|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-248 |
1.72e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 171.29 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 81 AQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAV 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
....*...
gi 1720385250 241 ISQDADLK 248
Cdd:COG0666 275 LLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-246 |
5.74e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 81 AQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAV 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
....*.
gi 1720385250 241 ISQDAD 246
Cdd:COG0666 242 GADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
1.38e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 97 GHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720385250 177 DVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-240 |
3.79e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 130.07 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPA 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 113 ENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720385250 193 CETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
9.19e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 91 HVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 1720385250 171 LLDHGADVNSRDKNGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
8.14e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 96.34 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPaeNIDNSGKTALHYAAAQGCLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1720385250 137 LLCEHKSPINLKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
1.31e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 95.57 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 90 LHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKsPINLKDlDGNIPLLVAVQNGHSEACH 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1720385250 170 FLLDHGADVNSRD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-239 |
1.77e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 101.28 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHVAA--K 95
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 96 NGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGC--LQAVQLLCEHKSPINLKDldgNIPLLvavqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 174 HGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
3.73e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 123 LHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHgADVNSRDkNGRTALMLACETGSSNTVD 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1720385250 203 ALIKKGADLSLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-224 |
4.52e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 94.71 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 88 SALHVAAKNGHP--ECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQA--VQLLCEHKSPINLKDLDGNIPLLVAVQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFN 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDslghNALHY 224
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-217 |
1.26e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 91.47 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 78 DVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAEniDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 158 VAVQNGHSEACHFLLDHGADVNSRDKNgrtalmlacETGSSNTVDALIKK---GADLSLVDSL 217
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVDKANTD---------DDFSPTELRELLQKrelGHSITIVDSV 714
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-222 |
1.50e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.56 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 43 GASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 123 LHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQngHSEACHFLLDHGADVNSRDKNGRTALMLACETGSS-NTV 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDII 271
|
170 180
....*....|....*....|.
gi 1720385250 202 DALIKKGADLSLVDSLGHNAL 222
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-230 |
1.26e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.92 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLKVMVTHGVDVTAQDSSGHSALHV--AAKNGHPECIRKL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 106 LQYKSPAENIDNSGKTALH-YAAAQGC-LQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF--LLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 182 DKNGRTALMLACETGSSNT--VDALIKKGADLSLVDSLGHNALHYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-108 |
2.06e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.15 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHgVDVTAQDsSGHSALHVAAKNGHPECI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*.
gi 1720385250 103 RKLLQY 108
Cdd:pfam12796 78 KLLLEK 83
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
2.18e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 82.73 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV---DVTAQDssGHSALHVAAKNGHPECIRKLLQYKSPAEN 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 115 IDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 1720385250 194 ETGSSNTVDALIKKGADLSLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
23-219 |
6.71e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 81.16 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECI 102
Cdd:PHA02874 128 LHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 103 RKLLQYKSPAENIDNSGKTALHYAAAQGcLQAVQLLCEHKSpINLKDLDGNIPLLVAVQNGHS-EACHFLLDHGADVNSR 181
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNAS-INDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIK 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720385250 182 DKNGRTALMLACETGSSNTV------DALIKKGAD-LSLVDSLGH 219
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVikdiiaNAVLIKEADkLKDSDFLEH 329
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
1.02e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 156 LLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKgADLSLVDSlGHNALHYSKLSENAGIQN 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 1720385250 236 LLLSK 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
4.58e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 79 VtaqdssghSALHVAAKNGhpECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLV 158
Cdd:PHA02874 94 T--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 159 AVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQnLLL 238
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLI 242
|
250
....*....|....*
gi 1720385250 239 SKIS---QDADLKTP 250
Cdd:PHA02874 243 NNASindQDIDGSTP 257
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-223 |
4.29e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.09 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKS 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 111 paeNIdNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGH-SEACHFLLDHGADVNSRDKNGRTAL 189
Cdd:PHA02876 236 ---NI-NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190
....*....|....*....|....*....|....*
gi 1720385250 190 MLACETG-SSNTVDALIKKGADLSLVDSLGHNALH 223
Cdd:PHA02876 312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLH 346
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-225 |
9.20e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.94 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-KVMVTHGVDVTAQDSSGHSALHVAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 96 NGH-PECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQ-AVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLD 173
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 174 HGADVNSRDKNGRTALMLA-CETGSSNTVDALIKKGADLSLVDSLGHNALHYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
1.20e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720385250 55 TAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
602-835 |
3.70e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.96 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 602 KEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEyihkaehERLMHVSNLSRAKSEeaLSEMKSQYSKVLN 681
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-------EAKLLLQQLSELESQ--LAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 682 ELTQLKQLVDAHKENSVSITEHlQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMvpkssyEK 761
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 762 LQASLESEVNALATKLKESVREREKAHSEVA---QVRSEVSQARREKDNIQTLLkakeqevTALVQKFQRAQEELAG 835
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELY-------ESLLQRLEEARLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-904 |
3.74e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 482
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 LSQESADgyshLREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppaeacEELRSSYCSVIENMN 562
Cdd:COG1196 309 ERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 563 KEKAFLFEKYQQAQEEIMKLKDTLKSQmpQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDA 642
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 643 AEYIHKAEHERLMHVSNLSRAKSEEALSE---MKSQYSKVLNELTQ---------LKQLVDAHKENSVSITEHLQVITTL 710
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEElaeAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 711 RTTAkemEEKISALTGHLANKEAEVAKLEKQLAEEKAA-------VSDAMVPKSSYEKLQASLESEVNALATKLKESVRE 783
Cdd:COG1196 537 EAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 784 REKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLK 863
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720385250 864 LKEALNSLSQLSYSTSSSKRQSQQLDLLQQQVKQLQNQLAE 904
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
405-867 |
5.55e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 405 QLQDSLHDLQKRLESSEAEKKQLQDELQSQRtdtlclnntEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglls 484
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR---------EELEKLEKEVKELEELKEEIEELEKELESLEGSKR----- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 485 qesadgyshlreapadeDIDTLKQDLQKAVEESarnKERVRELETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKE 564
Cdd:PRK03918 256 -----------------KLEEKIRELEERIEEL---KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 565 KAFLFEKYQQAQEEIMKLkdtlkSQMPQEAPDDSGDMKEAMNRmIDELNKQVsELSQLYREAQAELEDYRKRKS------ 638
Cdd:PRK03918 316 LSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR-LEELEERH-ELYEEAKAKKEELERLKKRLTgltpek 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 639 LEDAAEYIHKAEHERLMHVSNLSRAKSEeaLSEMKSQYSKVLNELTQLK--------QLVDAHKENsvSITEHLQVITTL 710
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGE--LKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKE--LLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 711 RTTAKEMEEKISALtghlankEAEVAKLEKQLAEEkaavSDAMVPKSSYEKLQaSLESEVNAL-ATKLKESVREREKAHS 789
Cdd:PRK03918 465 EKELKEIEEKERKL-------RKELRELEKVLKKE----SELIKLKELAEQLK-ELEEKLKKYnLEELEKKAEEYEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 790 EVAQVRSEVSQARREKDNIQTLlkakEQEVTALVQKFQRAQEELAGM-RRCSETSSKLEEDKDEKINEMT---REVLKLK 865
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEpfyNEYLELK 608
|
..
gi 1720385250 866 EA 867
Cdd:PRK03918 609 DA 610
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
1.02e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.67 E-value: 1.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720385250 121 TALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-868 |
2.27e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 564 EKAflfEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQL---YREAQAELEDYRKRKSLE 640
Cdd:COG1196 210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 641 DAAEYIHKAEHERLmhvsnlsrAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKEnsvsitEHLQVITTLRTTAKEMEEK 720
Cdd:COG1196 287 QAEEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 721 ISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQ 800
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720385250 801 ARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 868
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-239 |
3.84e-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: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 88 SALHVAAKNGHPECIRKLLQYKSpaenIDNS-----GKTALHYAAAQGCLQAVQLLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPS----CDLFqrgalGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 158 VAVQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALH 223
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180
....*....|....*....|
gi 1720385250 224 YSKLSENAGIQ----NLLLS 239
Cdd:cd22192 175 ILVLQPNKTFAcqmyDLILS 194
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-268 |
5.63e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 9 RKSDTNEWN-KNDDRLLQAVENG-DAEKVASLLgKKGASATKHDSEGKTAFHLAAA-KGHVECLKVMVTHGVDVTAQDSS 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 86 GHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYA-AAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNG- 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSsnTVDALIKKGADLS----LVDSLGHNALHYSKLSENAGIQNLLLS 239
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRH 532
|
250 260
....*....|....*....|....*....
