|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-248 |
4.81e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 172.83 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 81 AQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAV 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
....*...
gi 13507620 241 ISQDADLK 248
Cdd:COG0666 275 LLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-257 |
1.53e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 162.82 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 81 AQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAV 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250
....*....|....*..
gi 13507620 241 ISQDADLKTPTKPKQHD 257
Cdd:COG0666 242 GADLNAKDKDGLTALLL 258
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
4.04e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 153.19 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 97 GHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13507620 177 DVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-240 |
1.55e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPA 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 113 ENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13507620 193 CETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
3.11e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.60 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 91 HVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 13507620 171 LLDHGADVNSRDKNGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
5.47e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 96.72 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPaeNIDNSGKTALHYAAAQGCLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 13507620 137 LLCEHKSPINLKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
9.16e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 96.34 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 90 LHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKsPINLKDlDGNIPLLVAVQNGHSEACH 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 13507620 170 FLLDHGADVNSRD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-239 |
1.66e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 101.28 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHVAA--K 95
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 96 NGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGC--LQAVQLLCEHKSPINLKDldgNIPLLvavqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 174 HGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
2.39e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.40 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 123 LHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHgADVNSRDkNGRTALMLACETGSSNTVD 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 13507620 203 ALIKKGADLSLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-224 |
4.73e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 94.71 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 88 SALHVAAKNGHP--ECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQA--VQLLCEHKSPINLKDLDGNIPLLVAVQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFN 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDslghNALHY 224
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-217 |
1.27e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 91.47 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 78 DVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAEniDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507620 158 VAVQNGHSEACHFLLDHGADVNSRDKNgrtalmlacETGSSNTVDALIKK---GADLSLVDSL 217
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVDKANTD---------DDFSPTELRELLQKrelGHSITIVDSV 714
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-222 |
1.54e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.56 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 43 GASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 123 LHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQngHSEACHFLLDHGADVNSRDKNGRTALMLACETGSS-NTV 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDII 271
|
170 180
....*....|....*....|.
gi 13507620 202 DALIKKGADLSLVDSLGHNAL 222
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-230 |
1.32e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.92 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLKVMVTHGVDVTAQDSSGHSALHV--AAKNGHPECIRKL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 106 LQYKSPAENIDNSGKTALH-YAAAQGC-LQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF--LLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13507620 182 DKNGRTALMLACETGSSNT--VDALIKKGADLSLVDSLGHNALHYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-108 |
1.47e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.54 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHgVDVTAQDsSGHSALHVAAKNGHPECI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*.
gi 13507620 103 RKLLQY 108
Cdd:pfam12796 78 KLLLEK 83
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
2.14e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.73 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV---DVTAQDssGHSALHVAAKNGHPECIRKLLQYKSPAEN 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 115 IDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 13507620 194 ETGSSNTVDALIKKGADLSLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
23-219 |
6.70e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 81.16 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECI 102
Cdd:PHA02874 128 LHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 103 RKLLQYKSPAENIDNSGKTALHYAAAQGcLQAVQLLCEHKSpINLKDLDGNIPLLVAVQNGHS-EACHFLLDHGADVNSR 181
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNAS-INDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIK 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13507620 182 DKNGRTALMLACETGSSNTV------DALIKKGAD-LSLVDSLGH 219
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVikdiiaNAVLIKEADkLKDSDFLEH 329
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
7.46e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 156 LLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKgADLSLVDSlGHNALHYSKLSENAGIQN 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 13507620 236 LLLSK 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
4.78e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 79 VtaqdssghSALHVAAKNGhpECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLV 158
Cdd:PHA02874 94 T--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 159 AVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQnLLL 238
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLI 242
|
250
....*....|....*
gi 13507620 239 SKIS---QDADLKTP 250
Cdd:PHA02874 243 NNASindQDIDGSTP 257
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-223 |
4.47e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.09 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKS 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 111 paeNIdNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGH-SEACHFLLDHGADVNSRDKNGRTAL 189
Cdd:PHA02876 236 ---NI-NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190
....*....|....*....|....*....|....*
gi 13507620 190 MLACETG-SSNTVDALIKKGADLSLVDSLGHNALH 223
Cdd:PHA02876 312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLH 346
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-225 |
9.60e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.94 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-KVMVTHGVDVTAQDSSGHSALHVAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 96 NGH-PECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQ-AVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLD 173
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13507620 174 HGADVNSRDKNGRTALMLA-CETGSSNTVDALIKKGADLSLVDSLGHNALHYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
1.05e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 1.05e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 13507620 55 TAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
432-933 |
2.97e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 511
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 LSQESADGyshlREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppaeacEELRSSYCSVIENMN 591
Cdd:COG1196 309 ERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 592 KEKAFLFEKYQQAQEEIMKLKDTLKSQmpQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDA 671
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 672 AEYIHKAEHERLMHVSNLSRAKSEEALSE---MKSQYSKVLNELTQ---------LKQLVDAHKENSVSITEHLQVITTL 739
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEElaeAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 740 RTTAkemEEKISALTGHLANKEAEVAKLEKQLAEEKAA-------VSDAMVPKSSYEKLQASLESEVNALATKLKESVRE 812
Cdd:COG1196 537 EAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 813 REKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLK 892
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 13507620 893 LKEALNSLSQLSYSTSSSKRQSQQLDLLQQQVKQLQNQLAE 933
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
631-864 |
3.28e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.35 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 631 KEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEyihkaehERLMHVSNLSRAKSEeaLSEMKSQYSKVLN 710
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-------EAKLLLQQLSELESQ--LAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 711 ELTQLKQLVDAHKENSVSITEHlQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMvpkssyEK 790
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 791 LQASLESEVNALATKLKESVREREKAHSEVA---QVRSEVSQARREKDNIQTLLkakeqevTALVQKFQRAQEELAG 864
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELY-------ESLLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
434-896 |
3.35e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 434 QLQDSLHDLQKRLESSEAEKKQLQDELQSQRtdtlclnntEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglls 513
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR---------EELEKLEKEVKELEELKEEIEELEKELESLEGSKR----- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 514 qesadgyshlreapadeDIDTLKQDLQKAVEESarnKERVRELETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKE 593
Cdd:PRK03918 256 -----------------KLEEKIRELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 594 KAFLFEKYQQAQEEIMKLkdtlkSQMPQEAPDDSGDMKEAMNRmIDELNKQVsELSQLYREAQAELEDYRKRKS------ 667
Cdd:PRK03918 316 LSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR-LEELEERH-ELYEEAKAKKEELERLKKRLTgltpek 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 668 LEDAAEYIHKAEHERLMHVSNLSRAKSEeaLSEMKSQYSKVLNELTQLK--------QLVDAHKENsvSITEHLQVITTL 739
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGE--LKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKE--LLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 740 RTTAKEMEEKISALtghlankEAEVAKLEKQLAEEkaavSDAMVPKSSYEKLQaSLESEVNAL-ATKLKESVREREKAHS 818
Cdd:PRK03918 465 EKELKEIEEKERKL-------RKELRELEKVLKKE----SELIKLKELAEQLK-ELEEKLKKYnLEELEKKAEEYEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 819 EVAQVRSEVSQARREKDNIQTLlkakEQEVTALVQKFQRAQEELAGM-RRCSETSSKLEEDKDEKINEMT---REVLKLK 894
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEpfyNEYLELK 608
|
..
gi 13507620 895 EA 896
Cdd:PRK03918 609 DA 610
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
8.68e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 8.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 13507620 121 TALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-897 |
1.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 593 EKAflfEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQL---YREAQAELEDYRKRKSLE 669
Cdd:COG1196 210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 670 DAAEYIHKAEHERLmhvsnlsrAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKEnsvsitEHLQVITTLRTTAKEMEEK 749
Cdd:COG1196 287 QAEEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 750 ISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQ 829
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13507620 830 ARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 897
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-239 |
4.00e-10 |
|
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: 63.49 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 88 SALHVAAKNGHPECIRKLLQYKSpaenIDNS-----GKTALHYAAAQGCLQAVQLLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPS----CDLFqrgalGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 158 VAVQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALH 223
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180
....*....|....*....|
gi 13507620 224 YSKLSENAGIQ----NLLLS 239
Cdd:cd22192 175 ILVLQPNKTFAcqmyDLILS 194
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
432-889 |
4.82e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTdtlclnntEISENGSDLSQKLKETQskYEEAMKEVLSVQkqmklgl 511
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRE--------RLEELEEERDDLLAEAG--LDDADAEAVEAR------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 lsQESADGyshlREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEK-EQAEATKPPAEACEELRSSYCSVIENM 590
Cdd:PRK02224 316 --REELED----RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELrEEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 591 NKEKAFLFEKYQQAQEEimklkdtlksqmpqeaPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQaelEDYRKRKSLED 670
Cdd:PRK02224 390 EEEIEELRERFGDAPVD----------------LGNAEDFLEELREERDELREREAELEATLRTAR---ERVEEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 671 AA------EYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKE-----NSVSITEHLqvITTL 739
Cdd:PRK02224 451 AGkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleERREDLEEL--IAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 740 RTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALAtKLKESVREREKAHSE 819
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 820 VAQVR------SEVSQARREKdniqtlLKAKEQEVTALVQKFQRAQEELAGMRRcsETSSKLEEDKDEKINEMTRE 889
Cdd:PRK02224 608 IERLRekrealAELNDERRER------LAEKRERKRELEAEFDEARIEEAREDK--ERAEEYLEQVEEKLDELREE 675
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-246 |
1.64e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 61.62 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 9 RKSDTNEWN-KNDDRLLQAVENG-DAEKVASLLgKKGASATKHDSEGKTAFHLAAA-KGHVECLKVMVTHGVDVTAQDSS 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 86 GHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYA-AAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNG- 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSsnTVDALIKKGADLS----LVDSLGHNALHYSKLSENAGIQNLLLS 239
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRH 532
|
....*..
