWDFHNHE 505
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAklvdQYKELVAS---ERIVFQQELVSIFPDIIPVLKEDNLL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 506 EMKGLmdENCILKADIAI--LRQEICTMKNDNLEK-----ENKYLKDIKIVKETNAALE--------KYIKLNEEMITET 570
Cdd:pfam09731 281 SNDDL--NSLIAHAHREIdqLSKKLAELKKREEKHieralEKQKEELDKLAEELSARLEevraadeaQLRLEFEREREEI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 571 AFRYQQEL-NDLKAENT----RL-NAELLKEKESKKRLEADIES--------YQSRLAAAISK----------HSESVKT 626
Cdd:pfam09731 359 RESYEEKLrTELERQAEaheeHLkDVLVEQEIELQREFLQDIKEkveeeragRLLKLNELLANlkglekatssHSEVEDE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 627 ER----------NLKLALE------RTRDVSVQVEmssAISKVKAENEF---LTEQLSETQIK-----FNALKDKFRKTR 682
Cdd:pfam09731 439 NRkaqqlwlaveALRSTLEdgsadsRPRPLVRELK---ALKELASDDEVvkaALASLPEEAYQrgvytEAALRERFRRVA 515
|
490
....*....|..
gi 156104901 683 DSLRKKSLALET 694
Cdd:pfam09731 516 KEVRKVSLIDPE 527
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
132-164 |
4.01e-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: 38.42 E-value: 4.01e-04
10 20 30
....*....|....*....|....*....|....
gi 156104901 132 YGNTALHYAVYSE-STSLAEKLLSHGAHIEALDK 164
Cdd:pfam00023 1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
66-200 |
4.19e-04 |
|
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: 43.72 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 66 QHRTALHLACTSGHVQVVTLLVNRKCQI------DVCDKENRT-------PLIQAVHCQEEACAVILLEHGANP---NLK 129
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVsaratgRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 130 DIYGNTALHYAVY-----SESTSLA----EKLLSHGAH---IEALDKDNN----TPLLFAIICKKEKMVEFLLKKKASSH 193
Cdd:cd21882 152 DSLGNTVLHALVLqadntPENSAFVcqmyNLLLSYGAHldpTQQLEEIPNhqglTPLKLAAVEGKIVMFQHILQREFSGP 231
|
....*..
gi 156104901 194 AVDRLRR 200
Cdd:cd21882 232 YQPLSRK 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
457-748 |
4.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 457 KKNREELERKEK--QYKKEVeaKQLEPTVQSLEmKSKTARNTPNWDFHNHEE---MKGLMDENCILKADIAI-LRQEICT 530
Cdd:pfam10174 458 QREREDRERLEEleSLKKEN--KDLKEKVSALQ-PELTEKESSLIDLKEHASslaSSGLKKDSKLKSLEIAVeQKKEECS 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 531 mkndNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITetafRYQQELNDLKAENTRLnAELLKEKESKKRLE----ADI 606
Cdd:pfam10174 535 ----KLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVA----RYKEESGKAQAEVERL-LGILREVENEKNDKdkkiAEL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 607 ESYQSRlaaaisKHSESVKTERNLKLALERTRDVSVQV-------EMSSAISKVKAENEFLTEQLSETQIKFNALKDKFR 679
Cdd:pfam10174 606 ESLTLR------QMKEQNKKVANIKHGQQEMKKKGAQLleearrrEDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 680 KTRDSLRKKSLALETVQNDlsqTQQQTQEMKEMYQNA-----EAKVNN------STGKWNCVEERICHLQRENAWLVQQL 748
Cdd:pfam10174 680 STQQSLAEKDGHLTNLRAE---RRKQLEEILEMKQEAllaaiSEKDANiallelSSSKKKKTQEEVMALKREKDRLVHQL 756
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
68-98 |
6.12e-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: 38.04 E-value: 6.12e-04
10 20 30
....*....|....*....|....*....|..