gi 1720385250 240 KISQDADLKTPTKPKQLSDVSSPRSITST 268
Cdd:PHA02876 533 DIRNEVNPLKRVPTRFTSLRESFKEIIQS 561
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
403-860 |
7.09e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTdtlclnntEISENGSDLSQKLKETQskYEEAMKEVLSVQkqmklgl 482
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRE--------RLEELEEERDDLLAEAG--LDDADAEAVEAR------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 lsQESADGyshlREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEK-EQAEATKPPAEACEELRSSYCSVIENM 561
Cdd:PRK02224 316 --REELED----RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELrEEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 562 NKEKAFLFEKYQQAQEEimklkdtlksqmpqeaPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQaelEDYRKRKSLED 641
Cdd:PRK02224 390 EEEIEELRERFGDAPVD----------------LGNAEDFLEELREERDELREREAELEATLRTAR---ERVEEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 642 AA------EYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKE-----NSVSITEHLqvITTL 710
Cdd:PRK02224 451 AGkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleERREDLEEL--IAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 711 RTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALAtKLKESVREREKAHSE 790
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 791 VAQVR------SEVSQARREKdniqtlLKAKEQEVTALVQKFQRAQEELAGMRRcsETSSKLEEDKDEKINEMTRE 860
Cdd:PRK02224 608 IERLRekrealAELNDERRER------LAEKRERKRELEAEFDEARIEEAREDK--ERAEEYLEQVEEKLDELREE 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-853 |
3.46e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 404 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDtlclnNTEISEngsdLSQKLKETQSKYEEAMKEVLSVQKQMKLgll 483
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----EERLEE----LKKKLKELEKRLEELEERHELYEEAKAK--- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 484 sQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN----KERVRELETKLAEKEQA-EATKPPAEAC----------- 547
Cdd:PRK03918 371 -KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELKKAiEELKKAKGKCpvcgrelteeh 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 548 -EELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELN-KQVSELSQLYRE 625
Cdd:PRK03918 450 rKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 626 AQAELEDYRKR-KSLEDAAEYIHKAEHERlmhvsnlsrAKSEEALSEMKSQYSKVLNELTQ------------LKQLVDA 692
Cdd:PRK03918 530 LKEKLIKLKGEiKSLKKELEKLEELKKKL---------AELEKKLDELEEELAELLKELEElgfesveeleerLKELEPF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 693 HKE-----NSVS-ITEHLQVITTLRTTAKEMEEKisaltghLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLqaSL 766
Cdd:PRK03918 601 YNEylelkDAEKeLEREEKELKKLEEELDKAFEE-------LAETEKRLEELRKELEELEKKYSEEEYEELREEYL--EL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 767 ESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEqEVTALVQKFQR--AQEELAGMRRCSETSS 844
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKykALLKERALSKVGEIAS 750
|
490
....*....|
gi 1720385250 845 KL-EEDKDEK 853
Cdd:PRK03918 751 EIfEELTEGK 760
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
3.98e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 3.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 86 GHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
6.95e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 6.95e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 155 PLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALI 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
521-866 |
8.10e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 521 KERVRELETKLAEKEQAEatkpPAEACEELRSSYCSV---IENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-QMPQEAPD 596
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKD----LHERLNGLESELAELdeeIERYEEQREQARETRDEADEVLEEHEERREElETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 597 DSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAaeyihkaEHERL-MHVSNLSRAKSE--EALSEMK 673
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDA-------DAEAVeARREELEDRDEElrDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 674 SQYSKVLNELTQLKQLVDAHKENSvsitehlqviTTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAM 753
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 754 VPKSSYEKLQASLESEVNALATKLKE---SVREREKAHSEVAQVRSE------------------VSQARREKDNIQTLL 812
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAEL 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 813 KAKEQEVTALVQKFQRAQEELAGMRRCS------ETSSKLEEDKDEKINEMTREVLKLKE 866
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIErleerrEDLEELIAERRETIEEKRERAEELRE 544
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
609-904 |
1.10e-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: 59.30 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 609 IDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQ 688
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 689 LVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLES 768
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 769 EVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMR-RCSETSSKLE 847
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRID 939
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 848 EDKdEKINEmtREVLKLKEALNSLSQLSYSTSSSKRQSQQLDllqqqvkqlqNQLAE 904
Cdd:TIGR02168 940 NLQ-ERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRLE----------NKIKE 983
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
162-271 |
1.14e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 162 NGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSKI 241
Cdd:PTZ00322 92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
90 100 110
....*....|....*....|....*....|
gi 1720385250 242 SQDADLKTPTKPKQLSDVssPRSITSTPLS 271
Cdd:PTZ00322 172 QCHFELGANAKPDSFTGK--PPSLEDSPIS 199
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
1.42e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.58 E-value: 1.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 72 MVTHG-VDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-829 |
1.80e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 406 LQDSLHDLQKRLES--SEAEK----KQLQDELQSQRTDTLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQmk 479
Cdd:COG1196 191 LEDILGELERQLEPleRQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 480 lgllsqesadgyshlreapadedIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEatkppaEACEELRSSYCSVIE 559
Cdd:COG1196 269 -----------------------LEELRLELEELELELEEAQAEEYELLAELARLEQDI------ARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 560 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEapddsgdmkEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSL 639
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL---------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 640 EDAAEYIHKAEHERLmhvsnlsRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEE 719
Cdd:COG1196 391 ALRAAAELAAQLEEL-------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 720 KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYE-KLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 798
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
410 420 430
....*....|....*....|....*....|.
gi 1720385250 799 SQARREKDNIQTLLKAKEQEVTALVQKFQRA 829
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
51-275 |
2.73e-08 |
|
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: 57.78 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSpaeNIDNSGKTALHyAAA 128
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLS---CRGAVGDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 129 QGCLQAVQLLCEHKSPINLKDLD--------------GNIPLLVAVQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 184 ---NGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKL-SENA--------GIQNLLLSKISQDADlktpt 251
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMeNEFKaeyeelscQMYNFALSLLDKLRD----- 245
|
250 260
....*....|....*....|....
gi 1720385250 252 kPKQLSDVSSPRSITSTPLSGKES 275
Cdd:TIGR00870 246 -SKELEVILNHQGLTPLKLAAKEG 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
663-869 |
2.95e-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: 57.76 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 663 AKSEEALSEMKSQYSKVLNELTQLKQlvdahkensvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQL 742
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRK----------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 743 AEEKAAVSDAmvpkssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREkdniqtlLKAKEQEVTAL 822
Cdd:TIGR02168 750 AQLSKELTEL-------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELTLL 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720385250 823 VQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEALN 869
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
398-867 |
2.99e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 398 DNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQ--SQRTDTLCLNNTEISENGSDLSQKLKETQsKYEEAMKEVLSVQ 475
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAK 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 476 KQMKLGLLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN---KERVRELETKLAEKEQAEATKPPAE----ACE 548
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEedkkKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 549 ELRSSYCSvienmnKEKAflfEKYQQAQEEIMKlKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSElSQLYREAQA 628
Cdd:PTZ00121 1409 ELKKAAAA------KKKA---DEAKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 629 ELEDYRKRKSLEDAAEYIHKAEHErlMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVIT 708
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 709 TLRTT--AKEMEEKISALTG-HLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNAlatklkESVRERE 785
Cdd:PTZ00121 1556 ELKKAeeKKKAEEAKKAEEDkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------EELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 786 KAHSEVAQVRSEVSQARREKDNIQtllKAKEQEVTALVQKFQRAQEElagmRRCSETSSKLEEDKDEKINEMTREVLKLK 865
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELK---KAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
..
gi 1720385250 866 EA 867
Cdd:PTZ00121 1703 KA 1704
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-867 |
3.28e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLqDELQSQRTDtLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 482
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKEL-EELKEEIEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 LSQESADGYSHLREAPAD------------EDIDTLKQDLQKAVEESARNKERVRELETKLAE-KEQAEATKPPAEACEE 549
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEyldelreiekrlSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 550 LRSsycsVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKEAMNRMIDELNKQVSELS----- 620
Cdd:PRK03918 367 AKA----KKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELKkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 621 --------------QLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHV----SNLSRAKS-EEALSEMKSQYSKV-L 680
Cdd:PRK03918 438 cpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeSELIKLKElAEQLKELEEKLKKYnL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 681 NELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEE--------KAAVSDA 752
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKEL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 753 MVPKSSYEKLQASlESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTllKAKEQEVTALVQKFQRAQEE 832
Cdd:PRK03918 598 EPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRE 674
|
490 500 510
....*....|....*....|....*....|....*
gi 1720385250 833 LAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEA 867
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-195 |
3.81e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.81 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 113 ENIDNSGKTALHYAAAQgCL--QAVQLLCEHKSPINLKD-LDGNIPLLVAVqngHSE-ACHFLLDHGADVNSRDKNGRTA 188
Cdd:PHA02878 228 DARDKCGNTPLHISVGY-CKdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTP 303
|
....*..
gi 1720385250 189 LMLACET 195
Cdd:PHA02878 304 LSSAVKQ 310
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
592-868 |
1.41e-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: 55.84 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 592 QEAPDDSGDMKEAMNRMIDELNKQ---VSELSQLYREAQAELEDYRKRKS------------LEDAAEYIHKAEHERLMH 656
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEqleqeeeklkerLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 657 VSNLsrAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKensvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVA 736
Cdd:TIGR02169 757 KSEL--KELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 737 KLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKE---SVREREKAH----SEVAQVRSEVSQARREKDNIQ 809
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaALRDLESRLgdlkKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 810 TLLKAKEQEVTALVQKFQRAQEELA--GMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 868
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-869 |
1.52e-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: 55.45 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 397 TDNDVIIRQLQDSLHDLQKRLES--SEAEKKQLQDELQSQRTDTLCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSV 474
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 475 QKQMKLGLLSQESADGY---SHLREAPADEDIDTLKQDLQKAVEESARNKERVRELETKL---------AEKEQAEATKP 542
Cdd:TIGR02168 350 KEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerledrrerLQQEIEELLKK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 543 PAEACEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEApddsGDMKEAMNRmIDELNKQVSELSQL 622
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE----RELAQLQAR-LDSLERLQENLEGF 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 623 YREAqAELEDYRKRKS---------LEDAAEY---IHKAEHERLMH--VSNLSRAKSE-EALSEMKSQYSKVLnELTQLK 687
Cdd:TIGR02168 505 SEGV-KALLKNQSGLSgilgvlselISVDEGYeaaIEAALGGRLQAvvVENLNAAKKAiAFLKQNELGRVTFL-PLDSIK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 688 --QLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLA------------------------------------ 729
Cdd:TIGR02168 583 gtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnalelakklrpgyrivtldgdlvrpggvit 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 730 -----------NKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 798
Cdd:TIGR02168 663 ggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 799 SQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAgmrRCSETSSKLEEDkdekINEMTREVLKLKEALN 869
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELA---EAEAEIEELEAQ----IEQLKEELKALREALD 806
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-869 |
1.70e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLclnntEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQM--KL 480
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELE-----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 481 GLLSQESADGYSHLREA-PADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQA-EATKPPAEACEELRSSYCSVI 558
Cdd:COG1196 379 EELEELAEELLEALRAAaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 559 ENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQA 628
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLeelaeaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 629 ELEDY-------RKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSIT 701
Cdd:COG1196 539 ALEAAlaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 702 EHLQVITTLRTTAKEMEEKISALTGHlankEAEVAKLEKQLAEEKAAVSDAmvpksSYEKLQASLESEVNALATKLKESV 781
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAG----RLREVTLEGEGGSAGGSLTGG-----SRRELLAALLEAEAELEELAERLA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 782 REREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREV 861
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*...
gi 1720385250 862 LKLKEALN 869
Cdd:COG1196 770 ERLEREIE 777
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
1.78e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 68 CLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
403-695 |
2.20e-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: 54.96 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRtDTLCLNNTEISENGS---DLSQKLKETQSK---YEEAMKEVLSVQK 476
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 477 QMKLGLLSQESADGYSHLREAPADEDIDTLKQDLQK-AVEESARNK-ERVRELETKLA-EKEQAEATKPPAEACEELRSs 553
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlSVADAARRQfEKAYELVCKIAgEVERSQAWQTARELLRRYRS- 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 554 YCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAE 629
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720385250 630 LEDYR-KRKSLEDAAEYIHKAEH--ERLMHVSNLSRAKSEEALSEMKSQYSKvLNELTQLKQLVDAHKE 695
Cdd:COG3096 587 LEQLRaRIKELAARAPAWLAAQDalERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-224 |
2.46e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 2.46e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720385250 171 LLDHG-ADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHY 224
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
405-849 |
3.49e-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: 54.41 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 405 QLQDSLHDLQKRLESSEAEKKQLQDElqsqrtdtlclnNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglls 484
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIK----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 485 qesadgyshlreaPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQA-----------EATKPPAE----ACEE 549
Cdd:pfam01576 135 -------------KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKakslsklknkhEAMISDLEerlkKEEK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 550 LRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-----QMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQ--- 621
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALARLEEETAQKNNALKKIRELEAQISELQEdle 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 622 LYREAQAELEDYRK---------RKSLED-----AAEYIHKAEHERlmHVSNLSRAKSEEA------LSEMKSQYSKVLN 681
Cdd:pfam01576 282 SERAARNKAEKQRRdlgeelealKTELEDtldttAAQQELRSKREQ--EVTELKKALEEETrsheaqLQEMRQKHTQALE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 682 ELT-QLKQLvdahKENSVSITEHLQVittLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYE 760
Cdd:pfam01576 360 ELTeQLEQA----KRNKANLEKAKQA---LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 761 KLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQAR-------REKDNIQTLLKAKEQEVTALVQKFQRAQEEL 833
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512
|
490 500
....*....|....*....|....
