|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-248 |
5.76e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.53 E-value: 5.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
....*...
gi 564335594 241 ISQDADLK 248
Cdd:COG0666 275 LLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-257 |
1.42e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.98 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250
....*....|....*..
gi 564335594 241 ISQDADLKTPTKAKQHD 257
Cdd:COG0666 242 GADLNAKDKDGLTALLL 258
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
5.86e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 155.50 E-value: 5.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 97 GHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564335594 177 DVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-240 |
2.25e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 136.62 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 113 ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564335594 193 CETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
2.02e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.98 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 91 HIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 564335594 171 LLDHGADVNSRDKNGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
2.20e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 95.18 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 90 LHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKsPINLKDlDGNIPLLVAIQNGHSEACH 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335594 170 FLLDHGADVNSRD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-239 |
3.14e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 103.59 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHIAA--K 95
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 96 NGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGS--LQAVQVLCEHKSPINLKDldgNIPLLvaiqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 174 HGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
8.57e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 93.26 E-value: 8.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHgADVNSRDkNGRTALMLACETGSANTVE 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335594 203 ALIKKGADLNLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
3.58e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPaeSVDNLGKTALHYAAAQGSLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335594 137 VLCEHKSPINLKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-215 |
4.09e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 94.71 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 88 SALHIAAKNGHP--EYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQV--LCEHKSPINLKDLDGNIPLLVAIQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFN 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335594 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVD 215
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-178 |
1.72e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 91.08 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 78 DVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESvdNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180
....*....|....*....|.
gi 564335594 158 VAIQNGHSEACHFLLDHGADV 178
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADV 681
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
27-218 |
1.59e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.62 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 27 VENGDAEKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGH--PEYI 102
Cdd:PHA03095 91 LYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 103 KKLLQYKSPAESVDNLGKTALHYAA--AQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACH--FLLDHGADV 178
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLLIAGISI 250
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564335594 179 NSRDKNGRTALMLAceTGSANTV--EALIKKGADLNLVDSLG 218
Cdd:PHA03095 251 NARNRYGQTPLHYA--AVFNNPRacRRLIALGADINAVSSDG 290
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-222 |
1.93e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.17 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 43 GASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQngHSEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTV 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDII 271
|
170 180
....*....|....*....|.
gi 564335594 202 EALIKKGADLNLVDSLGHNAL 222
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
9.27e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.89 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV---DVTAQDssGHSALHIAAKNGHPEYIKKLLQYKSPAES 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 115 VDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 564335594 194 ETGSANTVEALIKKGADLNLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-108 |
3.13e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHgVDVTAQDsSGHSALHIAAKNGHPEYI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*.
gi 564335594 103 KKLLQY 108
Cdd:pfam12796 78 KLLLEK 83
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
3.84e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 156 LLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKgADLNLVDSlGHNALYYSKLSENAGIQS 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 564335594 236 LLLSK 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-230 |
7.18e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.61 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLKVMVTHGVDVTAQDSSGHSALHI--AAKNGHPEYIKKL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 106 LQYKSPAESVDNLGKTALH-YAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF--LLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 182 DKNGRTALMLACETGS--ANTVEALIKKGADLNLVDSLGHNALYYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
2.32e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.62 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 79 VtaqdssghSALHIAAKNGhpEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLV 158
Cdd:PHA02874 94 T--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 159 AIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG----HNALYYsklseNAGIQ 234
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplHNAIIH-----NRSAI 238
|
250
....*....|....*....
gi 564335594 235 SLLLSKIS---QDADLKTP 250
Cdd:PHA02874 239 ELLINNASindQDIDGSTP 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
102-246 |
1.07e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 102 IKKLLQYKSPAESVDNLGKTALHY---AAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEAC-HFLLDHGAD 177
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGAD 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335594 178 VNSRDKNGRTALMlACETG---SANTVEALIKKGADLNLVDSLGHNAL--YYSKLSENAGIQSLLLSKISQDAD 246
Cdd:PHA03095 110 VNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-179 |
1.93e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.63 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 1 MKSLKAKFRKS-DTNEWNKNDDRLLQAVEN-----GDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK--GHVECLKVM 72
Cdd:PHA03100 48 IDVVKILLDNGaDINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 73 VTHGVDVTAQDSSGHSALHIAAKNGHPEY------------------IKKLLQYKSPAESVDNLGKTALHYAAAQGSLQA 134
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564335594 135 VQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
67-225 |
2.44e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.46 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 67 ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPIN 146
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335594 147 LKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACeTGSANTVEALIKKgADLNLVDSLGHNALYYS 225
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-225 |
5.90e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-KVMVTHGVDVTAQDSSGHSALHIAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 96 NGH-PEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQ-AVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLD 173
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564335594 174 HGADVNSRDKNGRTALMLA-CETGSANTVEALIKKGADLNLVDSLGHNALYYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-238 |
4.79e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.09 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKS 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 111 -----------------------------PAESVDNLGKTALHYAAAQGSL-QAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:PHA02876 236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 161 QNGH-SEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLL 238
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
5.00e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.52 E-value: 5.00e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564335594 55 TAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
636-896 |
1.09e-11 |
|
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: 69.33 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 636 MVDELNKQVSELsqlyREAQAELEDYRK-RKSLEDATEYIHRAEHErlmhlsnlsrtKAEESLSDMRSQYSKVLNELTQL 714
Cdd:TIGR02169 192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELLKEKE-----------ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 715 KQLVDAHKENSVSITEHLEVITtlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyEKLQASL 794
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-------EERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 795 ESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKL 874
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260
....*....|....*....|..