gi 13507620 240 KISQDAD 246
Cdd:PHA02876 533 DIRNEVN 539
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
433-882 |
2.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 433 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDtlclnNTEISEngsdLSQKLKETQSKYEEAMKEVLSVQKQMKLgll 512
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----EERLEE----LKKKLKELEKRLEELEERHELYEEAKAK--- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 513 sQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN----KERVRELETKLAEKEQA-EATKPPAEAC----------- 576
Cdd:PRK03918 371 -KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELKKAiEELKKAKGKCpvcgrelteeh 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 577 -EELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELN-KQVSELSQLYRE 654
Cdd:PRK03918 450 rKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 655 AQAELEDYRKR-KSLEDAAEYIHKAEHERlmhvsnlsrAKSEEALSEMKSQYSKVLNELTQ------------LKQLVDA 721
Cdd:PRK03918 530 LKEKLIKLKGEiKSLKKELEKLEELKKKL---------AELEKKLDELEEELAELLKELEElgfesveeleerLKELEPF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 722 HKE-----NSVS-ITEHLQVITTLRTTAKEMEEKisaltghLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLqaSL 795
Cdd:PRK03918 601 YNEylelkDAEKeLEREEKELKKLEEELDKAFEE-------LAETEKRLEELRKELEELEKKYSEEEYEELREEYL--EL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 796 ESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEqEVTALVQKFQR--AQEELAGMRRCSETSS 873
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKykALLKERALSKVGEIAS 750
|
490
....*....|
gi 13507620 874 KL-EEDKDEK 882
Cdd:PRK03918 751 EIfEELTEGK 760
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
3.61e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 3.61e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 13507620 86 GHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
6.19e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 6.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 13507620 155 PLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALI 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
550-895 |
6.37e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 550 KERVRELETKLAEKEQAEatkpPAEACEELRSSYCSV---IENMNKEKAF----------LFEKYQQAQEEImklkDTLK 616
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKD----LHERLNGLESELAELdeeIERYEEQREQaretrdeadeVLEEHEERREEL----ETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 617 sqmpqEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAaeyihkaEHERL-MHVSNLSRAKSE 695
Cdd:PRK02224 258 -----AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDA-------DAEAVeARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 696 --EALSEMKSQYSKVLNELTQLKQLVDAHKENSvsitehlqviTTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE 773
Cdd:PRK02224 326 lrDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 774 EKAAVSDAMVPKSSYEKLQASLESEVNALATKLKE---SVREREKAHSEVAQVRSE------------------VSQARR 832
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRE 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507620 833 EKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCS------ETSSKLEEDKDEKINEMTREVLKLKE 895
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIErleerrEDLEELIAERRETIEEKRERAEELRE 544
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
638-933 |
9.62e-09 |
|
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: 59.69 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 638 IDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQ 717
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 718 LVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLES 797
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 798 EVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMR-RCSETSSKLE 876
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRID 939
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 877 EDKdEKINEmtREVLKLKEALNSLSQLSYSTSSSKRQSQQLDllqqqvkqlqNQLAE 933
Cdd:TIGR02168 940 NLQ-ERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRLE----------NKIKE 983
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
1.17e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.96 E-value: 1.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 72 MVTHG-VDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
435-858 |
1.45e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 435 LQDSLHDLQKRLES--SEAEK----KQLQDELQSQRTDTLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQmk 508
Cdd:COG1196 191 LEDILGELERQLEPleRQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 509 lgllsqesadgyshlreapadedIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEatkppaEACEELRSSYCSVIE 588
Cdd:COG1196 269 -----------------------LEELRLELEELELELEEAQAEEYELLAELARLEQDI------ARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 589 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEapddsgdmkEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSL 668
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL---------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 669 EDAAEYIHKAEHERLmhvsnlsRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEE 748
Cdd:COG1196 391 ALRAAAELAAQLEEL-------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 749 KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYE-KLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 827
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
410 420 430
....*....|....*....|....*....|.
gi 13507620 828 SQARREKDNIQTLLKAKEQEVTALVQKFQRA 858
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
432-896 |
2.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLqDELQSQRTDtLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 511
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKEL-EELKEEIEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 LSQESADGYSHLREAPAD------------EDIDTLKQDLQKAVEESARNKERVRELETKLAE-KEQAEATKPPAEACEE 578
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEyldelreiekrlSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 579 LRSsycsVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKEAMNRMIDELNKQVSELS----- 649
Cdd:PRK03918 367 AKA----KKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELKkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 650 --------------QLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHV----SNLSRAKS-EEALSEMKSQYSKV-L 709
Cdd:PRK03918 438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeSELIKLKElAEQLKELEEKLKKYnL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 710 NELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEE--------KAAVSDA 781
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKEL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 782 MVPKSSYEKLQASlESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTllKAKEQEVTALVQKFQRAQEE 861
Cdd:PRK03918 598 EPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRE 674
|
490 500 510
....*....|....*....|....*....|....*
gi 13507620 862 LAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEA 896
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-896 |
2.26e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 427 DNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQ--SQRTDTLCLNNTEISENGSDLSQKLKETQsKYEEAMKEVLSVQ 504
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAK 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 505 KQMKLGLLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN---KERVRELETKLAEKEQAEATKPPAE----ACE 577
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEedkkKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 578 ELRSSYCSvienmnKEKAflfEKYQQAQEEIMKlKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSElSQLYREAQA 657
Cdd:PTZ00121 1409 ELKKAAAA------KKKA---DEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 658 ELEDYRKRKSLEDAAEYIHKAEHErlMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVIT 737
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 738 TLRTT--AKEMEEKISALTG-HLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNAlatklkESVRERE 814
Cdd:PTZ00121 1556 ELKKAeeKKKAEEAKKAEEDkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------EELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 815 KAHSEVAQVRSEVSQARREKDNIQtllKAKEQEVTALVQKFQRAQEElagmRRCSETSSKLEEDKDEKINEMTREVLKLK 894
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELK---KAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
..
gi 13507620 895 EA 896
Cdd:PTZ00121 1703 KA 1704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
432-898 |
2.51e-08 |
|
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: 58.14 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTdtlclnntEISENGSDLS-QKLKETQSKYEEAMKEVLSVQKQMKLG 510
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQ--------EIEELLKKLEeAELKELQAELEELEEELEELQEELERL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 511 LLSQESADGyshlREAPADEDIDTLKQDLQKAVEESARNKERVRELETK-------LAEKEQAEATKPPAEACEELRSSY 583
Cdd:TIGR02168 460 EEALEELRE----ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvkalLKNQSGLSGILGVLSELISVDEGY 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 584 CSVIE-----NMNkekAFLFEKYQQAQEEIMKLKDT---------LKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELS 649
Cdd:TIGR02168 536 EAAIEaalggRLQ---AVVVENLNAAKKAIAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 650 QLYREAQAELEDYRKRKSLEDAAEYIHKAEHE---------------------RLMHVSNLSR----AKSEEALSEMKSQ 704
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsAKTNSSILERrreiEELEEKIEELEEK 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 705 YSKVLNELTQLKQlvdahkensvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAmvp 784
Cdd:TIGR02168 693 IAELEKALAELRK----------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL--- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 785 kssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREkdniqtlLKAKEQEVTALVQKFQRAQEELAG 864
Cdd:TIGR02168 760 ----EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELTLLNEEAANLRERLES 828
|
490 500 510
....*....|....*....|....*....|....
gi 13507620 865 MRRCSETSSKLEEDKDEKINEMTREVLKLKEALN 898
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-195 |
3.89e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.81 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 113 ENIDNSGKTALHYAAAQgCL--QAVQLLCEHKSPINLKD-LDGNIPLLVAVqngHSE-ACHFLLDHGADVNSRDKNGRTA 188
Cdd:PHA02878 228 DARDKCGNTPLHISVGY-CKdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTP 303
|
....*..
gi 13507620 189 LMLACET 195
Cdd:PHA02878 304 LSSAVKQ 310
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-898 |
1.10e-07 |
|
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: 56.22 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 426 TDNDVIIRQLQDSLHDLQKRLES--SEAEKKQLQDELQSQRTDTLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSV 503
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 504 QKQMKLGLLSQESADGY---SHLREAPADEDIDTLKQDLQKAVEESARNKERVRELETKL---------AEKEQAEATKP 571
Cdd:TIGR02168 350 KEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerledrrerLQQEIEELLKK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 572 PAEACEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEApddsGDMKEAMNRmIDELNKQVSELSQL 651
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE----RELAQLQAR-LDSLERLQENLEGF 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 652 YREAqAELEDYRKRKS---------LEDAAEY---IHKAEHERLMH--VSNLSRAKSE-EALSEMKSQYSKVLnELTQLK 716
Cdd:TIGR02168 505 SEGV-KALLKNQSGLSgilgvlselISVDEGYeaaIEAALGGRLQAvvVENLNAAKKAiAFLKQNELGRVTFL-PLDSIK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 717 --QLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLA------------------------------------ 758
Cdd:TIGR02168 583 gtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnalelakklrpgyrivtldgdlvrpggvit 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 759 -----------NKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 827
Cdd:TIGR02168 663 ggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 828 SQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAgmrRCSETSSKLEEDkdekINEMTREVLKLKEALN 898
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELA---EAEAEIEELEAQ----IEQLKEELKALREALD 806
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
621-897 |
1.13e-07 |
|
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: 56.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 621 QEAPDDSGDMKEAMNRMIDELNKQ---VSELSQLYREAQAELEDYRKRKS------------LEDAAEYIHKAEHERLMH 685
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEqleqeeeklkerLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 686 VSNLsrAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKensvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVA 765
Cdd:TIGR02169 757 KSEL--KELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 766 KLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKE---SVREREKAH----SEVAQVRSEVSQARREKDNIQ 838
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaALRDLESRLgdlkKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 839 TLLKAKEQEVTALVQKFQRAQEELA--GMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 897
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
432-898 |
1.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLclnntEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQM--KL 509
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELE-----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 510 GLLSQESADGYSHLREA-PADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQA-EATKPPAEACEELRSSYCSVI 587
Cdd:COG1196 379 EELEELAEELLEALRAAaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 588 ENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQA 657
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLeelaeaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 658 ELEDY-------RKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSIT 730
Cdd:COG1196 539 ALEAAlaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 731 EHLQVITTLRTTAKEMEEKISALTGHlankEAEVAKLEKQLAEEKAAVSDAmvpksSYEKLQASLESEVNALATKLKESV 810
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAG----RLREVTLEGEGGSAGGSLTGG-----SRRELLAALLEAEAELEELAERLA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 811 REREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREV 890
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*...