gi 1720385250 834 AGMRR--------CSETSSKLEED 849
Cdd:pfam01576 513 RNVERqlstlqaqLSDMKKKLEED 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
404-830 |
3.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 404 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDtlcLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSV-QKQMKLGL 482
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL---LQLLPLYQELEALEAELAELPERLEELEERLEELrELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 LSQESADGYSHLREAPADEDIDTLKQdLQKAVEESARNKERVRELETKLAEKEqaeatkppaEACEELRSSYCSVIENMN 562
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQRLAELEEELEEAQ---------EELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 563 KEKafLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELnkqVSELSQLYREAQAELEDYRKRKSLEDA 642
Cdd:COG4717 238 AAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 643 AEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLvdahkENSVSITEHLQVITTLRTTAK----EME 718
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----EEELQLEELEQEIAALLAEAGvedeEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 719 EKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSsyeklQASLESEVNALATKLKESVREREKAHSEVAQVRSEV 798
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....
gi 1720385250 799 SQARREK--DNIQTLLKAKEQEVTALVQKFQRAQ 830
Cdd:COG4717 463 EQLEEDGelAELLQELEELKAELRELAEEWAALK 496
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
499-867 |
3.82e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 499 ADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAtkppaeaceELRSSYCSVIENMNKEKAFL--FEKYQQAQ 576
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES---------DLEQDYQAASDHLNLVQTALrqQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 577 EEIMKLKDTLKSQM-----PQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEyihkaeh 651
Cdd:PRK04863 355 ADLEELEERLEEQNevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAK------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 652 eRLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTL---------RTTAKEME---E 719
Cdd:PRK04863 428 -QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIagevsrseaWDVARELLrrlR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 720 KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAmvpkSSYEK---LQASLESEVNALATKLKESVREREKAHSEVAQVRS 796
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL----AEFCKrlgKNLDDEDELEQLQEELEARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720385250 797 EVSQARREkdniqtlLKAKEQEVTALVQKFQRAQEELAGMRRCS----ETSSKLEE---DKDEKINEMTREVLKLKEA 867
Cdd:PRK04863 583 ALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSgeefEDSQDVTEymqQLLERERELTVERDELAAR 653
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
100-238 |
4.07e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 100 ECIRKLLQYKSPAENID-NSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADV 178
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720385250 179 NSRDKNGRTALMLAceTGSSNTVDA---LIKKGADLSLVDS-LGHNALHYSKLSENagIQNLLL 238
Cdd:PHA02878 228 DARDKCGNTPLHIS--VGYCKDYDIlklLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLL 287
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
145-240 |
4.48e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.49 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 145 INLKDLDGNIPLLVAVQNGHS---EACHFLLDHGADVNSRDKNGRTALMLACETGSS-NTVDALIKKGADLSLVDSLGHN 220
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRT 119
|
90 100
....*....|....*....|..
gi 1720385250 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 ... |
608-867 |
8.14e-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: 53.15 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 608 MIDELNKQVSELsqlyREAQAELEDYRK-RKSLEDAAEYIH---KAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNEL 683
Cdd:TIGR02169 192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 684 TQLKQLVDAHKENSVSITEHLQVitTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVS--DAMVPKS---- 757
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDklLAEIEELerei 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 758 -SYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGM 836
Cdd:TIGR02169 346 eEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
250 260 270
....*....|....*....|....*....|....*
gi 1720385250 837 R----RCSETSSKLEEDKDEKINEMTREVLKLKEA 867
Cdd:TIGR02169 426 NaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
132-240 |
8.40e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.53 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 132 LQAVQLLCEHKSPINLKDLDGNIPLLVAVQN----GHS-EACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDAL-- 204
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720385250 205 -IKKGADLSLVDSLGHNALH-YSKLSENAGIQ--NLLLSK 240
Cdd:PHA02798 131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-83 |
8.65e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 8.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQD 83
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-829 |
1.26e-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: 51.69 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 592 QEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRksLEDAAEYIHKAEHERLMHVSNLSRAKSEEA--- 668
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIRALEQELAALEAELAELEKEIAelr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 669 --LSEMKSQYSKVLNELTQLKQLVD-AHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLankeAEVAKLEKQLAEE 745
Cdd:COG4942 97 aeLEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 746 KAAVsdamvpkssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQK 825
Cdd:COG4942 173 RAEL----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 1720385250 826 FQRA 829
Cdd:COG4942 243 TPAA 246
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-206 |
1.75e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 127 AAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIK 206
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
467-866 |
1.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 467 AMKEVLSVQKQMKLGLLSQ----ESADGYSHL-----REAPADEDIDTL-------KQDLQKAVEESARNKERVRELETK 530
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQieekEEKDLHERLnglesELAELDEEIERYeeqreqaRETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 531 LAEKEQAEATKPPAE---------------ACEELRSSYCSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSQMPQEAP 595
Cdd:PRK02224 257 EAEIEDLRETIAETErereelaeevrdlreRLEELEEERDDLLAEAGLDDADA-EAVEARREELEDRDEELRDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 596 DDSGDMKEAMN--RMIDELNKQVSELSQLYREAQAELEDYRK-------------------RKSLEDAAEYIHKAEHERL 654
Cdd:PRK02224 336 AAQAHNEEAESlrEDADDLEERAEELREEAAELESELEEAREavedrreeieeleeeieelRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 655 MHVSNLSRAKSEEAlsEMKSQYSKVLNELTQLKQLVDAHK----ENSVSITEHLQVITtlrttakEMEEKISALTGHLAN 730
Cdd:PRK02224 416 ELREERDELREREA--ELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIE-------EDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 731 KEAEVAKLEKQLAEEKAAVsdamvpkssyeklqaSLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQT 810
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720385250 811 LLKAKEQEVTALVQKFQRAQEELAGM-RRCSETSSKLE-----EDKDEKINEMTREVLKLKE 866
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERLRE 613
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
403-867 |
1.88e-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: 51.89 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGSDLSQKL-KETQSKYEEAMKEVLSVQKQMKLG 481
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 482 LlsQESADGYSHLREAPADEDIDTLKQDLQKAVEESARN---------KERVRELETKLAEKEQAEATKPPAEACEELRS 552
Cdd:TIGR00618 461 L--QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLelqeepcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 553 SYCSVIENMnkekaflfekYQQAQEEIMKLKdTLKSQMpQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEd 632
Cdd:TIGR00618 539 QLETSEEDV----------YHQLTSERKQRA-SLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE- 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 633 YRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEaLSEMKSQYSKVLNELTQLKQlvdahKENSVSITE-HLQVITTLR 711
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-LALKLTALHALQLTLTQERV-----REHALSIRVlPKELLASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 712 TTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREkahsEV 791
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR----TV 755
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 792 AQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEA 867
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
91-185 |
1.97e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 91 HVAAkNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHF 170
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1720385250 171 LLDHGADVNSRDKNG 185
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
462-857 |
2.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 462 SKYEEAMKEVLSVQKQmKLGLLSQESADGYSHLREAPADED-IDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAT 540
Cdd:COG4717 49 ERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEeYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 541 KPPAEACEELRSSYCSVIENMNKEKA------FLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRmIDELNK 614
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEErleelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 615 QVSELSQLYREAQAELEDYRKR-KSLEDAAEyihkaeherlmhvsnlsRAKSEEALSEMKSQYsKVLNELTQLKQLVDAH 693
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEElEQLENELE-----------------AAALEERLKEARLLL-LIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 694 KENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEK-QLAEEKAAVSDAMVPkssyeklqaslESEVNA 772
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP-----------PDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 773 LATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDE 852
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
....*
gi 1720385250 853 KINEM 857
Cdd:COG4717 418 LEELL 422
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
19-220 |
2.22e-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: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTH-----GVDVTAQDSSGHSALHVA 93
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 94 AKNGHPECIRKLLQY----KSP----------AENIDNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPL-LV 158
Cdd:cd22192 97 VVNQNLNLVRELIARgadvVSPratgtffrpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 159 AVQNGHSEACH---FLLDHGADVNS------RDKNGRTALMLACETGSSNTVDALIKKGA--------------DLSLVD 215
Cdd:cd22192 177 VLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKRRhiqwtygpltstlyDLTEID 256
|
....*
gi 1720385250 216 SLGHN 220
Cdd:cd22192 257 SWGDE 261
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-141 |
2.26e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLKVMVTHGVDVTAQDSSG 86
Cdd:PTZ00322 43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720385250 87 HSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-93 |
2.30e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 2.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1720385250 50 DSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVA 93
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-238 |
2.57e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.76 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 60 AAAKGHVECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQGCLQAVQLLC 139
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 140 EHKSPINlkDL---DGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDS 216
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180
....*....|....*....|..