gi 564335594 875 EEDKDEKINEMTKEVLKLKEAL 896
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAI 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-917 |
1.55e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 637 VDELNKQVSELS------QLYREAQAELEDYRKR---KSLEDATEYIHRAEHERlmHLSNLSRTKAEESLSDMRSQYSKV 707
Cdd:COG1196 195 LGELERQLEPLErqaekaERYRELKEELKELEAElllLKLRELEAELEELEAEL--EELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 708 LNELTQLKQLVDAHKEN----SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvp 783
Cdd:COG1196 273 RLELEELELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 784 kasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAG 863
Cdd:COG1196 350 ----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564335594 864 LKrcsETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLE 917
Cdd:COG1196 426 LE---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
430-896 |
4.07e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKqlqdELQSQRTDTTCLNNTEISENGS--DLSQKLKDTQSKYEEAMKEVLSVQKQMK- 506
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKe 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 507 ----------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE-KEKAEATKPSSEVC 575
Cdd:PRK03918 285 lkelkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 576 EEMRnsycSVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKETMNRMVDELNKQVSELS--- 648
Cdd:PRK03918 365 EEAK----AKKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELKkak 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 649 ----------------QLYREAQAELEDYRKR-KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSD----MRSQYSKV 707
Cdd:PRK03918 436 gkcpvcgrelteehrkELLEEYTAELKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKY 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 708 -LNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-------------- 772
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlk 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 773 -------EKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQakREKENIQTLLKSKEQ 845
Cdd:PRK03918 596 elepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSR 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 846 EVTELVQKFQRAQEELAGLKRCSEtssKLEEDKdEKINEMTKEVLKLKEAL 896
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKAL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
430-944 |
7.09e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqmklgl 509
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKEL------------EEVLREINEISSELPELREELEKLEKEVKELEE------ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKrdkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENM 589
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK---KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 590 NKEKAFLFEKYQQAQEEIMKLkdtlkSQMPQEAPDDSGDMKETMNRmVDELNKQVsELSQLYREAQAELEDYRKRKS--- 666
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR-LEELEERH-ELYEEAKAKKEELERLKKRLTglt 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 667 ---LEDATEYIHRAEHERLMHLSNLSRTKAEesLSDMRSQYSKVLNELTQLK--------QLVDAHKENSvsITEHLEVI 735
Cdd:PRK03918 386 pekLEKELEELEKAKEEIEEEISKITARIGE--LKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL--LEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 736 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNALAA-KLKESVKEKEK 814
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA------------EQLKELEEKLKKYNLeELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 815 AHSEVAQVRSEVSQAKREKENIQTLLKSKEqevtELVQKFQRAQEELAGL-KRCSETSSKLEEDKDEKINEMTKEVLKLK 893
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYL 605
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 894 EALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEVVSVY 944
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-223 |
1.55e-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: 65.03 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 88 SALHIAAKNGHPEYIKKLLQYKSpaesVDN-----LGKTALHYAAAQGSLQAVQVLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPS----CDLfqrgaLGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 158 VAIQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALY 223
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
630-863 |
5.77e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.11 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 630 KETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihraehERLMHLSNLSRtkAEESLSDMRSQYSKVLN 709
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-------EAKLLLQQLSE--LESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 710 ELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMvpkasyEK 789
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335594 790 LQASLESEVNALAAK---LKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLkskeqevTELVQKFQRAQEELAG 863
Cdd:COG3206 314 ILASLEAELEALQAReasLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-------ESLLQRLEEARLAEAL 383
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
6.83e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 6.83e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564335594 121 TALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
1.82e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 1.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564335594 86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
2.04e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 2.04e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 155 PLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALI 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
637-932 |
2.16e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 637 VDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQ 716
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 717 LVDAHKEN-SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLE 795
Cdd:TIGR02168 779 EAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 796 SEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLK-RCSETSSKL 874
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRI 938
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 564335594 875 EEDKdEKINEmtKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEmlqqqvkqlqNQLAE 932
Cdd:TIGR02168 939 DNLQ-ERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRLE----------NKIKE 983
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-246 |
2.32e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 61.23 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 9 RKSDTNEWN-KNDDRLLQAVENG-DAEKVASLLgKKGASATKHDSEGKTAFHLAAA-KGHVECLKVMVTHGVDVTAQDSS 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA-AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNG- 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSanTVEALIKKGADLN----LVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRH 532
|
....*..