gi 13507620 891 LKLKEALN 898
Cdd:COG1196 770 ERLEREIE 777
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
51-227 |
1.87e-07 |
|
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: 55.09 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSpaeNIDNSGKTALHyAAA 128
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLS---CRGAVGDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 129 QGCLQAVQLLCEHKSPINLKDLD--------------GNIPLLVAVQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13507620 184 ---NGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKL 227
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
1.98e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.90 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 13507620 68 CLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
432-724 |
1.98e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRtDTLCLNNTEISENGS---DLSQKLKETQSK---YEEAMKEVLSVQK 505
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 506 QMKLGLLSQESADGYSHLREAPADEDIDTLKQDLQK-AVEESARNK-ERVRELETKLA-EKEQAEATKPPAEACEELRSs 582
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlSVADAARRQfEKAYELVCKIAgEVERSQAWQTARELLRRYRS- 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 583 YCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAE 658
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507620 659 LEDYR-KRKSLEDAAEYIHKAEH--ERLMHVSNLSRAKSEEALSEMKSQYSKvLNELTQLKQLVDAHKE 724
Cdd:COG3096 587 LEQLRaRIKELAARAPAWLAAQDalERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-224 |
2.03e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 2.03e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 13507620 171 LLDHG-ADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHY 224
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
433-859 |
2.59e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 433 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDtlcLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSV-QKQMKLGL 511
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL---LQLLPLYQELEALEAELAELPERLEELEERLEELrELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 LSQESADGYSHLREAPADEDIDTLKQdLQKAVEESARNKERVRELETKLAEKEqaeatkppaEACEELRSSYCSVIENMN 591
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQRLAELEEELEEAQ---------EELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 592 KEKafLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELnkqVSELSQLYREAQAELEDYRKRKSLEDA 671
Cdd:COG4717 238 AAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 672 AEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLvdahkENSVSITEHLQVITTLRTTAK----EME 747
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----EEELQLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 748 EKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSsyeklQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 827
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....
gi 13507620 828 SQARREK--DNIQTLLKAKEQEVTALVQKFQRAQ 859
Cdd:COG4717 463 EQLEEDGelAELLQELEELKAELRELAEEWAALK 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
434-878 |
2.65e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 434 QLQDSLHDLQKRLESSEAEKKQLQDElqsqrtdtlclnNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglls 513
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIK----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 514 qesadgyshlreaPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQA-----------EATKPPAE----ACEE 578
Cdd:pfam01576 135 -------------KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKakslsklknkhEAMISDLEerlkKEEK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 579 LRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-----QMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQ--- 650
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALARLEEETAQKNNALKKIRELEAQISELQEdle 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 651 LYREAQAELEDYRK---------RKSLED-----AAEYIHKAEHERlmHVSNLSRAKSEEA------LSEMKSQYSKVLN 710
Cdd:pfam01576 282 SERAARNKAEKQRRdlgeelealKTELEDtldttAAQQELRSKREQ--EVTELKKALEEETrsheaqLQEMRQKHTQALE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 711 ELT-QLKQLvdahKENSVSITEHLQVittLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYE 789
Cdd:pfam01576 360 ELTeQLEQA----KRNKANLEKAKQA---LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 790 KLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQAR-------REKDNIQTLLKAKEQEVTALVQKFQRAQEEL 862
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512
|
490 500
....*....|....*....|....
gi 13507620 863 AGMRR--------CSETSSKLEED 878
Cdd:pfam01576 513 RNVERqlstlqaqLSDMKKKLEED 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
528-896 |
3.49e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 528 ADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAtkppaeaceELRSSYCSVIENMNKEKAFL--FEKYQQAQ 605
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES---------DLEQDYQAASDHLNLVQTALrqQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 606 EEIMKLKDTLKSQM-----PQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEyihkaeh 680
Cdd:PRK04863 355 ADLEELEERLEEQNevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAK------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 681 eRLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTL---------RTTAKEME---E 748
Cdd:PRK04863 428 -QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIagevsrseaWDVARELLrrlR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 749 KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAmvpkSSYEK---LQASLESEVNALATKLKESVREREKAHSEVAQVRS 825
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL----AEFCKrlgKNLDDEDELEQLQEELEARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13507620 826 EVSQARREkdniqtlLKAKEQEVTALVQKFQRAQEELAGMRRCS----ETSSKLEE---DKDEKINEMTREVLKLKEA 896
Cdd:PRK04863 583 ALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSgeefEDSQDVTEymqQLLERERELTVERDELAAR 653
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
100-238 |
4.09e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 100 ECIRKLLQYKSPAENID-NSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADV 178
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507620 179 NSRDKNGRTALMLAceTGSSNTVDA---LIKKGADLSLVDS-LGHNALHYSKLSENagIQNLLL 238
Cdd:PHA02878 228 DARDKCGNTPLHIS--VGYCKDYDIlklLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLL 287
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
162-259 |
4.43e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 162 NGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSKI 241
Cdd:PTZ00322 92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
90
....*....|....*...
gi 13507620 242 SQDADLKTPTKPKQHDQV 259
Cdd:PTZ00322 172 QCHFELGANAKPDSFTGK 189
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
145-240 |
4.66e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 145 INLKDLDGNIPLLVAVQNGHS---EACHFLLDHGADVNSRDKNGRTALMLACETGSS-NTVDALIKKGADLSLVDSLGHN 220
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRT 119
|
90 100
....*....|....*....|..
gi 13507620 221 ALH-Y-SKLSENAGIQNLLLSK 240
Cdd:PHA03095 120 PLHvYlSGFNINPKVIRLLLRK 141
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
637-896 |
6.90e-07 |
|
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: 53.53 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 637 MIDELNKQVSELsqlyREAQAELEDYRK-RKSLEDAAEYIH---KAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNEL 712
Cdd:TIGR02169 192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 713 TQLKQLVDAHKENSVSITEHLQVitTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVS--DAMVPKS---- 786
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDklLAEIEELerei 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 787 -SYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGM 865
Cdd:TIGR02169 346 eEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
250 260 270
....*....|....*....|....*....|....*
gi 13507620 866 R----RCSETSSKLEEDKDEKINEMTREVLKLKEA 896
Cdd:TIGR02169 426 NaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-83 |
7.07e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 7.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQD 83
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
132-240 |
8.72e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.53 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 132 LQAVQLLCEHKSPINLKDLDGNIPLLVAVQN----GHS-EACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDAL-- 204
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 13507620 205 -IKKGADLSLVDSLGHNALH-YSKLSENAGIQ--NLLLSK 240
Cdd:PHA02798 131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
621-858 |
1.09e-06 |
|
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: 52.07 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 621 QEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRksLEDAAEYIHKAEHERLMHVSNLSRAKSEEA--- 697
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIRALEQELAALEAELAELEKEIAelr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 698 --LSEMKSQYSKVLNELTQLKQLVD-AHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLankeAEVAKLEKQLAEE 774
Cdd:COG4942 97 aeLEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 775 KAAVsdamvpkssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQK 854
Cdd:COG4942 173 RAEL----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 13507620 855 FQRA 858
Cdd:COG4942 243 TPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
496-895 |
1.31e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 496 AMKEVLSVQKQMKLGLLSQ----ESADGYSHL-----REAPADEDIDTL-------KQDLQKAVEESARNKERVRELETK 559
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQieekEEKDLHERLnglesELAELDEEIERYeeqreqaRETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 560 LAEKEQAEATKPPAE---------------ACEELRSSYCSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSQMPQEAP 624
Cdd:PRK02224 257 EAEIEDLRETIAETErereelaeevrdlreRLEELEEERDDLLAEAGLDDADA-EAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 625 DDSGDMKEAMN--RMIDELNKQVSELSQLYREAQAELEDYRK-------------------RKSLEDAAEYIHKAEHERL 683
Cdd:PRK02224 336 AAQAHNEEAESlrEDADDLEERAEELREEAAELESELEEAREavedrreeieeleeeieelRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 684 MHVSNLSRAKSEEAlsEMKSQYSKVLNELTQLKQLVDAHK----ENSVSITEHLQVITtlrttakEMEEKISALTGHLAN 759
Cdd:PRK02224 416 ELREERDELREREA--ELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIE-------EDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 760 KEAEVAKLEKQLAEEKAAVsdamvpkssyeklqaSLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQT 839
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13507620 840 LLKAKEQEVTALVQKFQRAQEELAGM-RRCSETSSKLE-----EDKDEKINEMTREVLKLKE 895
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERLRE 613
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
432-896 |
1.57e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGSDLSQKL-KETQSKYEEAMKEVLSVQKQMKLG 510
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 511 LlsQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN---------KERVRELETKLAEKEQAEATKPPAEACEELRS 581
Cdd:TIGR00618 461 L--QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLelqeepcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 582 SYCSVIENMnkekaflfekYQQAQEEIMKLKdTLKSQMpQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEd 661
Cdd:TIGR00618 539 QLETSEEDV----------YHQLTSERKQRA-SLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE- 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 662 YRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEaLSEMKSQYSKVLNELTQLKQlvdahKENSVSITE-HLQVITTLR 740
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-LALKLTALHALQLTLTQERV-----REHALSIRVlPKELLASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 741 TTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREkahsEV 820
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR----TV 755
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 821 AQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEA 896
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
491-886 |
1.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 491 SKYEEAMKEVLSVQKQmKLGLLSQESADGYSHLREAPADED-IDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAT 569
Cdd:COG4717 49 ERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEeYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 570 KPPAEACEELRSSYCSVIENMNKEKA------FLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRmIDELNK 643
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEErleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 644 QVSELSQLYREAQAELEDYRKR-KSLEDAAEyihkaeherlmhvsnlsRAKSEEALSEMKSQYsKVLNELTQLKQLVDAH 722
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEElEQLENELE-----------------AAALEERLKEARLLL-LIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 723 KENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEK-QLAEEKAAVSDAMVPkssyeklqaslESEVNA 801
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP-----------PDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 802 LATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDE 881
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
....*
gi 13507620 882 KINEM 886
Cdd:COG4717 418 LEELL 422
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-206 |
1.91e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 127 AAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIK 206
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-93 |
1.95e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.95e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 13507620 50 DSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVA 93
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
91-185 |
2.13e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 91 HVAAkNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF 170
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 13507620 171 LLDHGADVNSRDKNG 185
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
2.20e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 105 LLQYKSPAENI-DNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVA 159
Cdd:pfam13857 1 LLEHGPIDLNRlDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
19-220 |
2.31e-06 |
|
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: 51.55 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTH-----GVDVTAQDSSGHSALHVA 93
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 94 AKNGHPECIRKLLQY----KSP----------AENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPL-LV 158
Cdd:cd22192 97 VVNQNLNLVRELIARgadvVSPratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 159 AVQNGHSEACH---FLLDHGADVNS------RDKNGRTALMLACETGSSNTVDALIKKGA--------------DLSLVD 215
Cdd:cd22192 177 VLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKRRhiqwtygpltstlyDLTEID 256
|
....*
gi 13507620 216 SLGHN 220
Cdd:cd22192 257 SWGDE 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
690-867 |
2.35e-06 |
|
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: 50.92 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 690 SRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEK 769
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 770 QLAEEKAAVSDAMV----------------PKSS---------YEKLQASLESEVNALATKLKESVREREKAHSEVAQVR 824
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllsPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13507620 825 SEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 867
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
638-863 |
2.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 638 IDELNKQVSELSQLYREAqaeLEDYRKRKSLEDAAEYI--HKAEHERLMHVSNLSRA----KSEEALSEMKSQYSKVLNE 711
Cdd:COG4913 227 ADALVEHFDDLERAHEAL---EDAREQIELLEPIRELAerYAAARERLAELEYLRAAlrlwFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 712 LTQLKQLVDAHKENSVSITEHLQVITTLRTTA-----KEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAmvpKS 786
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 787 SYEKLQAslesEVNALATKLKEsvrEREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 863
Cdd:COG4913 381 EFAALRA----EAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-141 |
2.57e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLKVMVTHGVDVTAQDSSG 86
Cdd:PTZ00322 43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 13507620 87 HSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-238 |
2.72e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.76 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 60 AAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLC 139
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 140 EHKSPINlkDL---DGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDS 216
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180
....*....|....*....|..