gi 1720385250 217 LGHNALHYSKLSENAGIQNLLL 238
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLL 188
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
2.64e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 2.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 105 LLQYKSPAENI-DNSGKTALHYAAAQGCLQAVQLLCEHKSPINLKDLDGNIPLLVA 159
Cdd:pfam13857 1 LLEHGPIDLNRlDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
661-838 |
2.70e-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: 50.53 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 661 SRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEK 740
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 741 QLAEEKAAVSDAMV----------------PKSS---------YEKLQASLESEVNALATKLKESVREREKAHSEVAQVR 795
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllsPEDFldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720385250 796 SEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 838
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
609-834 |
2.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 609 IDELNKQVSELSQLYREAqaeLEDYRKRKSLEDAAEYI--HKAEHERLMHVSNLSRA----KSEEALSEMKSQYSKVLNE 682
Cdd:COG4913 227 ADALVEHFDDLERAHEAL---EDAREQIELLEPIRELAerYAAARERLAELEYLRAAlrlwFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 683 LTQLKQLVDAHKENSVSITEHLQVITTLRTTA-----KEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAmvpKS 757
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 758 SYEKLQAslesEVNALATKLKEsvrEREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 834
Cdd:COG4913 381 EFAALRA----EAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
3.46e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.26 E-value: 3.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 189 LMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSKISQDADLKTPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
403-869 |
4.04e-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: 50.84 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNnTEISENGSD---LSQKLKETQSKYEEAMKEVLSVQKQmk 479
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE-REIEEERKRrdkLTEEYAELKEELEDLRAELEEVDKE-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 480 lgllSQESADGYSHLREAPAD--EDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEAtkppaeaceELRSsycsv 557
Cdd:TIGR02169 380 ----FAETRDELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN---------ELEE----- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 558 ienmnkEKAFLFEKYQQAQEEIMKLKDTLKSqmpqeAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRK 637
Cdd:TIGR02169 442 ------EKEDKALEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 638 S----LEDAAEYIH---------KAEHERLMHVSNLSRAKS----EEALSEMKSQYSKV----------LNELTQLKQLV 690
Cdd:TIGR02169 511 AveevLKASIQGVHgtvaqlgsvGERYATAIEVAAGNRLNNvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 691 DAHKENSVsITEHLQVIT-----------TLRTTAkeMEEKISALTGHLANkeAEVAKLEKQLAEEKAAVSDAMVPKSSY 759
Cdd:TIGR02169 591 SILSEDGV-IGFAVDLVEfdpkyepafkyVFGDTL--VVEDIEAARRLMGK--YRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 760 EKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAG-MRR 838
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEElEED 745
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720385250 839 CSETSSKLEEDKDE------KINEMTREVLKLKEALN 869
Cdd:TIGR02169 746 LSSLEQEIENVKSElkeleaRIEELEEDLHKLEEALN 782
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-240 |
4.47e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.22 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLKVMVTHGVDVTAQDSSGHSALHVAAKNGHP---ECIRKLLQY 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 109 KSPAENIDNS-GKTALH--YAAAQGCLQA--VQLLCEHKSPINLKD-------LDGNIPLLVAVQNGHSEACHFLLDHgA 176
Cdd:PHA02798 171 GVDINTHNNKeKYDTLHcyFKYNIDRIDAdiLKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720385250 177 DVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSENAGIQNLLLSK 240
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
491-838 |
7.65e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 491 YSHLREAPA------DEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKP-------PAEACEELRSSycsv 557
Cdd:PRK04863 770 YSRFPEVPLfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadPEAELRQLNRR---- 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 558 IENMNKEKAFLFEKYQQAQEEImklkDTLKSQMpqeapddsgdmkEAMNRMIDELNK-QVSELSQLYREAQAELEdyrkr 636
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQL----EQAKEGL------------SALNRLLPRLNLlADETLADRVEEIREQLD----- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 637 kSLEDAAEYI--HKAEHERLMHVSNLSRAkSEEALSEMKSQYSKVLNELTQLKQLVDAHKEnSVSITEHLQVITTLRTTA 714
Cdd:PRK04863 905 -EAEEAKRFVqqHGNALAQLEPIVSVLQS-DPEQFEQLKQDYQQAQQTQRDAKQQAFALTE-VVQRRAHFSYEDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 715 KEmEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDamvpkssYEKLQASLESEVNALATKLKESVRE----------- 783
Cdd:PRK04863 982 KN-SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ-------YNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsg 1053
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 784 -REKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 838
Cdd:PRK04863 1054 aEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
403-866 |
9.43e-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: 49.66 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 479
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 480 LGLLSQESADGYS-------------HLREAPAD-EDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAE 545
Cdd:TIGR00606 666 SQFITQLTDENQSccpvcqrvfqteaELQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 546 aCEELRSSYCSVIENMNKEKAFLFEKYQQ-----AQEEI---------------MKLKDTLKSQMPQEAPDDSGDmkeaM 605
Cdd:TIGR00606 746 -IPELRNKLQKVNRDIQRLKNDIEEQETLlgtimPEEESakvcltdvtimerfqMELKDVERKIAQQAAKLQGSD----L 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 606 NRMIDELNKQVSELSQLYREAQAELEDYRK-----RKSLEDAAEYIHKAEHERLMHVSNLSRA-----KSEEALSEMKSQ 675
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdqQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfeeQLVELSTEVQSL 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 676 YSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKaavsdamvp 755
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKD---QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK--------- 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 756 kssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEV-SQARRE---KDNIQtlLKAKEQEVTALVQKFQRAQE 831
Cdd:TIGR00606 969 ----DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdTQKIQErwlQDNLT--LRKRENELKEVEEELKQHLK 1042
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720385250 832 ELAGMRRCSETSS--KLEEDKDEKINEMTREVLKLKE 866
Cdd:TIGR00606 1043 EMGQMQVLQMKQEhqKLEENIDLIKRNHVLALGRQKG 1079
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
600-834 |
9.79e-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: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 600 DMKEAMNRMID---ELNKQVSELsqlyrEAQAEL-EDYR-KRKSLEDAAEYIHKAEHERLmhvsnlsrakseealsemKS 674
Cdd:TIGR02168 183 RTRENLDRLEDilnELERQLKSL-----ERQAEKaERYKeLKAELRELELALLVLRLEEL------------------RE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 675 QYSKVLNELTQLKQLVDAHKENsvsITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMV 754
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 755 PKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 834
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
406-869 |
1.38e-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: 49.35 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 406 LQDSLHDLQKRLESSEAEKKQLQD----ELQSQRTDTLCLNNT--EISENGSDLSQKLKETQSKYEEAMKEVLS---VQK 476
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADirrrESQSQEDLRNQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLShegVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 477 QMKLGLLSQESADGyshlREAPADEDIDTLK-QDLQKAVEESarnkerVRELETKLAE--------KEQAEATKPPAE-A 546
Cdd:pfam15921 188 EIRSILVDFEEASG----KKIYEHDSMSTMHfRSLGSAISKI------LRELDTEISYlkgrifpvEDQLEALKSESQnK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 547 CEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMP--QEAPDDSGDMkeaMNRMIDELNKQVSELSQLYR 624
Cdd:pfam15921 258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiQEQARNQNSM---YMRQLSDLESTVSQLRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 625 EA----QAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSI 700
Cdd:pfam15921 335 EAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 701 tEHL-----------QVITTLRTTAK-----EMEEKISALTGHLANKEaEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQA 764
Cdd:pfam15921 415 -DHLrrelddrnmevQRLEALLKAMKsecqgQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 765 SLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQT---LLKAKEQEVTALVQKFQRAQEELAGMRRCSE 841
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNegdHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
490 500
....*....|....*....|....*...
gi 1720385250 842 TSSKLEEDKDEKINEMTREVLKLKEALN 869
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
1.52e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 1.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1720385250 145 INLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-834 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLclnNTEISENGSDLS---QKLKETQSKYEEAMKEVLSVQKQMk 479
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELL---EAELEELRAELArleAELERLEARLDALREELDELEAQI- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 480 lgllsqeSADGYShlREAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppAEACEELRSSYCSVIE 559
Cdd:COG4913 333 -------RGNGGD--RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL--RAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 560 NMNKEKAFLFEKYQQAQEEIMKLKDTL------KSQMPQEapddsgdMKEAMNRMIDELNKQVSELSQLyreaqAEL--- 630
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIaslerrKSNIPAR-------LLALRDALAEALGLDEAELPFV-----GELiev 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 631 --EDYRKRKSLE------------------DAAEYI---HKAEHERLMHVSNLSRAKSEEALSE------MKSQYSKVLN 681
Cdd:COG4913 470 rpEEERWRGAIErvlggfaltllvppehyaAALRWVnrlHLRGRLVYERVRTGLPDPERPRLDPdslagkLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 682 EL-TQLKQLVDAHKENSV--------SITEHLQVitTLRTTAKEM----------------EEKISALTGHLANKEAEVA 736
Cdd:COG4913 550 WLeAELGRRFDYVCVDSPeelrrhprAITRAGQV--KGNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 737 KLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATK-----LKESVREREKAHSEVAQVRSEVSQARREKDNIQTL 811
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLAALEEQLEELEAELEELEEE 707
|
490 500
....*....|....*....|...
gi 1720385250 812 LKAKEQEVTALVQKFQRAQEELA 834
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 |
2.40e-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: 41.80 E-value: 2.40e-05
10 20 30
....*....|....*....|....*....|
gi 1720385250 52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-183 |
3.01e-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: 3.01e-05
10 20 30
....*....|....*....|....*....|....