gi 564335594 240 KISQDAD 246
Cdd:PHA02876 533 DIRNEVN 539
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
432-881 |
2.83e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 432 QLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDttclnNTEISEngsdLSQKLKDTQSKYEEAMKEVLSVQ--KQMKLGL 509
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEK-----EERLEE----LKKKLKELEKRLEELEERHELYEeaKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKA----RVQELETKLVEKEKAEATKP------SSEVCEEMR 579
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGelkkEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 580 NSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgDMKETMNRMVDELNKQVSELSQL-YREAQAEL 658
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE----------SELIKLKELAEQLKELEEKLKKYnLEELEKKA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 659 EDYRKRKSLEDATEYIHRAEHERLMHLSNLSRTKA--EESLSDMRSQYSKVLNELTQ------------LKQLVDAHKE- 723
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAelEKKLDELEEELAELLKELEElgfesveeleerLKELEPFYNEy 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 724 NSVSITEHlEVITTLRTMAKEmEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLqaSLESEVNALAA 803
Cdd:PRK03918 605 LELKDAEK-ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRA 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 804 KLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEqEVTELVQKFQR--AQEELAGLKRCSETSSKL-EEDKDE 880
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKykALLKERALSKVGEIASEIfEELTEG 759
|
.
gi 564335594 881 K 881
Cdd:PRK03918 760 K 760
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-195 |
6.20e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 59.51 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 113 ESVDNLGKTALHYAAAQ-GSLQAVQVLCEHKSPINLKD-LDGNIPLLVAIqngHSE-ACHFLLDHGADVNSRDKNGRTAL 189
Cdd:PHA02878 228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304
|
....*.
gi 564335594 190 MLACET 195
Cdd:PHA02878 305 SSAVKQ 310
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
430-917 |
1.25e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnTEISEngsdLSQKLKDTQSKYEEAMKEVLSVQKQMKLG- 508
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELR--------LELEE----LELELEEAQAEEYELLAELARLEQDIARLe 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 509 -LLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 587
Cdd:COG1196 309 eRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 588 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSL 667
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 668 EDATEYIHRAEHERLMHLSNL-SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 746
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAaARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 747 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV 826
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 827 SQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYST 906
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490
....*....|.
gi 564335594 907 SSSKRQTQQLE 917
Cdd:COG1196 709 LAEAEEERLEE 719
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
517-894 |
1.39e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 517 GDSRLREVRVTDEDVDALKQ-DLQRALEESKRDKARVQELETKLVEkekaeaTKPSSEVCEEMRNSYCSVIENMNKekaf 595
Cdd:PRK02224 172 SDARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 596 LFEKYQQAQEEIMKLKdtlksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyih 675
Cdd:PRK02224 242 VLEEHEERREELETLE---------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 676 RAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsitehleviTTLRTMAKEMEEKTVTLQEH 755
Cdd:PRK02224 310 EAVEARREELED-RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 756 LASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKE---SVKEKEKAHSEVAQVRSE------- 825
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 826 -----------VSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE------ELAGLKRCSETSSKLEEDKDEKINEMTKE 888
Cdd:PRK02224 459 qpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRER 538
|
....*.
gi 564335594 889 VLKLKE 894
Cdd:PRK02224 539 AEELRE 544
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-222 |
2.39e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.19 E-value: 2.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564335594 171 LLDHG-ADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
521-865 |
2.65e-08 |
|
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: 58.16 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 521 LREVRVTDEDVDA----LKQDLQRaLEESKRDKARVQELETklvEKEKAEATKPSSEVcEEMRNSycsvIENMNKEKAFL 596
Cdd:TIGR02169 179 LEEVEENIERLDLiideKRQQLER-LRREREKAERYQALLK---EKREYEGYELLKEK-EALERQ----KEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 597 FEKYQQAQEEIMKLKDTLksqmpqeapddsgdmkETMNRMVDELNKQVSELSqlyreaqaELEDYRKRKSLEDATEYIHR 676
Cdd:TIGR02169 250 EEELEKLTEEISELEKRL----------------EEIEQLLEELNKKIKDLG--------EEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 677 AehERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHL----EVITTLRTMAKEMEEKTVTL 752
Cdd:TIGR02169 306 L--ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 753 QEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 832
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350
....*....|....*....|....*....|...