gi 13507620 217 LGHNALHYSKLSENAGIQNLLL 238
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLL 188
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
3.09e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 3.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507620 189 LMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSKISQDADLKTPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-898 |
3.52e-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: 51.22 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENG--SDLSQKLKETQSKYEEAMKEVLSVQKQmkl 509
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrDKLTEEYAELKEELEDLRAELEEVDKE--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 510 gllSQESADGYSHLREAPAD--EDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAtkppaeaceELRSsycsvi 587
Cdd:TIGR02169 380 ---FAETRDELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN---------ELEE------ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 588 enmnkEKAFLFEKYQQAQEEIMKLKDTLKSqmpqeAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKS 667
Cdd:TIGR02169 442 -----EKEDKALEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 668 ----LEDAAEYIH---------KAEHERLMHVSNLSRAKS----EEALSEMKSQYSKV----------LNELTQLKQLVD 720
Cdd:TIGR02169 512 veevLKASIQGVHgtvaqlgsvGERYATAIEVAAGNRLNNvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 721 AHKENSVsITEHLQVIT-----------TLRTTAkeMEEKISALTGHLANkeAEVAKLEKQLAEEKAAVSDAMVPKSSYE 789
Cdd:TIGR02169 592 ILSEDGV-IGFAVDLVEfdpkyepafkyVFGDTL--VVEDIEAARRLMGK--YRMVTLEGELFEKSGAMTGGSRAPRGGI 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 790 KLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAG-MRRC 868
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEElEEDL 746
|
490 500 510
....*....|....*....|....*....|....*.
gi 13507620 869 SETSSKLEEDKDE------KINEMTREVLKLKEALN 898
Cdd:TIGR02169 747 SSLEQEIENVKSElkeleaRIEELEEDLHKLEEALN 782
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-240 |
4.64e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.22 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHP---ECIRKLLQY 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 109 KSPAENIDNS-GKTALH--YAAAQGCLQA--VQLLCEHKSPINLKD-------LDGNIPLLVAVQNGHSEACHFLLDHgA 176
Cdd:PHA02798 171 GVDINTHNNKeKYDTLHcyFKYNIDRIDAdiLKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507620 177 DVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
520-867 |
7.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 520 YSHLREAPA------DEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKP-------PAEACEELRSSycsv 586
Cdd:PRK04863 770 YSRFPEVPLfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadPEAELRQLNRR---- 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 587 IENMNKEKAFLFEKYQQAQEEImklkDTLKSQMpqeapddsgdmkEAMNRMIDELNK-QVSELSQLYREAQAELEdyrkr 665
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQL----EQAKEGL------------SALNRLLPRLNLlADETLADRVEEIREQLD----- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 666 kSLEDAAEYI--HKAEHERLMHVSNLSRAkSEEALSEMKSQYSKVLNELTQLKQLVDAHKEnSVSITEHLQVITTLRTTA 743
Cdd:PRK04863 905 -EAEEAKRFVqqHGNALAQLEPIVSVLQS-DPEQFEQLKQDYQQAQQTQRDAKQQAFALTE-VVQRRAHFSYEDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 744 KEmEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDamvpkssYEKLQASLESEVNALATKLKESVRE----------- 812
Cdd:PRK04863 982 KN-SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ-------YNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsg 1053
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 813 -REKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 867
Cdd:PRK04863 1054 aEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
432-895 |
9.00e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 508
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 509 LGLLSQESADGYS-------------HLREAPAD-EDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAE 574
Cdd:TIGR00606 666 SQFITQLTDENQSccpvcqrvfqteaELQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 575 aCEELRSSYCSVIENMNKEKAFLFEKYQQ-----AQEEI---------------MKLKDTLKSQMPQEAPDDSGDmkeaM 634
Cdd:TIGR00606 746 -IPELRNKLQKVNRDIQRLKNDIEEQETLlgtimPEEESakvcltdvtimerfqMELKDVERKIAQQAAKLQGSD----L 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 635 NRMIDELNKQVSELSQLYREAQAELEDYRK-----RKSLEDAAEYIHKAEHERLMHVSNLSRA-----KSEEALSEMKSQ 704
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdqQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfeeQLVELSTEVQSL 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 705 YSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKaavsdamvp 784
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKD---QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK--------- 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 785 kssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV-SQARRE---KDNIQtlLKAKEQEVTALVQKFQRAQE 860
Cdd:TIGR00606 969 ----DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdTQKIQErwlQDNLT--LRKRENELKEVEEELKQHLK 1042
|
490 500 510
....*....|....*....|....*....|....*..
gi 13507620 861 ELAGMRRCSETSS--KLEEDKDEKINEMTREVLKLKE 895
Cdd:TIGR00606 1043 EMGQMQVLQMKQEhqKLEENIDLIKRNHVLALGRQKG 1079
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-863 |
9.03e-06 |
|
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: 49.67 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 629 DMKEAMNRMID---ELNKQVSELsqlyrEAQAEL-EDYR-KRKSLEDAAEYIHKAEHERLmhvsnlsrakseealsemKS 703
Cdd:TIGR02168 183 RTRENLDRLEDilnELERQLKSL-----ERQAEKaERYKeLKAELRELELALLVLRLEEL------------------RE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 704 QYSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMV 783
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 784 PKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 863
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
1.30e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.30e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 13507620 145 INLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
435-898 |
1.57e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 435 LQDSLHDLQKRLESSEAEKKQLQD----ELQSQRTDTLCLNNT--EISENGSDLSQKLKETQSKYEEAMKEVLS---VQK 505
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADirrrESQSQEDLRNQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLShegVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 506 QMKLGLLSQESADGyshlREAPADEDIDTLK-QDLQKAVEESarnkerVRELETKLAE--------KEQAEATKPPAE-A 575
Cdd:pfam15921 188 EIRSILVDFEEASG----KKIYEHDSMSTMHfRSLGSAISKI------LRELDTEISYlkgrifpvEDQLEALKSESQnK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 576 CEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMP--QEAPDDSGDMkeaMNRMIDELNKQVSELSQLYR 653
Cdd:pfam15921 258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiQEQARNQNSM---YMRQLSDLESTVSQLRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 654 EA----QAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSI 729
Cdd:pfam15921 335 EAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 730 tEHL-----------QVITTLRTTAK-----EMEEKISALTGHLANKEaEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQA 793
Cdd:pfam15921 415 -DHLrrelddrnmevQRLEALLKAMKsecqgQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 794 SLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQT---LLKAKEQEVTALVQKFQRAQEELAGMRRCSE 870
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
490 500
....*....|....*....|....*...
gi 13507620 871 TSSKLEEDKDEKINEMTREVLKLKEALN 898
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
432-863 |
1.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLclnNTEISENGSDLS---QKLKETQSKYEEAMKEVLSVQKQMk 508
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELL---EAELEELRAELArleAELERLEARLDALREELDELEAQI- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 509 lgllsqeSADGYShlREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppAEACEELRSSYCSVIE 588
Cdd:COG4913 333 -------RGNGGD--RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL--RAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 589 NMNKEKAFLFEKYQQAQEEIMKLKDTL------KSQMPQEapddsgdMKEAMNRMIDELNKQVSELSQLyreaqAEL--- 659
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIaslerrKSNIPAR-------LLALRDALAEALGLDEAELPFV-----GELiev 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 660 --EDYRKRKSLE------------------DAAEYI---HKAEHERLMHVSNLSRAKSEEALSE------MKSQYSKVLN 710
Cdd:COG4913 470 rpEEERWRGAIErvlggfaltllvppehyaAALRWVnrlHLRGRLVYERVRTGLPDPERPRLDPdslagkLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 711 EL-TQLKQLVDAHKENSV--------SITEHLQVitTLRTTAKEM----------------EEKISALTGHLANKEAEVA 765
Cdd:COG4913 550 WLeAELGRRFDYVCVDSPeelrrhprAITRAGQV--KGNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 766 KLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATK-----LKESVREREKAHSEVAQVRSEVSQARREKDNIQTL 840
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
490 500
....*....|....*....|...
gi 13507620 841 LKAKEQEVTALVQKFQRAQEELA 863
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELD 730
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
52-81 |
2.20e-05 |
|
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: 42.19 E-value: 2.20e-05
10 20 30
....*....|....*....|....*....|
gi 13507620 52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-183 |
2.76e-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: 41.89 E-value: 2.76e-05
10 20 30
....*....|....*....|....*....|....