gi 1720385250 151 DGNIPLLVAV-QNGHSEACHFLLDHGADVNSRDK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
678-834 |
3.44e-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: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 678 KVLNELTQLKQLVDAHKEnsvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKS 757
Cdd:COG1579 14 ELDSELDRLEHRLKELPA---ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 758 sYEKLQ---ASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELA 834
Cdd:COG1579 91 -YEALQkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
503-857 |
3.50e-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: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 503 IDTLKQDLQKAVEE--------------SARNKERVRELETKLAEKEQAEATkppaeaceeLRSSYCSVIENMNKEKAFL 568
Cdd:pfam10174 291 IDQLKQELSKKESEllalqtkletltnqNSDCKQHIEVLKESLTAKEQRAAI---------LQTEVDALRLRLEEKESFL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 569 FEKYQQAQEeIMKLKDTLKSQMpqeapDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAAEyih 647
Cdd:pfam10174 362 NKKTKQLQD-LTEEKSTLAGEI-----RDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERvKSLQTDSS--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 648 kaeherlmhVSNLSRAKSEEALSEMKsqysKVLNELTQLKQLVDahkensvsiTEHLQVITTLRTTAKEMEEKISALTGH 727
Cdd:pfam10174 433 ---------NTDTALTTLEEALSEKE----RIIERLKEQRERED---------RERLEELESLKKENKDLKEKVSALQPE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 728 LANKEAEVAKLEkqlaEEKAAVSDAMVPKSSYEK-LQASLES---EVNALATKLKesvrereKAHsevaqvrsEVSQARR 803
Cdd:pfam10174 491 LTEKESSLIDLK----EHASSLASSGLKKDSKLKsLEIAVEQkkeECSKLENQLK-------KAH--------NAEEAVR 551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 804 EKDNIQTLLKAKEQEVTALVQKFQRAQ---EELAGMRRCSETSsklEEDKDEKINEM 857
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKAQaevERLLGILREVENE---KNDKDKKIAEL 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
459-911 |
4.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 459 ETQSKYEEAMKEVLSVQKQMKLgllsqESADGYSHLREAPADEDiDTLKQDLQKAveESARNKERVRELEtklaEKEQAE 538
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEA-----RKAEDARKAEEARKAED-AKRVEIARKA--EDARKAEEARKAE----DAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 539 ATKPPAEA--CEELRSSYcsviENMNKEKAFLFEKYQQAqEEIMKLKDTLKSQMPQEAPDDSGDMKEAMN----RMIDEL 612
Cdd:PTZ00121 1180 AARKAEEVrkAEELRKAE----DARKAEAARKAEEERKA-EEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeeRNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 613 NKQVSELSQLYREAQAELEDYRKRKsledaAEYIHKAEHERlmhvsnlsraKSEEAlseMKSQYSKVLNELTQLKQLVDA 692
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARK-----ADELKKAEEKK----------KADEA---KKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 693 HKENSVSITEHLQVITTLRTTAKEMEEKISAltghlANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNA 772
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEA-----AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 773 LATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA-LVQKFQRAQEELAGMRRCSETSSKLEE-DK 850
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEaKK 1471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 851 DEKINEMTREVLKLKEALNSLSQLSYSTSSSKRQSQQLDLLQQQVKQLQNQLAECKKHHQE 911
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-691 |
5.61e-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: 47.37 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 402 IIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDT----LCLNNTEISENGSdlsqKLKETQSKYEEAMKEVLSVQKQ 477
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleEALNDLEARLSHS----RIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 478 mklgLLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARNKERV-------RELETKLAEKEQAEatkppaeacEEL 550
Cdd:TIGR02169 814 ----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkkEELEEELEELEAAL---------RDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 551 RSSYCSV---IENMNKEKAFLFEKYQQAQEEIMKLKDTLKsqmpqeapddsgDMKEAmnrmideLNKQVSELSQLYREAQ 627
Cdd:TIGR02169 881 ESRLGDLkkeRDELEAQLRELERKIEELEAQIEKKRKRLS------------ELKAK-------LEALEEELSEIEDPKG 941
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720385250 628 AELEDYRKRKSLEDAAEYIHKAEHE--RLMHVSNLS---RAKSEEALSEMKSQYSKVLNELTQLKQLVD 691
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEirALEPVNMLAiqeYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
602-868 |
7.21e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 602 KEAMNRM-------------IDELNKQVSELS------QLYREAQAELEDYrkrksleDAAEYIHKAEHERLmhvsNLSR 662
Cdd:COG1196 175 EEAERKLeateenlerlediLGELERQLEPLErqaekaERYRELKEELKEL-------EAELLLLKLRELEA----ELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 663 AKSEEALSEMKsqyskvLNELTQLKQLVDAHKEnsvsitehlqvitTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQL 742
Cdd:COG1196 244 LEAELEELEAE------LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 743 AEEkaavsdamvpkssyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTAL 822
Cdd:COG1196 305 ARL--------------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720385250 823 VQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 868
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
100-274 |
8.01e-05 |
|
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: 46.41 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 100 ECIRKLLQ---YKSPAenidnSGKTALHYAA---AQGCLQAVQLLCE-HKSPINLKDL----------DGNIPLLVAVQN 162
Cdd:cd21882 9 ECLRWYLTdsaYQRGA-----TGKTCLHKAAlnlNDGVNEAIMLLLEaAPDSGNPKELvnapctdefyQGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 163 GHSEACHFLLDHGADVNSR------DKNGRTA-------LMLACETGSSNTVDALIKKGAD---LSLVDSLGHNALHYSK 226
Cdd:cd21882 84 RNLNLVRLLVENGADVSARatgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720385250 227 LSENAGIQNLLLSK------ISQDADLkTPTKPkqLSDVSSPRSITSTPLSGKE 274
Cdd:cd21882 164 LQADNTPENSAFVCqmynllLSYGAHL-DPTQQ--LEEIPNHQGLTPLKLAAVE 214
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
418-814 |
8.88e-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: 46.21 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 418 ESSEAEKK--QLQDELQSQRTdtlclNNTEISENGSDLSQKLKETQSKYEEAMKevlsvqKQMKLGLLSQESADGYSHLR 495
Cdd:pfam13166 90 ESIEIQEKiaKLKKEIKDHEE-----KLDAAEANLQKLDKEKEKLEADFLDECW------KKIKRKKNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 496 EAPADE-DIDTLKQDLQKAVEESarNKERVRELETKLAEKEQAEATKPP--------AEACEELRSS---YCSVIENMNK 563
Cdd:pfam13166 159 EANFKSrLLREIEKDNFNAGVLL--SDEDRKAALATVFSDNKPEIAPLTfnvidfdaLEKAEILIQKvigKSSAIEELIK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 564 EkAFLFEKYQQAQEEIMKLKDTL---KSQMPQEA--------PDDSGDMKEAMNRMIDELNKQVSELSQLYreaQAELED 632
Cdd:pfam13166 237 N-PDLADWVEQGLELHKAHLDTCpfcGQPLPAERkaaleahfDDEFTEFQNRLQKLIEKVESAISSLLAQL---PAVSDL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 633 YRKRKSLEDAAEYIHKAEHERLMHVSNLSR---AKSEEALSEmkSQYSKVLNELTQLKQLVDAhkensvsitehlqvitt 709
Cdd:pfam13166 313 ASLLSAFELDVEDIESEAEVLNSQLDGLRRaleAKRKDPFKS--IELDSVDAKIESINDLVAS----------------- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 710 lrttakeMEEKISALTGHLANKEAEVAKLEKQLaeEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHS 789
Cdd:pfam13166 374 -------INELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLRE 444
|
410 420
....*....|....*....|....*
gi 1720385250 790 EVAQVRSEVSQARREKDNIQTLLKA 814
Cdd:pfam13166 445 EIKELEAQLRDHKPGADEINKLLKA 469
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
669-818 |
1.54e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 669 LSEMKSQYSKVLNELT-QLKQLVDAhkensvsitehlqvITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKA 747
Cdd:PRK09039 44 LSREISGKDSALDRLNsQIAELADL--------------LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 748 AVSDAmvpkssyeklqaslESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQE 818
Cdd:PRK09039 110 AGAAA--------------EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKR 166
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
1.90e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 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 |
2.20e-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: 2.20e-04
10 20
....*....|....*....|....*....
gi 1720385250 151 DGNIPLLVAVQNGHSEACHFLLDHGADVN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
129-232 |
2.34e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.05 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 129 QGCLQAVQLLCEHKSPINLKDLDGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKG 208
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100
....*....|....*....|....*....
gi 1720385250 209 A-----DLSLVDSLGHNALHYSKLSENAG 232
Cdd:PHA02876 235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
421-761 |
2.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 421 EAEKKQLQDELQSQrtdtlclnnTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGllSQESADGYSHLREAPAD 500
Cdd:PTZ00121 1465 KAEEAKKADEAKKK---------AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 501 EDIDTLK--QDLQKAVE----ESARNKERVRELETKLAEKEQAEATKPPAEACEEL-RSSYCSVIENMNKEKAFLFEKYQ 573
Cdd:PTZ00121 1534 KKADEAKkaEEKKKADElkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAK 1613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 574 QAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQvSELSQLYREAQAELEDYRKRKsledaAEYIHKAEHEr 653
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKK-----AEEAKKAEED- 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 654 lmhvsnlsRAKSEEALSEMKSQYSKVlnELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHL----A 729
Cdd:PTZ00121 1687 --------EKKAAEALKKEAEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeeK 1756
|
330 340 350
....*....|....*....|....*....|..
gi 1720385250 730 NKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEK 761
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-595 |
3.23e-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: 43.98 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELQ------SQRTDTLCLNNTEISENGSDLSQ------KLKETQSKYEEAMKE 470
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAalerriAALARRIRALEQELAALEAELAElekeiaELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 471 VLSV------QKQMKLGLLSQESADGYSHLRE----APADED-IDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEA 539
Cdd:COG4942 109 LLRAlyrlgrQPPLALLLSPEDFLDAVRRLQYlkylAPARREqAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 540 TKppaeacEELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAP 595
Cdd:COG4942 189 AL------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
528-802 |
3.33e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 528 ETKLA-EKEQAEATKPP--AEACEELRSSYCSVIENmnKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEaPDDSGDMKEA 604
Cdd:PRK10929 25 EKQITqELEQAKAAKTPaqAEIVEALQSALNWLEER--KGSLERAKQYQQVIDNFPKLSAELRQQLNNE-RDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 605 MNrmIDELNKQV----SELSQLYREAQAELEDYRK-RKSL-------EDAAEYIHKAEhERLMHVSN----LSRAKSEEA 668
Cdd:PRK10929 102 MS--TDALEQEIlqvsSQLLEKSRQAQQEQDRAREiSDSLsqlpqqqTEARRQLNEIE-RRLQTLGTpntpLAQAQLTAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 669 LSEMKSQYSKVlNELtQLKQLVDAHKensvsitehlQVITTLRT-TAKEMEEKISALTGHLAN-------KEAEVAkLEK 740
Cdd:PRK10929 179 QAESAALKALV-DEL-ELAQLSANNR----------QELARLRSeLAKKRSQQLDAYLQALRNqlnsqrqREAERA-LES 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385250 741 --QLAEEKAAvsdamVPKSSYEKLQAS--LESEVNALATKLKESVREREKAHSEVAQVRSEVSQAR 802
Cdd:PRK10929 246 teLLAEQSGD-----LPKSIVAQFKINreLSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLR 306
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
3.41e-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: 3.41e-04
10 20 30
....*....|....*....|....*....|...
gi 1720385250 52 EGKTAFHLAAAK-GHVECLKVMVTHGVDVTAQD 83
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-211 |
3.46e-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: 3.46e-04
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
405-832 |
3.57e-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: 44.72 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 405 QLQDSLHDLQKRLESSEAEKKQlqdelQSQRTDTLCLNNTEISENGSDLSQKLKETQsKYEEAMKEVLS-----VQKQMK 479
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQ-----NKRLWDRDTGNSITIDHLRRELDDRNMEVQ-RLEALLKAMKSecqgqMERQMA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 480 LGLLSQESADGYSHLreapaDEDIDTLKQDLQKAVEE------SARNKER-VRELETKLAEKEQA-EATKPPAEACEELR 551
Cdd:pfam15921 452 AIQGKNESLEKVSSL-----TAQLESTKEMLRKVVEEltakkmTLESSERtVSDLTASLQEKERAiEATNAEITKLRSRV 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 552 SSYCSVIENMNKEKAFLfeKYQQAQEEIMKLKDTLK--------------SQMPQEAPDDSGDM---KEAMNRMIDELNK 614
Cdd:pfam15921 527 DLKLQELQHLKNEGDHL--RNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMqveKAQLEKEINDRRL 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 615 QVSELSQLYREAQAELEDYRKRKS-LEDAAEYIHKAEHERLMHVSNLSRAKsEEALSEMKSQYskvlNELTQLKQLVDAH 693
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEARVSdLELEKVKLVNAGSERLRAVKDIKQER-DQLLNEVKTSR----NELNSLSEDYEVL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 694 KENSVSITEHLQVITT-----LRTTAKEMEEK---ISALTGHLANKEAEVAKLEKQLAEEKAAVsDAMVPKSSY------ 759
Cdd:pfam15921 680 KRNFRNKSEEMETTTNklkmqLKSAQSELEQTrntLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQSKIQFleeamt 758
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720385250 760 --EKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEE 832
Cdd:pfam15921 759 naNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
636-867 |
3.63e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 636 RKSLEDAAEYIHKAEherLMHVSNLSRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHK-----ENSVSITEHLQVITTL 710
Cdd:PRK05771 15 KSYKDEVLEALHELG---VVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 711 RTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE-----------------EKAAVSDAMVPKSSYEKLQASLESEVNAL 773
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 774 ATKLKESV-------REREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAgmrrcsETSSKL 846
Cdd:PRK05771 172 ISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELK------ELAKKY 245
|
250 260
....*....|....*....|....*
gi 1720385250 847 EEDK---DEKI-NEMTREVLKLKEA 867
Cdd:PRK05771 246 LEELlalYEYLeIELERAEALSKFL 270
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-654 |
4.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQDELqsqrtdtlclnnteisengsDLSQKLKEtqskYEEAMKEVLSVQKQmkLGL 482
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERR--------------------EALQRLAE----YSWDEIDVASAERE--IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 LSQEsadgYSHLREAPAdeDIDTLKQDLQKAVEESARNKERVRELETKLA--EKEQAEATkppaEACEELRSSYCSVIEN 560
Cdd:COG4913 673 LEAE----LERLDASSD--DLAALEEQLEELEAELEELEEELDELKGEIGrlEKELEQAE----EELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 561 MNKEKAFLFEKYQQAQeeimkLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDyrkrkSLE 640
Cdd:COG4913 743 ARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA-----DLE 812
|
250
....*....|....