gi 156104901 68 RTALHLACTS-GHVQVVTLLVNRKCQIDVCDK 98
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
517-755 |
6.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 517 LKADIAILRQEIctmknDNLEKE-NKYLKDIKIVKETNAALEKYIKLNEEMITETafryQQELNDLKAENTRLNAEllkE 595
Cdd:COG4942 25 AEAELEQLQQEI-----AELEKElAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKE---I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 596 KESKKRLEADIESYQSRLAAAiskhsesVKTERNLKLALERTRDVSVQVEMSSAIskVKAENEFLTEQLSETQIKFNALK 675
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL-------YRLGRQPPLALLLSPEDFLDAVRRLQY--LKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 676 DKfrktRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNNSTGKwncVEERICHLQRENAWLVQQLDDVHQKE 755
Cdd:COG4942 164 AL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEA 236
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
116-174 |
7.20e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 7.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 156104901 116 AVILLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLFAI 174
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAV 219
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
196-239 |
8.57e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 8.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 156104901 196 DRLRRSALMLAVYYDSPGIVNILLKQNIDVFAQDMCGRDAEDYA 239
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
444-802 |
8.84e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 444 QENEEKTNVNMLYKKNREELERKEKQYKKEVEAKQ-------LEPTVQSLEMKSKTARNTPNWDFHNH-EEMKGLMDENc 515
Cdd:pfam05483 205 QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEkqvslllIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQDEN- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 516 ilkadiaiLRQEIctMKNDNLEKEnkyLKDIKIVKETNAALEKYIKLNEEMITETAFRY-------QQELNDLKAENTRL 588
Cdd:pfam05483 284 --------LKELI--EKKDHLTKE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekeaqMEELNKAKAAHSFV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 589 NAELlkeKESKKRLEADIESYQSRLAaaiskhsesvKTERNLK-LALERTRDVSVQVEMSSAISKVKAENEFLTEQLSET 667
Cdd:pfam05483 351 VTEF---EATTCSLEELLRTEQQRLE----------KNEDQLKiITMELQKKSSELEEMTKFKNNKEVELEELKKILAED 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 668 QI------KFNALKDKFRKTRDSL------RKKSLALETVQNDLSQTQQQ--TQEMKEMYQNAE-AKVNNSTGKWNCVEe 732
Cdd:pfam05483 418 EKlldekkQFEKIAEELKGKEQELifllqaREKEIHDLEIQLTAIKTSEEhyLKEVEDLKTELEkEKLKNIELTAHCDK- 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156104901 733 richLQRENAWLVQQLDD-VHQKEDHKEIVTNIQRGFIESGKKDLVLEEKSKKLMNECDHLKESLFQYERE 802
Cdd:pfam05483 497 ----LLLENKELTQEASDmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
119-172 |
1.27e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 156104901 119 LLEHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDNNTPLLF 172
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
536-722 |
1.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 536 LEKENKYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQ---QELNDLKAENTRLNAELLKEKESKKRLEA-------- 604
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldel 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 605 --------------------DIESYQSRLAAAISKHSESVKTERNLKLALERTRDVSVQVEMSSA-ISKVKAENEFLTEQ 663
Cdd:PRK03918 569 eeelaellkeleelgfesveELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEeLAETEKRLEELRKE 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156104901 664 LSETQIKFNalKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVNN 722
Cdd:PRK03918 649 LEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
567-720 |
3.14e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 567 ITETAFRYQQELNDLKAENTRLNAELLKEKESKKRLEADIESYQSRLAAAISKHSESVKternlklALERTRDVSVQVEM 646
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR-------ALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 647 -------------SSAISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTQEMKEMY 713
Cdd:COG3883 108 llgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
....*..
gi 156104901 714 QNAEAKV 720
Cdd:COG3883 188 SAEEAAA 194
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
132-161 |
3.44e-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: 35.64 E-value: 3.44e-03
10 20 30
....*....|....*....|....*....|
gi 156104901 132 YGNTALHYAVYSESTSLAEKLLSHGAHIEA 161
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
118-192 |
3.65e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 39.26 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156104901 118 ILLEHGANPNLKD-IYGNTALHYAVYSESTSLAEKLLSH-GAHIEALDKDNNTPLLFAIICKKEKMVEFLLKKKASS 192
Cdd:PHA02741 82 HLIELGADINAQEmLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATS 158
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-721 |
4.53e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 456 YKKNREELERKEKQYKK-EVEAKQLEPTVQSLEMKSKTARNTpnwdfhnHEEMKGLMDEnciLKADIAILRQEIctmknd 534
Cdd:COG1196 234 LRELEAELEELEAELEElEAELEELEAELAELEAELEELRLE-------LEELELELEE---AQAEEYELLAEL------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 535 nlekeNKYLKDIKIVKETNAALEKYIKLNEEMITETAFRY---QQELNDLKAENTRLNAELLKEKESKKRLEADIESYQS 611
Cdd:COG1196 298 -----ARLEQDIARLEERRRELEERLEELEEELAELEEELeelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 612 RLAAAISKHSESVKTERNLKLALERTRDVSVQVEMSSA-----ISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSLR 686
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|....*
gi 156104901 687 KKSLALETVQNDLSQTQQQTQEMKEMYQNAEAKVN 721
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-95 |
6.26e-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: 34.87 E-value: 6.26e-03
10 20 30
....*....|....*....|....*....|
gi 156104901 66 QHRTALHLACTSGHVQVVTLLVNRKCQIDV 95
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
88-229 |
7.44e-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: 40.06 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 88 NRKCQIDVCDKENRTPLIQAVHCQE-EACAVILLEHGANPNLkdiyGNTALHYAVYSESTSLaEKLLSH--------GAH 158
Cdd:TIGR00870 40 PKKLNINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILLHllaafrksGPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 159 IEALDKDNN------TPLLFAIICKKEKMVEFLLKKKASSHA------------VDRLRRSALMLAVY--YDSPGIVNIL 218
Cdd:TIGR00870 115 ELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFYHGESPLNAAacLGSPSIVALL 194
|
170
....*....|.