gi 13507620 151 DGNIPLLVAV-QNGHSEACHFLLDHGADVNSRDK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-863 |
2.76e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 707 KVLNELTQLKQLVDAHKEnsvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKS 786
Cdd:COG1579 14 ELDSELDRLEHRLKELPA---ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 787 sYEKLQ---ASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 863
Cdd:COG1579 91 -YEALQkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
532-886 |
3.28e-05 |
|
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: 47.89 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 532 IDTLKQDLQKAVEE--------------SARNKERVRELETKLAEKEQAEATkppaeaceeLRSSYCSVIENMNKEKAFL 597
Cdd:pfam10174 291 IDQLKQELSKKESEllalqtkletltnqNSDCKQHIEVLKESLTAKEQRAAI---------LQTEVDALRLRLEEKESFL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 598 FEKYQQAQEeIMKLKDTLKSQMpqeapDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAAEyih 676
Cdd:pfam10174 362 NKKTKQLQD-LTEEKSTLAGEI-----RDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERvKSLQTDSS--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 677 kaeherlmhVSNLSRAKSEEALSEMKsqysKVLNELTQLKQLVDahkensvsiTEHLQVITTLRTTAKEMEEKISALTGH 756
Cdd:pfam10174 433 ---------NTDTALTTLEEALSEKE----RIIERLKEQRERED---------RERLEELESLKKENKDLKEKVSALQPE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 757 LANKEAEVAKLEkqlaEEKAAVSDAMVPKSSYEK-LQASLES---EVNALATKLKesvrereKAHsevaqvrsEVSQARR 832
Cdd:pfam10174 491 LTEKESSLIDLK----EHASSLASSGLKKDSKLKsLEIAVEQkkeECSKLENQLK-------KAH--------NAEEAVR 551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 833 EKDNIQTLLKAKEQEVTALVQKFQRAQ---EELAGMRRCSETSsklEEDKDEKINEM 886
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKAQaevERLLGILREVENE---KNDKDKKIAEL 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
488-940 |
3.44e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 488 ETQSKYEEAMKEVLSVQKQMKLgllsqESADGYSHLREAPADEDiDTLKQDLQKAveESARNKERVRELEtklaEKEQAE 567
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEA-----RKAEDARKAEEARKAED-AKRVEIARKA--EDARKAEEARKAE----DAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 568 ATKPPAEA--CEELRSSYcsviENMNKEKAFLFEKYQQAqEEIMKLKDTLKSQMPQEAPDDSGDMKEAMN----RMIDEL 641
Cdd:PTZ00121 1180 AARKAEEVrkAEELRKAE----DARKAEAARKAEEERKA-EEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeeRNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 642 NKQVSELSQLYREAQAELEDYRKRKsledaAEYIHKAEHERlmhvsnlsraKSEEAlseMKSQYSKVLNELTQLKQLVDA 721
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARK-----ADELKKAEEKK----------KADEA---KKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 722 HKENSVSITEHLQVITTLRTTAKEMEEKISAltghlANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNA 801
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEA-----AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 802 LATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA-LVQKFQRAQEELAGMRRCSETSSKLEE-DK 879
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEaKK 1471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 880 DEKINEMTREVLKLKEALNSLSQLSYSTSSSKRQSQQLDLLQQQVKQLQNQLAECKKHHQE 940
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-720 |
4.36e-05 |
|
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: 47.76 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 431 IIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDT----LCLNNTEISENGSdlsqKLKETQSKYEEAMKEVLSVQKQ 506
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleEALNDLEARLSHS----RIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 507 mklgLLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARNKERV-------RELETKLAEKEQAEatkppaeacEEL 579
Cdd:TIGR02169 814 ----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkkEELEEELEELEAAL---------RDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 580 RSSYCSV---IENMNKEKAFLFEKYQQAQEEIMKLKDTLKsqmpqeapddsgDMKEAmnrmideLNKQVSELSQLYREAQ 656
Cdd:TIGR02169 881 ESRLGDLkkeRDELEAQLRELERKIEELEAQIEKKRKRLS------------ELKAK-------LEALEEELSEIEDPKG 941
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13507620 657 AELEDYRKRKSLEDAAEYIHKAEHE--RLMHVSNLS---RAKSEEALSEMKSQYSKVLNELTQLKQLVD 720
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEirALEPVNMLAiqeYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
631-897 |
5.95e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 631 KEAMNRM-------------IDELNKQVSELS------QLYREAQAELEDYrkrksleDAAEYIHKAEHERLmhvsNLSR 691
Cdd:COG1196 175 EEAERKLeateenlerlediLGELERQLEPLErqaekaERYRELKEELKEL-------EAELLLLKLRELEA----ELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 692 AKSEEALSEMKsqyskvLNELTQLKQLVDAHKEnsvsitehlqvitTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQL 771
Cdd:COG1196 244 LEAELEELEAE------LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 772 AEEkaavsdamvpkssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTAL 851
Cdd:COG1196 305 ARL--------------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 13507620 852 VQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 897
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
447-843 |
7.70e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.59 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 447 ESSEAEKK--QLQDELQSQRTdtlclNNTEISENGSDLSQKLKETQSKYEEAMKevlsvqKQMKLGLLSQESADGYSHLR 524
Cdd:pfam13166 90 ESIEIQEKiaKLKKEIKDHEE-----KLDAAEANLQKLDKEKEKLEADFLDECW------KKIKRKKNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 525 EAPADE-DIDTLKQDLQKAVEESarNKERVRELETKLAEKEQAEATKPP--------AEACEELRSS---YCSVIENMNK 592
Cdd:pfam13166 159 EANFKSrLLREIEKDNFNAGVLL--SDEDRKAALATVFSDNKPEIAPLTfnvidfdaLEKAEILIQKvigKSSAIEELIK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 593 EkAFLFEKYQQAQEEIMKLKDTL---KSQMPQEA--------PDDSGDMKEAMNRMIDELNKQVSELSQLYreaQAELED 661
Cdd:pfam13166 237 N-PDLADWVEQGLELHKAHLDTCpfcGQPLPAERkaaleahfDDEFTEFQNRLQKLIEKVESAISSLLAQL---PAVSDL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 662 YRKRKSLEDAAEYIHKAEHERLMHVSNLSR---AKSEEALSEmkSQYSKVLNELTQLKQLVDAhkensvsitehlqvitt 738
Cdd:pfam13166 313 ASLLSAFELDVEDIESEAEVLNSQLDGLRRaleAKRKDPFKS--IELDSVDAKIESINDLVAS----------------- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 739 lrttakeMEEKISALTGHLANKEAEVAKLEKQLaeEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHS 818
Cdd:pfam13166 374 -------INELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLRE 444
|
410 420
....*....|....*....|....*
gi 13507620 819 EVAQVRSEVSQARREKDNIQTLLKA 843
Cdd:pfam13166 445 EIKELEAQLRDHKPGADEINKLLKA 469
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
698-847 |
1.49e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 698 LSEMKSQYSKVLNELT-QLKQLVDAhkensvsitehlqvITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKA 776
Cdd:PRK09039 44 LSREISGKDSALDRLNsQIAELADL--------------LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 777 AVSDAmvpkssyeklqaslESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQE 847
Cdd:PRK09039 110 AGAAA--------------EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKR 166
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
1.74e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 13507620 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMV 73
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-179 |
2.08e-04 |
|
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: 39.11 E-value: 2.08e-04
10 20
....*....|....*....|....*....
gi 13507620 151 DGNIPLLVAVQNGHSEACHFLLDHGADVN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-790 |
2.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 450 EAEKKQLQDELQSQrtdtlclnnTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGllSQESADGYSHLREAPAD 529
Cdd:PTZ00121 1465 KAEEAKKADEAKKK---------AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 530 EDIDTLK--QDLQKAVE----ESARNKERVRELETKLAEKEQAEATKPPAEACEEL-RSSYCSVIENMNKEKAFLFEKYQ 602
Cdd:PTZ00121 1534 KKADEAKkaEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAK 1613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 603 QAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQvSELSQLYREAQAELEDYRKRKsledaAEYIHKAEHEr 682
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKK-----AEEAKKAEED- 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 683 lmhvsnlsRAKSEEALSEMKSQYSKVlnELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHL----A 758
Cdd:PTZ00121 1687 --------EKKAAEALKKEAEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeeK 1756
|
330 340 350
....*....|....*....|....*....|..
gi 13507620 759 NKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEK 790
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
129-232 |
2.43e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.05 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 129 QGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKG 208
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100
....*....|....*....|....*....
gi 13507620 209 A-----DLSLVDSLGHNALHYSKLSENAG 232
Cdd:PHA02876 235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
432-624 |
2.77e-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: 44.37 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELQ------SQRTDTLCLNNTEISENGSDLSQ------KLKETQSKYEEAMKE 499
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAalerriAALARRIRALEQELAALEAELAElekeiaELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 500 VLSV------QKQMKLGLLSQESADGYSHLRE----APADED-IDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEA 568
Cdd:COG4942 109 LLRAlyrlgrQPPLALLLSPEDFLDAVRRLQYlkylAPARREqAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 569 TKppaeacEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAP 624
Cdd:COG4942 189 AL------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-189 |
2.80e-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: 44.87 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 64 GHVECLKVMVTHgvDVTAQDSSGHSALHVAA---KNGHPECIRKLLQ----YKSPAENIDNS-------GKTALHYAAAQ 129
Cdd:cd21882 6 GLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEaapdSGNPKELVNAPctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 130 GCLQAVQLLCEH--------------KSPINLKDLdGNIPLLVAVQNGHSEACHFLLDHGADVNS---RDKNGRTAL 189
Cdd:cd21882 84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVL 159
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
3.06e-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: 38.81 E-value: 3.06e-04
10 20 30
....*....|....*....|....*....|...