gi 1720385250 641 DAAEYIhkAEHERL 654
Cdd:COG4913 813 SLPEYL--ALLDRL 824
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
716-813 |
5.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 716 EMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDamvpkssyeklqasLESEVNALATKLKESVREREKAHS---EVA 792
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER--------------LERELSEARSEERREIRKDREISRldrEIE 475
|
90 100
....*....|....*....|.
gi 1720385250 793 QVRSEVSQARREKDNIQTLLK 813
Cdd:COG2433 476 RLERELEEERERIEELKRKLE 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
616-866 |
5.89e-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: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 616 VSELSQLYREAQAEledyRKRKSLEDAAEYIhkaeherlmhvsnlsraksEEALSEMKSQYSKVLNELTQLKQlvdahKE 695
Cdd:COG3206 154 ANALAEAYLEQNLE----LRREEARKALEFL-------------------EEQLPELRKELEEAEAALEEFRQ-----KN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 696 NSVSITEHLQVITTlrtTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVpkssyEKLQASLESEVNALAT 775
Cdd:COG3206 206 GLVDLSEEAKLLLQ---QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 776 KLKESVREREKAHSEVAQVRSEVSQARRE-KDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRrcsetsskleedkdEKI 854
Cdd:COG3206 278 ELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLE--------------ARL 343
|
250
....*....|..
gi 1720385250 855 NEMTREVLKLKE 866
Cdd:COG3206 344 AELPELEAELRR 355
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
89-326 |
6.34e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.50 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 89 ALHVAAKNGHPECIRKLLQYKSPAENIDnsgktALH-YAAAQGCLQAV--QLLCEHKSPiNLKDLDGNIPLLVAVQNGHS 165
Cdd:PHA02946 12 SLYAKYNSKNLDVFRNMLQAIEPSGNYH-----ILHaYCGIKGLDERFveELLHRGYSP-NETDDDGNYPLHIASKINNN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 166 EACHFLLDHGADVNSRDKNGRTAL-----------------------------------MLACETGSSNTVDALIKKGAD 210
Cdd:PHA02946 86 RIVAMLLTHGADPNACDKQHKTPLyylsgtddevierinllvqygakinnsvdeegcgpLLACTDPSERVFKKIMSIGFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 211 LSLVDSLGHNALHYSKLSEN------AGIQNLLLSKISQDADLKTPTK---PKQLSDVSSPRSITSTPLSGKESVfFAEA 281
Cdd:PHA02946 166 ARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTPLHivcSKTVKNVDIINLLLPSTDVNKQNK-FGDS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720385250 282 PFKAEISSIQE----NKdRLSDSTAGADSLLDISSEADQQDLLVLLQAK 326
Cdd:PHA02946 245 PLTLLIKTLSPahliNK-LLSTSNVITDQTVNICIFYDRDDVLEIINDK 292
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-149 |
9.11e-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: 9.11e-04
10 20 30
....*....|....*....|....*....|..
gi 1720385250 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 |
1.09e-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: 1.09e-03
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
450-835 |
1.30e-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: 42.65 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 450 GSDLSQKLKETQSKYEEAMKevLSVQKQMKLGLLSQESADGYshLREAPADEDIDTLK-QDLQKAVEESARNKERVRELE 528
Cdd:TIGR00618 118 GRILAAKKSETEEVIHDLLK--LDYKTFTRVVLLPQGEFAQF--LKAKSKEKKELLMNlFPLDQYTQLALMEFAKKKSLH 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 529 TKL-AEKEQAEATKPPAEaceELRSSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpQEAPDDSGDMKEAMNR 607
Cdd:TIGR00618 194 GKAeLLTLRSQLLTLCTP---CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ--EEQLKKQQLLKQLRAR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 608 mIDELNKQVSELSQLYRE-----------------AQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKSEEALS 670
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERinrarkaaplaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 671 EMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLankEAEVAKLEKQLAEEKAAVS 750
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL---QREQATIDTRTSAFRDLQG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 751 DAMVPKSSyEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQ 830
Cdd:TIGR00618 425 QLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
....*
gi 1720385250 831 EELAG 835
Cdd:TIGR00618 504 CPLCG 508
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
1.32e-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: 1.32e-03
10 20 30
....*....|....*....|....*....|...
gi 1720385250 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 |
1.36e-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: 1.36e-03
10 20
....*....|....*....|....*....
gi 1720385250 184 NGRTALMLACETGSSNTVDALIKKGADLS 212
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
502-866 |
1.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 502 DIDTLKQDLQKAVEESARNKERVRELETKLAEKEqaeatkppaeaceelrssycsvienmnKEKAFLFEKYQQAQEEIMK 581
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEKSHSITL---------------------------KEIERLSIEYNNAMDDYNN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 582 LKDTLKSQMPQEapddsgdmkeamnrmiDELNKQVSELSQLYREAQAELEDYRKRKSLEdaaeyihkaehERLMHVSNLS 661
Cdd:PRK01156 237 LKSALNELSSLE----------------DMKNRYESEIKTAESDLSMELEKNNYYKELE-----------ERHMKIINDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 662 RAKSEEALSEmksqYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEkisaltghlanKEAEVAKLEKQ 741
Cdd:PRK01156 290 VYKNRNYIND----YFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIK-----------KKSRYDDLNNQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 742 LAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA 821
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720385250 822 LVQK---FQRAQEELAGMRRCSETSSKLEEDK---------------DEKINEMTREVLKLKE 866
Cdd:PRK01156 435 LRENldeLSRNMEMLNGQSVCPVCGTTLGEEKsnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
405-741 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 405 QLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNN--TEISENGSDLSQKLKETQSKYEEAMKEVLSVQ------K 476
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERqrRELESRVAELKEELRQSREKHEELEEKYKELSasseelS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 477 QMKLGLLSQEsADGYSHLREApaDEDIDTLKQDLQKAVEESARNKERVRELETKLAEKE-QAEATKPPAEACEELRSSYC 555
Cdd:pfam07888 115 EEKDALLAQR-AAHEARIREL--EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 556 SVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDS--------------------------GDMKEAMNRMI 609
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAlleelrslqerlnaserkveglgeelSSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 610 DELNK----------QVSELSQLYREAQAELEdyRKRKSLEDAAEyihkAEHERLMHVSNlSRAKSEEALSEMKSQYSKV 679
Cdd:pfam07888 272 AELHQarlqaaqltlQLADASLALREGRARWA--QERETLQQSAE----ADKDRIEKLSA-ELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720385250 680 LNELTQLKQLvdahkeNSVSITEhlqvittlrtTAKEMEEKISALtgHLANKEAEVAKLEKQ 741
Cdd:pfam07888 345 EVELGREKDC------NRVQLSE----------SRRELQELKASL--RVAQKEKEQLQAEKQ 388
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
403-629 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 403 IRQLQDSLHDLQKRLESSEAEKKQLQdelqsQRTDTLclnntEISENGSDLSQKLKETQSKYEEAmkEVLSVQKQMKLGL 482
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFR-----QKNGLV-----DLSEEAKLLLQQLSELESQLAEA--RAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 483 LSQESADGYSHLREAPADEDIDTLKQDLQKA----VEESARNKE---RVRELETKLAEKEQaeatkppaeaceELRSSYC 555
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELeaelAELSARYTPnhpDVIALRAQIAALRA------------QLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720385250 556 SVIENMNKEKAFLfekyQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEaMNRMIDELNKQVSELSQLYREAQAE 629
Cdd:COG3206 313 RILASLEAELEAL----QAREASLQAQLAQLEARL-AELPELEAELRR-LEREVEVARELYESLLQRLEEARLA 380
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
520-751 |
1.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 520 NKERVREL----------------ETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKEKAFLfekyQQAQEEIMKLk 583
Cdd:PHA02562 172 NKDKIRELnqqiqtldmkidhiqqQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI----EELTDELLNL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 584 dtlksQMPQEapddsgDMKEAMNRMIDELNKQVSELSQLyreaQAELEDYRKRKSLEDAAEYIHkaEHERLMhvsnlsrA 663
Cdd:PHA02562 247 -----VMDIE------DPSAALNKLNTAAAKIKSKIEQF----QKVIKMYEKGGVCPTCTQQIS--EGPDRI-------T 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 664 KSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITE-------HLQVITTLRTTAKEMEEKISALTGHLANKEAEVA 736
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250
....*....|....*
gi 1720385250 737 KLEKQLAEEKAAVSD 751
Cdd:PHA02562 383 KLQDELDKIVKTKSE 397
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
171-224 |
2.40e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 171 LLDHGADVNSRDKNGRTALMLACETGSSN---TVDALIKKGADLSLVDSLGHNALHY 224
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHL 89
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
405-869 |
2.43e-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: 41.88 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 405 QLQDSLHDlqkRLESSEAEKKQLQDELQSQRtdtlclnnteISENGSDLSQKLKETQSKYEEAMKEVLS----VQKQMKL 480
Cdd:TIGR00618 212 CMPDTYHE---RKQVLEKELKHLREALQQTQ----------QSHAYLTQKREAQEEQLKKQQLLKQLRArieeLRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 481 GLLSQESADGYSHLreAPADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAEACEELRSSY---CSV 557
Cdd:TIGR00618 279 LEETQERINRARKA--APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsqEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 558 IENMNKEKAFLFEKYQQAQEEIMKLKdtlksqmpqeapddsgDMKEAMNRMIDELNKQVSELSQLYRE-AQAELEDYRKR 636
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIH----------------TLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 637 ksledaAEYIHKAeherlmhvsnlsRAKSEEALSEMKSQYSKVL--NELTQLKQLVDAHKENSVSITEHLQVITTLRTTA 714
Cdd:TIGR00618 421 ------DLQGQLA------------HAKKQQELQQRYAELCAAAitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 715 KEmEEKISALTGHLANKEAEVAK-LEKQLAEEKAAVSDAMVPKSSYEKLQAsLESEVNALATKLkESVRerekahsevAQ 793
Cdd:TIGR00618 483 LQ-ETRKKAVVLARLLELQEEPCpLCGSCIHPNPARQDIDNPGPLTRRMQR-GEQTYAQLETSE-EDVY---------HQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 794 VRSEVSQARREKDNIQTLlkakEQEVTALVQKFQRAQEELAGMRRCSET----SSKLEEDKDEKINEMTREVLKLKEALN 869
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
409-741 |
2.54e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 409 SLHDLQKRLESSEAEKKQLQDELQSQRTDTLCLNNtEISENGSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLGLLSQ 485
Cdd:COG5022 804 SLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEV-EFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVELAER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 486 ESadgyshlreapadedidtlkQDLQKAVEESARNKERVRELETKLAEKEQAEATKPPAEA--CEELRSSYCSVIENMNK 563
Cdd:COG5022 883 QL--------------------QELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLefKTELIARLKKLLNNIDL 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 564 EKAFLFEkyQQAQEEIMKLKDTlKSQMPQEAPDdSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDY----RKRKSL 639
Cdd:COG5022 943 EEGPSIE--YVKLPELNKLHEV-ESKLKETSEE-YEDLLKKSTILVREGNKANSELKNFKKELAELSKQYgalqESTKQL 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 640 EDaaEYIHKAEHERLMHVSNLSRA--KSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEM 717
Cdd:COG5022 1019 KE--LPVEVAELQSASKIISSESTelSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTI 1096
|
330 340
....*....|....*....|....*
gi 1720385250 718 EEK-ISALTGHLANKEAEVAKLEKQ 741
Cdd:COG5022 1097 NVKdLEVTNRNLVKPANVLQFIVAQ 1121
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
72-238 |
2.74e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.19 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 72 MVTHGVDVTAQDSSGHSALHVAAKNGHPECIRKLLQYKSPAENIDNSGKTALHYAAAQG--CLQAVQLLCEHKSPINLK- 148
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAKINNSv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 149 DLDGNIPLLvAVQNGHSEACHFLLDHGADVNSRDKNGRTAL--MLACETGSSNTVDALIKKGADLSLVDSLGHNALHY-- 224
Cdd:PHA02946 138 DEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIvc 216
|
170
....*....|....