gi 564335594 833 KENIQTLLKSKEQEVTELVQKFQRAQEELAGLK 865
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-238 |
4.91e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.54 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 60 AAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLC 139
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 140 EHKSPINlkDL---DGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDS 216
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180
....*....|....*....|..
gi 564335594 217 LGHNALYYSKLSENAGIQSLLL 238
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLL 188
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
19-207 |
8.37e-08 |
|
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: 56.17 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTH-----GVDVTAQDSSGHSALHIA 93
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 94 AKNGHPEYIKKLLQY----KSP-------AESVDNL---GKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL-LV 158
Cdd:cd22192 97 VVNQNLNLVRELIARgadvVSPratgtffRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564335594 159 AIQNGHSEACH---FLLDHGADVNS------RDKNGRTALMLACETGSANTVEALIKK 207
Cdd:cd22192 177 VLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
448-896 |
1.42e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 448 EAEKKQLQDELQSQRTDTTCLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVT 527
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 528 DEDVDALKQDLQ--RALEESKR---DKARVQELETKLVEKEKAEATKPSSEvceEMRNSYCSVIENMNKEKAflfEKYQQ 602
Cdd:PTZ00121 1417 KKKADEAKKKAEekKKADEAKKkaeEAKKADEAKKKAEEAKKAEEAKKKAE---EAKKADEAKKKAEEAKKA---DEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 603 AQEEIMKLKDTLKSQMPQEAPDDSGDMKETmNRMVDELNK-----QVSELSQlyREAQAELEDYRKRKSLEDATEYIHRA 677
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE-AKKADEAKKaeeakKADEAKK--AEEKKKADELKKAEELKKAEEKKKAE 1567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 678 EHERLMHLSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLA 757
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEE----AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKE 1642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 758 SKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENiq 837
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-- 1720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 564335594 838 tlLKSKEQEVTELVQKFQRAQEELaglKRCSETSSKLEEDKDeKINEMTKEVLKLKEAL 896
Cdd:PTZ00121 1721 --LKKAEEENKIKAEEAKKEAEED---KKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEI 1773
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-256 |
1.81e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.84 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHP---EYIKKLLQY 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 109 KSPAESVDN-LGKTALH----YAAAQGSLQAVQVLCEHKSPINLKD-------LDGNIPLLVAIQNGHSEACHFLLDHgA 176
Cdd:PHA02798 171 GVDINTHNNkEKYDTLHcyfkYNIDRIDADILKLFVDNGFIINKENkshkkkfMEYLNSLLYDNKRFKKNILDFIFSY-I 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 177 DVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGI-QSLLLSKISQDADLKTPTKAKQ 255
Cdd:PHA02798 250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIfNSILNKKPNKNTISYTYYKLRK 329
|
.
gi 564335594 256 H 256
Cdd:PHA02798 330 H 330
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-206 |
2.62e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 127 AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIK 206
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
628-895 |
2.86e-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: 54.68 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 628 DMKETMNRMVD---ELNKQV------SELSQLYREAQAELEDYRKRKSLEDATEYihraeherlmhlsnlsrtkaeesls 698
Cdd:TIGR02168 183 RTRENLDRLEDilnELERQLkslerqAEKAERYKELKAELRELELALLVLRLEEL------------------------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 699 dmRSQYSKVLNELTQLKQLVDAHKENsvsITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 778
Cdd:TIGR02168 238 --REELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 779 DAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQ 858
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564335594 859 EELAG----LKRCSETSSKLEEDKDEKINEMTKEVLKLKEA 895
Cdd:TIGR02168 393 LQIASlnneIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-93 |
3.15e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 3.15e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 564335594 50 DSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIA 93
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
131-240 |
3.20e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.07 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 131 SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQN----GHS-EACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEAL- 204
Cdd:PHA02798 50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILl 129
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564335594 205 --IKKGADLNLVDSLGHNAL-YYSKLSENAGIQ--SLLLSK 240
Cdd:PHA02798 130 fmIENGADTTLLDKDGFTMLqVYLQSNHHIDIEiiKLLLEK 170
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
4.13e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 4.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335594 189 LMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKISQDADLKTPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
100-229 |
4.22e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 100 EYIKKLLQYKSPAESVD-NLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564335594 179 NSRDKNGRTALMLAC-ETGSANTVEALIKKGADLNLVDS-LGHNALYYSKLSE 229
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-83 |
4.97e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.57 E-value: 4.97e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQD 83
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
432-893 |
5.92e-07 |
|
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: 53.58 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 432 QLQDTLHDLQKRLETSEAEKKQLQ-------------DELQSQRTDttclNNTEISENGSDLSQKLKDTQSKYEEAMKEV 498
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitiDHLRRELDD----RNMEVQRLEALLKAMKSECQGQMERQMAAI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 499 LSvqKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELEtKLVEKEKAEATKPSSEVCEEM 578