gi 13507620 52 EGKTAFHLAAAK-GHVECLKVMVTHGVDVTAQD 83
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
100-223 |
3.26e-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: 44.49 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 100 ECIRKLLQ---YKSPAenidnSGKTALHYAA---AQGCLQAVQLLCE-HKSPINLKDL----------DGNIPLLVAVQN 162
Cdd:cd21882 9 ECLRWYLTdsaYQRGA-----TGKTCLHKAAlnlNDGVNEAIMLLLEaAPDSGNPKELvnapctdefyQGQTALHIAIEN 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 163 GHSEACHFLLDHGADVNSR------DKNGRTA-------LMLACETGSSNTVDALIKKGAD---LSLVDSLGHNALH 223
Cdd:cd21882 84 RNLNLVRLLVENGADVSARatgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-213 |
3.40e-04 |
|
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: 38.72 E-value: 3.40e-04
10 20 30
....*....|....*....|....*....|
gi 13507620 184 NGRTALMLACETGSSNTVDALIKKGADLSL 213
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
557-831 |
3.57e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 557 ETKLA-EKEQAEATKPP--AEACEELRSSYCSVIENmnKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEaPDDSGDMKEA 633
Cdd:PRK10929 25 EKQITqELEQAKAAKTPaqAEIVEALQSALNWLEER--KGSLERAKQYQQVIDNFPKLSAELRQQLNNE-RDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 634 MNrmIDELNKQV----SELSQLYREAQAELEDYRK-RKSL-------EDAAEYIHKAEhERLMHVSN----LSRAKSEEA 697
Cdd:PRK10929 102 MS--TDALEQEIlqvsSQLLEKSRQAQQEQDRAREiSDSLsqlpqqqTEARRQLNEIE-RRLQTLGTpntpLAQAQLTAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 698 LSEMKSQYSKVlNELtQLKQLVDAHKensvsitehlQVITTLRT-TAKEMEEKISALTGHLAN-------KEAEVAkLEK 769
Cdd:PRK10929 179 QAESAALKALV-DEL-ELAQLSANNR----------QELARLRSeLAKKRSQQLDAYLQALRNqlnsqrqREAERA-LES 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13507620 770 --QLAEEKAAvsdamVPKSSYEKLQAS--LESEVNALATKLKESVREREKAHSEVAQVRSEVSQAR 831
Cdd:PRK10929 246 teLLAEQSGD-----LPKSIVAQFKINreLSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLR 306
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
665-896 |
3.76e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 665 RKSLEDAAEYIHKAEherLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHK-----ENSVSITEHLQVITTL 739
Cdd:PRK05771 15 KSYKDEVLEALHELG---VVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 740 RTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE-----------------EKAAVSDAMVPKSSYEKLQASLESEVNAL 802
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 803 ATKLKESV-------REREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAgmrrcsETSSKL 875
Cdd:PRK05771 172 ISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELK------ELAKKY 245
|
250 260
....*....|....*....|....*
gi 13507620 876 EEDK---DEKI-NEMTREVLKLKEA 896
Cdd:PRK05771 246 LEELlalYEYLeIELERAEALSKFL 270
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
434-861 |
3.87e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 434 QLQDSLHDLQKRLESSEAEKKQlqdelQSQRTDTLCLNNTEISENGSDLSQKLKETQsKYEEAMKEVLS-----VQKQMK 508
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQ-----NKRLWDRDTGNSITIDHLRRELDDRNMEVQ-RLEALLKAMKSecqgqMERQMA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 509 LGLLSQESADGYSHLreapaDEDIDTLKQDLQKAVEE------SARNKER-VRELETKLAEKEQA-EATKPPAEACEELR 580
Cdd:pfam15921 452 AIQGKNESLEKVSSL-----TAQLESTKEMLRKVVEEltakkmTLESSERtVSDLTASLQEKERAiEATNAEITKLRSRV 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 581 SSYCSVIENMNKEKAFLfeKYQQAQEEIMKLKDTLK--------------SQMPQEAPDDSGDM---KEAMNRMIDELNK 643
Cdd:pfam15921 527 DLKLQELQHLKNEGDHL--RNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMqveKAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 644 QVSELSQLYREAQAELEDYRKRKS-LEDAAEYIHKAEHERLMHVSNLSRAKsEEALSEMKSQYskvlNELTQLKQLVDAH 722
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEARVSdLELEKVKLVNAGSERLRAVKDIKQER-DQLLNEVKTSR----NELNSLSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 723 KENSVSITEHLQVITT-----LRTTAKEMEEK---ISALTGHLANKEAEVAKLEKQLAEEKAAVsDAMVPKSSY------ 788
Cdd:pfam15921 680 KRNFRNKSEEMETTTNklkmqLKSAQSELEQTrntLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQSKIQFleeamt 758
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13507620 789 --EKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEE 861
Cdd:pfam15921 759 naNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
432-683 |
4.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQDELqsqrtdtlclnnteisengsDLSQKLKEtqskYEEAMKEVLSVQKQmkLGL 511
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERR--------------------EALQRLAE----YSWDEIDVASAERE--IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 LSQEsadgYSHLREAPAdeDIDTLKQDLQKAVEESARNKERVRELETKLA--EKEQAEATkppaEACEELRSSYCSVIEN 589
Cdd:COG4913 673 LEAE----LERLDASSD--DLAALEEQLEELEAELEELEEELDELKGEIGrlEKELEQAE----EELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 590 MNKEKAFLFEKYQQAQeeimkLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDyrkrkSLE 669
Cdd:COG4913 743 ARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA-----DLE 812
|
250
....*....|....
gi 13507620 670 DAAEYIhkAEHERL 683
Cdd:COG4913 813 SLPEYL--ALLDRL 824
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
645-895 |
5.15e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 645 VSELSQLYREAQAEledyRKRKSLEDAAEYIhkaeherlmhvsnlsraksEEALSEMKSQYSKVLNELTQLKQlvdahKE 724
Cdd:COG3206 154 ANALAEAYLEQNLE----LRREEARKALEFL-------------------EEQLPELRKELEEAEAALEEFRQ-----KN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 725 NSVSITEHLQVITTlrtTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVpkssyEKLQASLESEVNALAT 804
Cdd:COG3206 206 GLVDLSEEAKLLLQ---QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 805 KLKESVREREKAHSEVAQVRSEVSQARRE-KDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRrcsetsskleedkdEKI 883
Cdd:COG3206 278 ELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE--------------ARL 343
|
250
....*....|..
gi 13507620 884 NEMTREVLKLKE 895
Cdd:COG3206 344 AELPELEAELRR 355
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
745-842 |
5.18e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 745 EMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDamvpkssyeklqasLESEVNALATKLKESVREREKAHS---EVA 821
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--------------LERELSEARSEERREIRKDREISRldrEIE 475
|
90 100
....*....|....*....|.
gi 13507620 822 QVRSEVSQARREKDNIQTLLK 842
Cdd:COG2433 476 RLERELEEERERIEELKRKLE 496
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
89-250 |
7.42e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.12 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 89 ALHVAAKNGHPECIRKLLQYKSPAENIDnsgktALH-YAAAQGCLQAV--QLLCEHKSPiNLKDLDGNIPLLVAVQNGHS 165
Cdd:PHA02946 12 SLYAKYNSKNLDVFRNMLQAIEPSGNYH-----ILHaYCGIKGLDERFveELLHRGYSP-NETDDDGNYPLHIASKINNN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 166 EACHFLLDHGADVNSRDKNGRTAL-----------------------------------MLACETGSSNTVDALIKKGAD 210
Cdd:PHA02946 86 RIVAMLLTHGADPNACDKQHKTPLyylsgtddevierinllvqygakinnsvdeegcgpLLACTDPSERVFKKIMSIGFE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13507620 211 LSLVDSLGHNALHYSKLSEN------AGIQNLLLSKISQDADLKTP 250
Cdd:PHA02946 166 ARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-149 |
8.34e-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: 37.65 E-value: 8.34e-04
10 20 30
....*....|....*....|....*....|..
gi 13507620 119 GKTALHYAAAQ-GCLQAVQLLCEHKSPINLKD 149
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-109 |
1.03e-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: 37.18 E-value: 1.03e-03
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
479-864 |
1.11e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 479 GSDLSQKLKETQSKYEEAMKevLSVQKQMKLGLLSQESADGYshLREAPADEDIDTLK-QDLQKAVEESARNKERVRELE 557
Cdd:TIGR00618 118 GRILAAKKSETEEVIHDLLK--LDYKTFTRVVLLPQGEFAQF--LKAKSKEKKELLMNlFPLDQYTQLALMEFAKKKSLH 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 558 TKL-AEKEQAEATKPPAEaceELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpQEAPDDSGDMKEAMNR 636
Cdd:TIGR00618 194 GKAeLLTLRSQLLTLCTP---CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ--EEQLKKQQLLKQLRAR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 637 mIDELNKQVSELSQLYRE-----------------AQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALS 699
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERinrarkaaplaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 700 EMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLankEAEVAKLEKQLAEEKAAVS 779
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL---QREQATIDTRTSAFRDLQG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 780 DAMVPKSSyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQ 859
Cdd:TIGR00618 425 QLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
....*
gi 13507620 860 EELAG 864
Cdd:TIGR00618 504 CPLCG 508
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
1.18e-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. 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: 1.18e-03
10 20 30
....*....|....*....|....*....|...
gi 13507620 184 NGRTALMLACE-TGSSNTVDALIKKGADLSLVD 215
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-212 |
1.40e-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: 36.85 E-value: 1.40e-03
10 20
....*....|....*....|....*....
gi 13507620 184 NGRTALMLACETGSSNTVDALIKKGADLS 212
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
434-770 |
1.44e-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: 42.19 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 434 QLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNN--TEISENGSDLSQKLKETQSKYEEAMKEVLSVQ------K 505
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERqrRELESRVAELKEELRQSREKHEELEEKYKELSasseelS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 506 QMKLGLLSQEsADGYSHLREApaDEDIDTLKQDLQKAVEESARNKERVRELETKLAEKE-QAEATKPPAEACEELRSSYC 584
Cdd:pfam07888 115 EEKDALLAQR-AAHEARIREL--EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 585 SVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSG--------DMKEAMNRMIDELNKQVSELSQLYREAQ 656
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALleelrslqERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 657 AELEDYR--------------------------KRKSLEDAAEyihkAEHERLMHVSNlSRAKSEEALSEMKSQYSKVLN 710
Cdd:pfam07888 272 AELHQARlqaaqltlqladaslalregrarwaqERETLQQSAE----ADKDRIEKLSA-ELQRLEERLQEERMEREKLEV 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 711 ELTQLKQLvdahkeNSVSITEhlqvittlrtTAKEMEEKISALtgHLANKEAEVAKLEKQ 770
Cdd:pfam07888 347 ELGREKDC------NRVQLSE----------SRRELQELKASL--RVAQKEKEQLQAEKQ 388
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
531-895 |
1.46e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 531 DIDTLKQDLQKAVEESARNKERVRELETKLAEKEqaeatkppaeaceelrssycsvienmnKEKAFLFEKYQQAQEEIMK 610
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEKSHSITL---------------------------KEIERLSIEYNNAMDDYNN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 611 LKDTLKSQMPQEapddsgdmkeamnrmiDELNKQVSELSQLYREAQAELEDYRKRKSLEdaaeyihkaehERLMHVSNLS 690
Cdd:PRK01156 237 LKSALNELSSLE----------------DMKNRYESEIKTAESDLSMELEKNNYYKELE-----------ERHMKIINDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 691 RAKSEEALSEmksqYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEkisaltghlanKEAEVAKLEKQ 770
Cdd:PRK01156 290 VYKNRNYIND----YFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIK-----------KKSRYDDLNNQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 771 LAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA 850
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13507620 851 LVQK---FQRAQEELAGMRRCSETSSKLEEDK---------------DEKINEMTREVLKLKE 895
Cdd:PRK01156 435 LRENldeLSRNMEMLNGQSVCPVCGTTLGEEKsnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
434-898 |
1.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 434 QLQDSLHDlqkRLESSEAEKKQLQDELQSQRtdtlclnnteISENGSDLSQKLKETQSKYEEAMKEVLS----VQKQMKL 509
Cdd:TIGR00618 212 CMPDTYHE---RKQVLEKELKHLREALQQTQ----------QSHAYLTQKREAQEEQLKKQQLLKQLRArieeLRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 510 GLLSQESADGYSHLreAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAEACEELRSSY---CSV 586
Cdd:TIGR00618 279 LEETQERINRARKA--APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsqEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 587 IENMNKEKAFLFEKYQQAQEEIMKLKdtlksqmpqeapddsgDMKEAMNRMIDELNKQVSELSQLYRE-AQAELEDYRKR 665
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIH----------------TLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 666 ksledaAEYIHKAeherlmhvsnlsRAKSEEALSEMKSQYSKVL--NELTQLKQLVDAHKENSVSITEHLQVITTLRTTA 743
Cdd:TIGR00618 421 ------DLQGQLA------------HAKKQQELQQRYAELCAAAitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 744 KEmEEKISALTGHLANKEAEVAK-LEKQLAEEKAAVSDAMVPKSSYEKLQAsLESEVNALATKLkESVRerekahsevAQ 822
Cdd:TIGR00618 483 LQ-ETRKKAVVLARLLELQEEPCpLCGSCIHPNPARQDIDNPGPLTRRMQR-GEQTYAQLETSE-EDVY---------HQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 823 VRSEVSQARREKDNIQTLlkakEQEVTALVQKFQRAQEELAGMRRCSET----SSKLEEDKDEKINEMTREVLKLKEALN 898
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
432-658 |
1.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 432 IRQLQDSLHDLQKRLESSEAEKKQLQdelqsQRTDTLclnntEISENGSDLSQKLKETQSKYEEAmkEVLSVQKQMKLGL 511
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFR-----QKNGLV-----DLSEEAKLLLQQLSELESQLAEA--RAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 512 LSQESADGYSHLREAPADEDIDTLKQDLQKA----VEESARNKE---RVRELETKLAEKEQaeatkppaeaceELRSSYC 584
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELeaelAELSARYTPnhpDVIALRAQIAALRA------------QLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13507620 585 SVIENMNKEKAFLfekyQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEaMNRMIDELNKQVSELSQLYREAQAE 658
Cdd:COG3206 313 RILASLEAELEAL----QAREASLQAQLAQLEARL-AELPELEAELRR-LEREVEVARELYESLLQRLEEARLA 380
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
549-780 |
1.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 549 NKERVREL----------------ETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKEKAFLfekyQQAQEEIMKLk 612