gi 1720385250 225 SKLSENAGIQNLLL 238
Cdd:PHA02946 217 SKTVKNVDIINLLL 230
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
600-869 |
3.22e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 600 DMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYihkaeherlmhvSNLSrakseeaLSEMKSQYSKV 679
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL------------STLS-------LRQLESRLAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 680 LNELTQL-KQLVDAhkeNSVSITEHLQ---VITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVsDAmvp 755
Cdd:PRK11281 134 LDQLQNAqNDLAEY---NSQLVSLQTQperAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALL-NA--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 756 KSSYEKlqasLESEVNALATKLKESVREREKAH-----SEVAQVRSEVSQARREKDNiQTLLKAKEQEVTALVQKFQRAQ 830
Cdd:PRK11281 207 QNDLQR----KSLEGNTQLQDLLQKQRDYLTARiqrleHQLQLLQEAINSKRLTLSE-KTVQEAQSQDEAARIQANPLVA 281
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720385250 831 EELAGMRRCSETSSKleedKDEKINEMTREVLKLKEALN 869
Cdd:PRK11281 282 QELEINLQLSQRLLK----ATEKLNTLTQQNLRVKNWLD 316
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
610-804 |
3.23e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 610 DELNKQVSELSQLYREAQAELEDYRKRKS---------------LEDAA----EYIH-KAEHERLMHVSNLsRAKSEEAL 669
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAerareldllrfqleeLEAAAlqpgEEEElEEERRRLSNAEKL-REALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 670 SEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE----- 744
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALlrrla 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 745 EKAAVSDAMVPkSSYEKLQASLEsEVNALATKLKESVREREKAHSEVAQVRSEVSQARRE 804
Cdd:COG0497 313 RKYGVTVEELL-AYAEELRAELA-ELENSDERLEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
412-866 |
3.29e-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: 41.16 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 412 DLQKRLESSEAEKKQLQDELQSQRTDTLCLNNTEISENGS-----DLSQKLKETQSKYEEAMKEVLSVQKQMKLglLSQE 486
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnlkKKIQKNKSLESQISELKKQNNQLKDNIEK--KQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 487 SADGYSHLREApaDEDIDTLKQDLQKAVEESARNKERVRELETKLAEKE------QAEATKPPAEACEELRSSYCSVIEN 560
Cdd:TIGR04523 241 INEKTTEISNT--QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkqlnqlKSEISDLNNQKEQDWNKELKSELKN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 561 MNKEKAFLFEKYQQAQEEIMKLKDTLkSQMPQEAPDdsgdmKEAMNRMID-ELNKQVSELSQLYREAQAELEDYRKRKSL 639
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQI-SQLKKELTN-----SESENSEKQrELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 640 EDAAEyihkaehERLMHVSNLSRAKsEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQV----ITTLRTTAK 715
Cdd:TIGR04523 393 INDLE-------SKIQNQEKLNQQK-DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliIKNLDNTRE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 716 EMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVR 795
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 796 SEV---------SQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKE 866
Cdd:TIGR04523 545 DELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
584-801 |
3.38e-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: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 584 DTLKSQMPQEAPDDSGDMKEAMNRmIDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAAEYIHKAEHERLMHVSNLSR 662
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEALQAEiDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 663 AKSE--------EALSEMKSqYSKVLNELTQLKQLVDAHKEnsvSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAE 734
Cdd:COG3883 94 ALYRsggsvsylDVLLGSES-FSDFLDRLSALSKIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385250 735 VAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQA 801
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-179 |
3.46e-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: 3.46e-03
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-858 |
3.81e-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: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 397 TDNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTLClNNTEISENGSDLSQKLKETQSKYEEAMKEVlsvQK 476
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL---EK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 477 QMKLG----LLSQESADGYSHlREAPADEDIDTLKQDLQKAVEESARNKER------------------VRELETKLAEK 534
Cdd:pfam15921 350 QLVLAnselTEARTERDQFSQ-ESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhlRRELDDRNMEV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 535 EQAEAT-KPPAEACEELRSSYCSVIENMNKEkaflFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSgdMKEAMNRMIDELN 613
Cdd:pfam15921 429 QRLEALlKAMKSECQGQMERQMAAIQGKNES----LEKVSSLTAQLESTKEMLRKVVEELTAKKM--TLESSERTVSDLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 614 KQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSrakseEALSEMKSQYSKVLNELTQ----LKQL 689
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC-----EALKLQMAEKDKVIEILRQqienMTQL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 690 VDAHKENSVSI-TEHLQVITTLRTTAKEMEE----------KISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSS 758
Cdd:pfam15921 578 VGQHGRTAGAMqVEKAQLEKEINDRRLELQEfkilkdkkdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 759 YEKLQASLESEVNALATK---LKESVREREK---------------AHSEVAQVRSEVS-------QARREKDNIQTLLK 813
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDyevLKRNFRNKSEemetttnklkmqlksAQSELEQTRNTLKsmegsdgHAMKVAMGMQKQIT 737
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1720385250 814 AKEQEVTALVQKFQRAQEelaGMRRCSETSSKLEEDKDEKINEMT 858
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEE---AMTNANKEKHFLKEEKNKLSQELS 779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
558-797 |
4.27e-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: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 558 IENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEAMNRmIDELNKQVSELSQLYREAQAELED----- 632
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN-EEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGEraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 633 YRKRKSL---------EDAAEYIHKAEherlmhvsnlsrakseeALSEMKSQYSKVLNELTQLKQLVDAHKENSVsiteh 703
Cdd:COG3883 96 YRSGGSVsyldvllgsESFSDFLDRLS-----------------ALSKIADADADLLEELKADKAELEAKKAELE----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 704 lQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVRE 783
Cdd:COG3883 154 -AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|....