gi 156104901 219 LKQNIDVFAQD 229
Cdd:TIGR00870 195 SEDPADILTAD 205
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
67-95 |
7.56e-03 |
|
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: 34.54 E-value: 7.56e-03
10 20
....*....|....*....|....*....
gi 156104901 67 HRTALHLACTSGHVQVVTLLVNRKCQIDV 95
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
132-161 |
8.35e-03 |
|
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: 34.54 E-value: 8.35e-03
10 20 30
....*....|....*....|....*....|
gi 156104901 132 YGNTALHYAVYSESTSLAEKLLSHGAHIEA 161
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
446-733 |
8.75e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 446 NEEKTNVNMLYKKNREELERkekqykkevEAKQLEPTVQSLEMKSKTARNtpnwdfhNHEEMKGLMDENCILKADIAILR 525
Cdd:pfam07888 54 NRQREKEKERYKRDREQWER---------QRRELESRVAELKEELRQSRE-------KHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 526 QEICTMKNDNLEKENKYLKDIKIVkeTNAALEKYIKLneEMITETAFRYQQELNDLKAENTRLNAELLKEKESKKRLEAD 605
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTL--TQRVLERETEL--ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 606 IESYQSRLAAAISKhsesvkternlklALERTRDVSVQVEMSSAISKVKAENEFLTEQLSETQIKFNALKDKFRKTRDSL 685
Cdd:pfam07888 194 FQELRNSLAQRDTQ-------------VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156104901 686 RKKSLALETVQNDLSQTQQQTQEMKemYQNAEAKVNNSTGKWNCVEER 733
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLT--LQLADASLALREGRARWAQER 306
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
507-716 |
8.92e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.73 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 507 MKGLMDEncilKADIAILRQEICTMKNDNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQQELndlKAENT 586
Cdd:pfam07111 448 IKGLMAR----KVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQG---EAERQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 587 RLNAELLKEKESKKRLEADIESYQSRLAAAISKHSESVKTERNLKLALERTRDVSVQvemssAISKVKAENEF-LTEQLS 665
Cdd:pfam07111 521 QLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQ-----ALQEKVAEVETrLREQLS 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156104901 666 ETQIKFNALKDKFRKTRDSLRKkslaletVQNDLSQTQQQTQEMKEMYQNA 716
Cdd:pfam07111 596 DTKRRLNEARREQAKAVVSLRQ-------IQHRATQEKERNQELRRLQDEA 639
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
512-821 |
9.48e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 512 DENCILKADIAILRQEICTMKNdNLEKENKYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQQELNDLKAENTRL--- 588
Cdd:COG5185 212 TGNLGSESTLLEKAKEIINIEE-ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLikq 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 589 ---NAELLKEKESKKRLEADIESYQSRLAAA-ISKHSESVKTERNLKLALERTRDVSVQVEMSSAISKVKA--ENEFLTE 662
Cdd:COG5185 291 fenTKEKIAEYTKSIDIKKATESLEEQLAAAeAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEeiENIVGEV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 663 QLSETQIKFNALKDKFRKTRDSLRKKSLALETVQNDLSQTQQQTqeMKEMYQNAEAKVNNSTGKWNCVEERichlQRENA 742
Cdd:COG5185 371 ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDT--LKAADRQIEELQRQIEQATSSNEEV----SKLLN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104901 743 WLVQQLDDVHQK--EDHKEIVTNIQRGFIESGKKDL-VLEEKSKKLMNECDHLKESLfQYEREKTEGVVSIKEDKYFQTS 819
Cdd:COG5185 445 ELISELNKVMREadEESQSRLEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKATL-EKLRAKLERQLEGVRSKLDQVA 523
|
..
gi 156104901 820 RK 821
Cdd:COG5185 524 ES 525
|
|
| |