Cdd:PHA02562 172 NKDKIRELnqqiqtldmkidhiqqQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI----EELTDELLNL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 613 dtlksQMPQEapddsgDMKEAMNRMIDELNKQVSELSQLyreaQAELEDYRKRKSLEDAAEYIHkaEHERLMhvsnlsrA 692
Cdd:PHA02562 247 -----VMDIE------DPSAALNKLNTAAAKIKSKIEQF----QKVIKMYEKGGVCPTCTQQIS--EGPDRI-------T 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 693 KSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITE-------HLQVITTLRTTAKEMEEKISALTGHLANKEAEVA 765
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250
....*....|....*
gi 13507620 766 KLEKQLAEEKAAVSD 780
Cdd:PHA02562 383 KLQDELDKIVKTKSE 397
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
171-224 |
2.49e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 2.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 171 LLDHGADVNSRDKNGRTALMLACETGSSN---TVDALIKKGADLSLVDSLGHNALHY 224
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHL 89
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
438-770 |
2.53e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 438 SLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNtEISENGSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLGLLSQ 514
Cdd:COG5022 804 SLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEV-EFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVELAER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 515 ESadgyshlreapadedidtlkQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAEA--CEELRSSYCSVIENMNK 592
Cdd:COG5022 883 QL--------------------QELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLefKTELIARLKKLLNNIDL 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 593 EKAFLFEkyQQAQEEIMKLKDTlKSQMPQEAPDdSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDY----RKRKSL 668
Cdd:COG5022 943 EEGPSIE--YVKLPELNKLHEV-ESKLKETSEE-YEDLLKKSTILVREGNKANSELKNFKKELAELSKQYgalqESTKQL 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 669 EDaaEYIHKAEHERLMHVSNLSRA--KSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEM 746
Cdd:COG5022 1019 KE--LPVEVAELQSASKIISSESTelSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTI 1096
|
330 340
....*....|....*....|....*
gi 13507620 747 EEK-ISALTGHLANKEAEVAKLEKQ 770
Cdd:COG5022 1097 NVKdLEVTNRNLVKPANVLQFIVAQ 1121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
441-895 |
2.76e-03 |
|
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: 41.54 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 441 DLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGS-----DLSQKLKETQSKYEEAMKEVLSVQKQMKLglLSQE 515
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnlkKKIQKNKSLESQISELKKQNNQLKDNIEK--KQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 516 SADGYSHLREApaDEDIDTLKQDLQKAVEESARNKERVRELETKLAEKE------QAEATKPPAEACEELRSSYCSVIEN 589
Cdd:TIGR04523 241 INEKTTEISNT--QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkqlnqlKSEISDLNNQKEQDWNKELKSELKN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 590 MNKEKAFLFEKYQQAQEEIMKLKDTLkSQMPQEAPDdsgdmKEAMNRMID-ELNKQVSELSQLYREAQAELEDYRKRKSL 668
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQI-SQLKKELTN-----SESENSEKQrELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 669 EDAAEyihkaehERLMHVSNLSRAKsEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQV----ITTLRTTAK 744
Cdd:TIGR04523 393 INDLE-------SKIQNQEKLNQQK-DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliIKNLDNTRE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 745 EMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVR 824
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 825 SEV---------SQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKE 895
Cdd:TIGR04523 545 DELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
72-238 |
2.84e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.19 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 72 MVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQG--CLQAVQLLCEHKSPINLK- 148
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAKINNSv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 149 DLDGNIPLLvAVQNGHSEACHFLLDHGADVNSRDKNGRTAL--MLACETGSSNTVDALIKKGADLSLVDSLGHNALHY-- 224
Cdd:PHA02946 138 DEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIvc 216
|
170
....*....|....
gi 13507620 225 SKLSENAGIQNLLL 238
Cdd:PHA02946 217 SKTVKNVDIINLLL 230
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
639-833 |
3.04e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 639 DELNKQVSELSQLYREAQAELEDYRKRKS---------------LEDAA----EYIH-KAEHERLMHVSNLsRAKSEEAL 698
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAerareldllrfqleeLEAAAlqpgEEEElEEERRRLSNAEKL-REALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 699 SEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE----- 773
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALlrrla 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 774 EKAAVSDAMVPkSSYEKLQASLEsEVNALATKLKESVREREKAHSEVAQVRSEVSQARRE 833
Cdd:COG0497 313 RKYGVTVEELL-AYAEELRAELA-ELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
629-898 |
3.20e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 629 DMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYihkaeherlmhvSNLSrakseeaLSEMKSQYSKV 708
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL------------STLS-------LRQLESRLAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 709 LNELTQL-KQLVDAhkeNSVSITEHLQ---VITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVsDAmvp 784
Cdd:PRK11281 134 LDQLQNAqNDLAEY---NSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALL-NA--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 785 KSSYEKlqasLESEVNALATKLKESVREREKAH-----SEVAQVRSEVSQARREKDNiQTLLKAKEQEVTALVQKFQRAQ 859
Cdd:PRK11281 207 QNDLQR----KSLEGNTQLQDLLQKQRDYLTARiqrleHQLQLLQEAINSKRLTLSE-KTVQEAQSQDEAARIQANPLVA 281
|
250 260 270
....*....|....*....|....*....|....*....
gi 13507620 860 EELAGMRRCSETSSKleedKDEKINEMTREVLKLKEALN 898
Cdd:PRK11281 282 QELEINLQLSQRLLK----ATEKLNTLTQQNLRVKNWLD 316
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
613-830 |
3.53e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 613 DTLKSQMPQEAPDDSGDMKEAMNRmIDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAAEYIHKAEHERLMHVSNLSR 691
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEALQAEiDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 692 AKSE--------EALSEMKSqYSKVLNELTQLKQLVDAHKEnsvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAE 763
Cdd:COG3883 94 ALYRsggsvsylDVLLGSES-FSDFLDRLSALSKIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13507620 764 VAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQA 830
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-179 |
3.56e-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: 35.70 E-value: 3.56e-03
10 20
....*....|....*....|....*
gi 13507620 155 PLLVAVQNGHSEACHFLLDHGADVN 179
Cdd:pfam13606 5 PLHLAARNGRLEIVKLLLENGADIN 29
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
622-894 |
3.59e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 622 EAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYR-KRKSL-EDAAEYIHKAEHERLMhvsnlsRAKSEEALS 699
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELnAQVKELREEAQELREK------RDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 700 EMKSQYSKVLNELTQLKQLVDAHKENsvsitehLQVITTLRTTAKEMEEKISAL------TGHLANKEAEVAKLEKQLAE 773
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKE-------LAELNKAGGSIDKLRKEIERLewrqqtEVLSPEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 774 EKAAVSDAMVPKSSYEKLQASLES---EVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA 850
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKElrkEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13507620 851 LVQKFQRAQEELAGMR----RCSETSSKLEEDKDEKINEMTREVLKLK 894
Cdd:COG1340 228 LHEEIIELQKELRELRkelkKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-667 |
3.64e-03 |
|
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: 41.20 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 426 TDNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnTEISENGSDLSQKLKETQSKYEeamkevlsvQK 505
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAA---------NL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 506 QMKLGLLSQESADGYSHLREapADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppAEACEELRSSYCS 585
Cdd:TIGR02168 823 RERLESLERRIAATERRLED--LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL--EEALALLRSELEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 586 V---IENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKEAMN----------RMIDELN 642
Cdd:TIGR02168 899 LseeLRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKRLE 978
|
250 260
....*....|....*....|....*
gi 13507620 643 KQVSELSQLYREAQAELEDYRKRKS 667
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-887 |
3.98e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 426 TDNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLClNNTEISENGSDLSQKLKETQSKYEEAMKEVlsvQK 505
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL---EK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 506 QMKLG----LLSQESADGYSHlREAPADEDIDTLKQDLQKAVEESARNKER------------------VRELETKLAEK 563
Cdd:pfam15921 350 QLVLAnselTEARTERDQFSQ-ESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhlRRELDDRNMEV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 564 EQAEAT-KPPAEACEELRSSYCSVIENMNKEkaflFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSgdMKEAMNRMIDELN 642
Cdd:pfam15921 429 QRLEALlKAMKSECQGQMERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 643 KQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSrakseEALSEMKSQYSKVLNELTQ----LKQL 718
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC-----EALKLQMAEKDKVIEILRQqienMTQL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 719 VDAHKENSVSI-TEHLQVITTLRTTAKEMEE----------KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSS 787
Cdd:pfam15921 578 VGQHGRTAGAMqVEKAQLEKEINDRRLELQEfkilkdkkdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 788 YEKLQASLESEVNALATK---LKESVREREK---------------AHSEVAQVRSEVS-------QARREKDNIQTLLK 842
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDyevLKRNFRNKSEemetttnklkmqlksAQSELEQTRNTLKsmegsdgHAMKVAMGMQKQIT 737
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 13507620 843 AKEQEVTALVQKFQRAQEelaGMRRCSETSSKLEEDKDEKINEMT 887
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEE---AMTNANKEKHFLKEEKNKLSQELS 779
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
639-830 |
4.07e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 639 DELNKQVSELSQLYREAQAE---LEDYRKRK---SLEDAAEYIHK------AEHERLMHVSnLSRAKSEEALSEMKSQYS 706
Cdd:COG3096 937 EQLQADYLQAKEQQRRLKQQifaLSEVVQRRphfSYEDAVGLLGEnsdlneKLRARLEQAE-EARREAREQLRQAQAQYS 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 707 KVLNELTQLKQLVDAHKEnsvsitehlqvittlrtTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMvpKS 786
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQ-----------------TLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSR--RS 1076
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13507620 787 SYEKLQASLESEVNALATKLKesvrereKAHSEVAQVRSEVSQA 830
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLR-------KAERDYKQEREQVVQA 1113
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
694-866 |
4.18e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 694 SEEALSEMKSQYSKVLNELTQLKQLVDAhKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE 773
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 774 EKAAVSD------AMVPKSSYEKLQASLESEVNALATKLKESVRE-REKAHSEVAQVRSEVsqarrekdNIQTLLKAKEQ 846
Cdd:cd22656 161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDElKALIADDEAKLAAAL--------RLIADLTAADT 232
|
170 180
....*....|....*....|
gi 13507620 847 EVTALVQKFQRAQEELAGMR 866
Cdd:cd22656 233 DLDNLLALIGPAIPALEKLQ 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
448-897 |
4.30e-03 |
|
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: 40.86 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 448 SSEAEKKQLQDELQSQRTDTLCLNNT--EISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKL----GLLSQESADGYS 521
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAiqELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLlketCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 522 HLREapadeDIDTLKQDLQKAVEESARNKERVReLETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKEKAFLFeky 601
Cdd:pfam05483 176 YERE-----ETRQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL--- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 602 QQAQEEIMKLKDTlkSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHE 681
Cdd:pfam05483 247 IQITEKENKMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 682 RLMHVSNLSRAKSEEaLSEMKSQYSKVLNELT----QLKQLVDAHKENSVSITEHLQVITT-LRTTAKEMEEkisaLTGH 756
Cdd:pfam05483 325 TICQLTEEKEAQMEE-LNKAKAAHSFVVTEFEattcSLEELLRTEQQRLEKNEDQLKIITMeLQKKSSELEE----MTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 757 LANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQA----------SLESEVNALATKLKESVREREKAHSEVAQVRSE 826
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13507620 827 VSQARREKDNIQT-----LLKAKE--QEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 897
Cdd:pfam05483 480 LEKEKLKNIELTAhcdklLLENKEltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
587-826 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 587 IENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEAMNRmIDELNKQVSELSQLYREAQAELED----- 661
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN-EEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGEraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 662 YRKRKSL---------EDAAEYIHKAEherlmhvsnlsrakseeALSEMKSQYSKVLNELTQLKQLVDAHKENSVsiteh 732
Cdd:COG3883 96 YRSGGSVsyldvllgsESFSDFLDRLS-----------------ALSKIADADADLLEELKADKAELEAKKAELE----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 733 lQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVRE 812
Cdd:COG3883 154 -AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|....