gi 1720385250 784 REKAHSEVAQVRSE 797
Cdd:COG3883 233 AAAAAAAAAAAASA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-638 |
4.31e-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: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 397 TDNDVIIRQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnTEISENGSDLSQKLKETQSKYEeamkevlsvQK 476
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAA---------NL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 477 QMKLGLLSQESADGYSHLREapADEDIDTLKQDLQKAVEESARNKERVRELETKLAEKEQAEATKppAEACEELRSSYCS 556
Cdd:TIGR02168 823 RERLESLERRIAATERRLED--LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL--EEALALLRSELEE 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 557 V---IENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKEAMN----------RMIDELN 613
Cdd:TIGR02168 899 LseeLRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKRLE 978
|
250 260
....*....|....*....|....*
gi 1720385250 614 KQVSELSQLYREAQAELEDYRKRKS 638
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
610-801 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 610 DELNKQVSELSQLYREAQAE---LEDYRKRK---SLEDAAEYIHKAE------HERLMHVSnLSRAKSEEALSEMKSQYS 677
Cdd:COG3096 937 EQLQADYLQAKEQQRRLKQQifaLSEVVQRRphfSYEDAVGLLGENSdlneklRARLEQAE-EARREAREQLRQAQAQYS 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 678 KVLNELTQLKQLVDAHKEnsvsitehlqvittlrtTAKEMEEKISALTGHLANKEAEVAKLEKQLAEEKAAVSDAMvpKS 757
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQ-----------------TLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSR--RS 1076
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720385250 758 SYEKLQASLESEVNALATKLKesvrereKAHSEVAQVRSEVSQA 801
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLR-------KAERDYKQEREQVVQA 1113
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
84-239 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 84 SSGHSALHVAAKNGHP---ECIRKLLQYKSPAENID---NS--------GKTALHYAAAQGCLQAVQLLCEHKSPINLKD 149
Cdd:cd22193 27 STGKTCLMKALLNLNPgtnDTIRILLDIAEKTDNLKrfiNAeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 150 LD--------------GNIPLLVAVQNGHSEACHFLLDHG---ADVNSRDKNGRTALMlACETGSSNTVD--ALIKKGAD 210
Cdd:cd22193 107 KGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH-ALVTVADNTKEntKFVTRMYD 185
|
170 180 190
....*....|....*....|....*....|
gi 1720385250 211 LSLVDSLG-HNALHYSKLSENAGIQNLLLS 239
Cdd:cd22193 186 MILIRGAKlCPTVELEEIRNNDGLTPLQLA 215
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
593-865 |
4.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 593 EAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYR-KRKSL-EDAAEYIHKAEHERLMhvsnlsRAKSEEALS 670
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELnAQVKELREEAQELREK------RDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 671 EMKSQYSKVLNELTQLKQLVDAHKENsvsitehLQVITTLRTTAKEMEEKISAL------TGHLANKEAEVAKLEKQLAE 744
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKE-------LAELNKAGGSIDKLRKEIERLewrqqtEVLSPEEEKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 745 EKAAVSDAMVPKSSYEKLQASLES---EVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTA 821
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKElrkEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720385250 822 LVQKFQRAQEELAGMR----RCSETSSKLEEDKDEKINEMTREVLKLK 865
Cdd:COG1340 228 LHEEIIELQKELRELRkelkKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
665-837 |
5.17e-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: 40.05 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 665 SEEALSEMKSQYSKVLNELTQLKQLVDAhKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAE 744
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 745 EKAAVSD------AMVPKSSYEKLQASLESEVNALATKLKESVRE-REKAHSEVAQVRSEVsqarrekdNIQTLLKAKEQ 817
Cdd:cd22656 161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDElKALIADDEAKLAAAL--------RLIADLTAADT 232
|
170 180
....*....|....*....|
gi 1720385250 818 EVTALVQKFQRAQEELAGMR 837
Cdd:cd22656 233 DLDNLLALIGPAIPALEKLQ 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
558-785 |
6.12e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 558 IENMNKEK-AFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYRE----------A 626
Cdd:PRK05771 33 IEDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEikeleeeiseL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 627 QAELEDYRKRK---------SLEDAAEY-----------IHKAEHERLMHVSNL-------------------SRAKSEE 667
Cdd:PRK05771 113 ENEIKELEQEIerlepwgnfDLDLSLLLgfkyvsvfvgtVPEDKLEELKLESDVenveyistdkgyvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 668 ALSEMKS-QYSKV-LNELTQLKQLVDAHKENSVSITEHLQ-VITTLRTTAKEMEEKISALTGHLANkEAEVAKLEKQLAE 744
Cdd:PRK05771 193 VEEELKKlGFERLeLEEEGTPSELIREIKEELEEIEKEREsLLEELKELAKKYLEELLALYEYLEI-ELERAEALSKFLK 271
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720385250 745 -EKAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVRERE 785
Cdd:PRK05771 272 tDKTFAIEGWVPEDRVKKLKELIDKATGGSAYVEFVEPDEEE 313
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-79 |
6.43e-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: 6.43e-03
10 20
....*....|....*....|....*...
gi 1720385250 52 EGKTAFHLAAAKGHVECLKVMVTHGVDV 79
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
419-868 |
6.62e-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: 40.48 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 419 SSEAEKKQLQDELQSQRTDTLCLNNT--EISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKL----GLLSQESADGYS 492
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAiqELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLlketCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 493 HLREapadeDIDTLKQDLQKAVEESARNKERVReLETKLAEKEQAEATKPPAEACEELRSSYCSVIENMNKEKAFLFeky 572
Cdd:pfam05483 176 YERE-----ETRQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL--- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 573 QQAQEEIMKLKDTlkSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHE 652
Cdd:pfam05483 247 IQITEKENKMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 653 RLMHVSNLSRAKSEEaLSEMKSQYSKVLNELT----QLKQLVDAHKENSVSITEHLQVITT-LRTTAKEMEEkisaLTGH 727
Cdd:pfam05483 325 TICQLTEEKEAQMEE-LNKAKAAHSFVVTEFEattcSLEELLRTEQQRLEKNEDQLKIITMeLQKKSSELEE----MTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 728 LANKEAEVAKLEKQLAEEKAAVSDAMVPKSSYEKLQA----------SLESEVNALATKLKESVREREKAHSEVAQVRSE 797
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720385250 798 VSQARREKDNIQT-----LLKAKE--QEVTALVQKFQRAQEELAGMRRCSETSSKLEEDKDEKINEMTREVLKLKEAL 868
Cdd:pfam05483 480 LEKEKLKNIELTAhcdklLLENKEltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
116-247 |
6.85e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 39.64 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 116 DNSGKTALHYAAAQgclQAVQLLCEHKSPINLKDL-DGNIPLLVAVQNGHSEACHFLLDHGADVNSRDKNGRTALMLACE 194
Cdd:PHA02791 27 DVHGHSALYYAIAD---NNVRLVCTLLNAGALKNLlENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720385250 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 ... |
404-857 |
7.15e-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: 40.16 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 404 RQLQDSLHDLQKRLESSEAEKKQLQDELQSQRTDTlclnnteisengSDLSQKLKETQSKYEEAMKEVLSVQKQMK--LG 481
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSEL------------ESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 482 LLSQESADGYSHLREAPADEDIDTLKQDLQKAVEESARNKER-VRELETKLAE-KEQAEATKPPAEACEELRSSYCSVIE 559
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDmKKKLEEDAGTLEALEEGKKRLQRELE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 560 NMN---KEKAFLFEKY-------QQAQEEIMKLKDTLKS-------------QMPQEAPDDSGDMKE------------- 603
Cdd:pfam01576 556 ALTqqlEEKAAAYDKLektknrlQQELDDLLVDLDHQRQlvsnlekkqkkfdQMLAEEKAISARYAEerdraeaeareke 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 604 ----AMNRMIDELNKQVSELSQLYREAQAELEDYRKRKslEDAAEYIHKAEHerlmhvsnlSRAKSEEALSEMKSQYSKV 679
Cdd:pfam01576 636 tralSLARALEEALEAKEELERTNKQLRAEMEDLVSSK--DDVGKNVHELER---------SKRALEQQVEEMKTQLEEL 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 680 LNELTQLKqlvDAHKENSVSITE-HLQVITTLRTTAKEMEEKISALTghlankeAEVAKLEKQLAEEKAAVSDAMVPKSS 758
Cdd:pfam01576 705 EDELQATE---DAKLRLEVNMQAlKAQFERDLQARDEQGEEKRRQLV-------KQVRELEAELEDERKQRAQAVAAKKK 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 759 YEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQKFQRAQEELAGMRR 838
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
490
....*....|....*....
gi 1720385250 839 CSETSsklEEDKDEKINEM 857
Cdd:pfam01576 855 ARRQA---QQERDELADEI 870
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-146 |
7.45e-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: 7.45e-03
10 20
....*....|....*....|....*...
gi 1720385250 119 GKTALHYAAAQGCLQAVQLLCEHKSPIN 146
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
568-848 |
7.73e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 568 LFEKYQQAQEEImklkDTLKSQmpqeapddsgdmKEAMNRMIDELNKQVSELSQ--LYREAQAELEdyrkrksledaaey 645
Cdd:COG0497 163 AYRAWRALKKEL----EELRAD------------EAERARELDLLRFQLEELEAaaLQPGEEEELE-------------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 646 ihkAEHERLMHVSNLsRAKSEEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALT 725
Cdd:COG0497 213 ---EERRRLSNAEKL-REALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 726 GHLANKEAEVAKLEKQLAEekaavsdamvpkssyeklqasleseVNALATKLKESVrerekahSEVAQVRSEVSQARREK 805
Cdd:COG0497 289 DSLEFDPERLEEVEERLAL-------------------------LRRLARKYGVTV-------EELLAYAEELRAELAEL 336
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720385250 806 DNIQTLLKAKEQEVTALVQKFQRAQEELAGMRRcsETSSKLEE 848
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEK 377
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
603-857 |
8.08e-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: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 603 EAMNRMIDELNKQVSELSQLYREAQAE--------LEDYRKRKSLEDAAEYIHKA---------EHERLMHVSNLSRAKS 665
Cdd:TIGR01612 568 EEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklkLELKEKIKNISDKNEYIKKAidlkkiienNNAYIDELAKISPYQV 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 666 EEALSEMKSQYSKVLNELTQLKQ---------LVDAHKENSVSITEHlqvittlRTTAKEMEEKISALTGHLANKEAEVA 736
Cdd:TIGR01612 648 PEHLKNKDKIYSTIKSELSKIYEddidalyneLSSIVKENAIDNTED-------KAKLDDLKSKIDKEYDKIQNMETATV 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 737 KLE-KQLAEEKAAVSDAMV--PKSSYEKLQASLESEVNALATKLKE---SVREREKAHSEVAQVRSEVSQARREKDNIQT 810
Cdd:TIGR01612 721 ELHlSNIENKKNELLDIIVeiKKHIHGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELNKYKSKISEIKNHYNDQIN 800
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720385250 811 LLKAKEQEVTalvQKFQRAQEELagmrrcsETSSKLEEDKDEKINEM 857
Cdd:TIGR01612 801 IDNIKDEDAK---QNYDKSKEYI-------KTISIKEDEIFKIINEM 837
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
586-860 |
8.11e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 40.10 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 586 LKSQMPQEAPDDSGDMKEAMNRMIDELNKQVSELSQLYREAQAELEDYRKRKSLEDAAEYIHKAEHERLMHVSNLSRAKS 665
Cdd:COG2770 255 LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 666 EEALSEMKSQYSKVLNELTQLKQLVDAHKENSVSITEHLQVITTLRTTAKEMEEKISALTGHLANKEAEVAKLEKQLAEE 745
Cdd:COG2770 335 LLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 746 KAAVSDAMVPKSSYEKLQASLESEVNALATKLKESVREREKAHSEVAQVRSEVSQARREKDNIQTLLKAKEQEVTALVQK 825
Cdd:COG2770 415 ALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEE 494
|
250 260 270
....*....|....*....|....*....|....*
gi 1720385250 826 FQRAQEELAGMRRCSETSSKLEEDKDEKINEMTRE 860
Cdd:COG2770 495 EEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVA 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
439-699 |
8.82e-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: 39.36 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 439 LCLNNTEISENGSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLLSQESADGyshlREAPADEDIDTLKQDLQKAVEESA 518
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 519 RNKERVRELETKLAEKEQAEAtkppaeacEELRSSYcsVIENMNKEKAFL-FEKYQQAQEEIMKLKDTLKSQmpQEAPDD 597
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELA--------ELLRALY--RLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPAR--REQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385250 598 SGDMKEAMNRMIDELNKQVSELSQLYREAQAEledyrkRKSLEDAaeyihKAEHERLMHVSNLSRAKSEEALSEMKSQYS 677
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEE------RAALEAL-----KAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260
....*....|....*....|..
gi 1720385250 678 KVLNELTQLKQLVDAHKENSVS 699
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
160-230 |
8.94e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.05 E-value: 8.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385250 160 VQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSSNTVDALIKKGADLSLVDSLGHNALHYSKLSEN 230
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| |