gi 13507620 813 REKAHSEVAQVRSE 826
Cdd:COG3883 233 AAAAAAAAAAAASA 246
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
84-239 |
4.79e-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: 40.55 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 84 SSGHSALHVAAKNGHP---ECIRKLLQYKSPAENID---NS--------GKTALHYAAAQGCLQAVQLLCEHKSPINLKD 149
Cdd:cd22193 27 STGKTCLMKALLNLNPgtnDTIRILLDIAEKTDNLKrfiNAeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 150 LD--------------GNIPLLVAVQNGHSEACHFLLDHG---ADVNSRDKNGRTALMlACETGSSNTVD--ALIKKGAD 210
Cdd:cd22193 107 KGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH-ALVTVADNTKEntKFVTRMYD 185
|
170 180 190
....*....|....*....|....*....|
gi 13507620 211 LSLVDSLG-HNALHYSKLSENAGIQNLLLS 239
Cdd:cd22193 186 MILIRGAKlCPTVELEEIRNNDGLTPLQLA 215
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
587-814 |
6.34e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 587 IENMNKEK-AFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYRE----------A 655
Cdd:PRK05771 33 IEDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEikeleeeiseL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 656 QAELEDYRKRK---------SLEDAAEY-----------IHKAEHERLMHVSNL-------------------SRAKSEE 696
Cdd:PRK05771 113 ENEIKELEQEIerlepwgnfDLDLSLLLgfkyvsvfvgtVPEDKLEELKLESDVenveyistdkgyvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 697 ALSEMKS-QYSKV-LNELTQLKQLVDAHKENSVSITEHLQ-VITTLRTTAKEMEEKISALTGHLANkEAEVAKLEKQLAE 773
Cdd:PRK05771 193 VEEELKKlGFERLeLEEEGTPSELIREIKEELEEIEKEREsLLEELKELAKKYLEELLALYEYLEI-ELERAEALSKFLK 271
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 13507620 774 -EKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVRERE 814
Cdd:PRK05771 272 tDKTFAIEGWVPEDRVKKLKELIDKATGGSAYVEFVEPDEEE 313
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-79 |
6.62e-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: 34.93 E-value: 6.62e-03
10 20
....*....|....*....|....*...
gi 13507620 52 EGKTAFHLAAAKGHVECLKVMVTHGVDV 79
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
116-247 |
6.78e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.64 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 116 DNSGKTALHYAAAQgclQAVQLLCEHKSPINLKDL-DGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACE 194
Cdd:PHA02791 27 DVHGHSALYYAIAD---NNVRLVCTLLNAGALKNLlENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 13507620 195 TGSSNTVDALIKKGADLSLVDSLG-HNALHYSKLSENAGIQNLLLSKISQDADL 247
Cdd:PHA02791 104 SGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
433-886 |
7.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 433 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnteisengSDLSQKLKETQSKYEEAMKEVLSVQKQMK--LG 510
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSEL------------ESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 511 LLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARNKER-VRELETKLAE-KEQAEATKPPAEACEELRSSYCSVIE 588
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDmKKKLEEDAGTLEALEEGKKRLQRELE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 589 NMN---KEKAFLFEK-------YQQAQEEIMKLKDTLKS-------------QMPQEAPDDSGDMKE------------- 632
Cdd:pfam01576 556 ALTqqlEEKAAAYDKlektknrLQQELDDLLVDLDHQRQlvsnlekkqkkfdQMLAEEKAISARYAEerdraeaeareke 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 633 ----AMNRMIDELNKQVSELSQLYREAQAELEDYRKRKslEDAAEYIHKAEHerlmhvsnlSRAKSEEALSEMKSQYSKV 708
Cdd:pfam01576 636 tralSLARALEEALEAKEELERTNKQLRAEMEDLVSSK--DDVGKNVHELER---------SKRALEQQVEEMKTQLEEL 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 709 LNELTQLKqlvDAHKENSVSITE-HLQVITTLRTTAKEMEEKISALTghlankeAEVAKLEKQLAEEKAAVSDAMVPKSS 787
Cdd:pfam01576 705 EDELQATE---DAKLRLEVNMQAlKAQFERDLQARDEQGEEKRRQLV-------KQVRELEAELEDERKQRAQAVAAKKK 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 788 YEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 867
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
490
....*....|....*....
gi 13507620 868 CSETSsklEEDKDEKINEM 886
Cdd:pfam01576 855 ARRQA---QQERDELADEI 870
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
597-877 |
7.41e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 597 LFEKYQQAQEEImklkDTLKSQmpqeapddsgdmKEAMNRMIDELNKQVSELSQ--LYREAQAELEdyrkrksledaaey 674
Cdd:COG0497 163 AYRAWRALKKEL----EELRAD------------EAERARELDLLRFQLEELEAaaLQPGEEEELE-------------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 675 ihkAEHERLMHVSNLsRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALT 754
Cdd:COG0497 213 ---EERRRLSNAEKL-REALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 755 GHLANKEAEVAKLEKQLAEekaavsdamvpkssyeklqasleseVNALATKLKESVrerekahSEVAQVRSEVSQARREK 834
Cdd:COG0497 289 DSLEFDPERLEEVEERLAL-------------------------LRRLARKYGVTV-------EELLAYAEELRAELAEL 336
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13507620 835 DNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRcsETSSKLEE 877
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEK 377
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
615-889 |
7.65e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 40.10 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 615 LKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKS 694
Cdd:COG2770 255 LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 695 EEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEE 774
Cdd:COG2770 335 LLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 775 KAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQK 854
Cdd:COG2770 415 ALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEE 494
|
250 260 270
....*....|....*....|....*....|....*
gi 13507620 855 FQRAQEELAGMRRCSETSSKLEEDKDEKINEMTRE 889
Cdd:COG2770 495 EEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVA 529
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-146 |
7.68e-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: 34.93 E-value: 7.68e-03
10 20
....*....|....*....|....*...
gi 13507620 119 GKTALHYAAAQGCLQAVQLLCEHKSPIN 146
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
468-728 |
8.31e-03 |
|
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: 39.75 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 468 LCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLLSQESADGyshlREAPADEDIDTLKQDLQKAVEESA 547
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 548 RNKERVRELETKLAEKEQAEAtkppaeacEELRSSYcsVIENMNKEKAFL-FEKYQQAQEEIMKLKDTLKSQmpQEAPDD 626
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELA--------ELLRALY--RLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPAR--REQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 627 SGDMKEAMNRMIDELNKQVSELSQLYREAQAEledyrkRKSLEDAaeyihKAEHERLMHVSNLSRAKSEEALSEMKSQYS 706
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEE------RAALEAL-----KAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260
....*....|....*....|..
gi 13507620 707 KVLNELTQLKQLVDAHKENSVS 728
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
632-886 |
8.44e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 632 EAMNRMIDELNKQVSELSQLYREAQAE--------LEDYRKRKSLEDAAEYIHKA---------EHERLMHVSNLSRAKS 694
Cdd:TIGR01612 568 EEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklkLELKEKIKNISDKNEYIKKAidlkkiienNNAYIDELAKISPYQV 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 695 EEALSEMKSQYSKVLNELTQLKQ---------LVDAHKENSVSITEHlqvittlRTTAKEMEEKISALTGHLANKEAEVA 765
Cdd:TIGR01612 648 PEHLKNKDKIYSTIKSELSKIYEddidalyneLSSIVKENAIDNTED-------KAKLDDLKSKIDKEYDKIQNMETATV 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13507620 766 KLE-KQLAEEKAAVSDAMV--PKSSYEKLQASLESEVNALATKLKE---SVREREKAHSEVAQVRSEVSQARREKDNIQT 839
Cdd:TIGR01612 721 ELHlSNIENKKNELLDIIVeiKKHIHGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELNKYKSKISEIKNHYNDQIN 800
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 13507620 840 LLKAKEQEVTalvQKFQRAQEELagmrrcsETSSKLEEDKDEKINEM 886
Cdd:TIGR01612 801 IDNIKDEDAK---QNYDKSKEYI-------KTISIKEDEIFKIINEM 837
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
160-230 |
9.27e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.05 E-value: 9.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13507620 160 VQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSEN 230
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| |