Cdd:pfam15921 454 QG--KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 579 RNsycsvIENMNKEKAFLfeKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAEL 658
Cdd:pfam15921 531 QE-----LQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 659 EDYRKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVIT-T 737
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 738 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 817
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 818 EVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLK 893
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
430-897 |
7.07e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnnteisengsDLSQKLKDTQSKYEEAMKEVLSVQKQMKLgl 509
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE------------ELEREIEEERKRRDKLTEEYAELKEELED-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEkaeatkpssevcEEMRNSYCSVIENM 589
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL------------ADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 590 NK---EKAFLFEKYQQAQEEIMKLKDTLKSqmpqeAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 666
Cdd:TIGR02169 437 NEleeEKEDKALEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 667 LEDATEYIHRAEHERLMHLSNLSR--TKAEESLSDMRSQYSKV-------------------------LNELTQLKQLVD 719
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNVVVeddavakeaiellkrrkagratflpLNKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 720 AHKENSVsITEHLEVIT---TLRTMAKEMEEKTVTLQEHLASKE--GEV--AKLEKQLAEEKAAMSDAMVPKASYEKLQA 792
Cdd:TIGR02169 592 ILSEDGV-IGFAVDLVEfdpKYEPAFKYVFGDTLVVEDIEAARRlmGKYrmVTLEGELFEKSGAMTGGSRAPRGGILFSR 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 793 SLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETS 871
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLE 750
|
490 500 510
....*....|....*....|....*....|..
gi 564335594 872 SKLEEDKDE------KINEMTKEVLKLKEALN 897
Cdd:TIGR02169 751 QEIENVKSElkeleaRIEELEEDLHKLEEALN 782
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
7.53e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 7.53e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 72 MVTHG-VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
35-161 |
7.95e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKngHPEYIKKLLQYKSPAES 114
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIND 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564335594 115 VDNLGKTALHYAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQ 161
Cdd:PHA02874 250 QDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
51-227 |
8.18e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 53.16 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVdnlGKTALHyAAA 128
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 129 QGSLQAVQVLCEHKSPINLKDLD--------------GNIPLLVAIQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564335594 184 ---NGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKL 227
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
8.25e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564335594 68 CLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
485-915 |
8.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 485 KDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQdlqRALEESKRDKARVQELETKLVEKEK 564
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 565 AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQAqEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQV 644
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 645 SElSQLYREAQAELEDYRKRKSLEDATEYIHRAEHERL----MHLSNLSRTKAEESL--SDMRSQYSKVLNELTQLKQLV 718
Cdd:PTZ00121 1441 EE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeeAKKADEAKKKAEEAKkkADEAKKAAEAKKKADEAKKAE 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 719 DAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSD------AMVPKASYEKLQA 792
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeaKKAEEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 793 SLESEVNALAAKLKESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTElVQKFQRAQEElaGLKRCSETSS 872
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEE--NKIKAAEEAK 1668
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564335594 873 KLEEDKD--EKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQ 915
Cdd:PTZ00121 1669 KAEEDKKkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
52-256 |
8.92e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESV-DNLGKTALHYAAAQG 130
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 131 SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGAD 210
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564335594 211 LNLVDSLGHNALYYSKLSEN-AGIQSLLLSKiSQDADLKTPTKAKQH 256
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIENNkIDIVRLFIKR-GADCNIMFMIEGEEC 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
430-897 |
1.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnntEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQM--KL 507
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELE-----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 508 GLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVI 586
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 587 ENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQA 656
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLeelaeaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 657 ELEDY-------RKRKSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNE---LTQLKQLVDAHKENSV 726
Cdd:COG1196 539 ALEAAlaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdLVASDLREADARYYVL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 727 SITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNALAAKLK 806
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR------------ELLAALLEAEAELEELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 807 ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMT 886
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
490
....*....|.
gi 564335594 887 KEVLKLKEALN 897
Cdd:COG1196 767 RELERLEREIE 777
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
91-185 |
1.57e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 91 HIAAkNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 564335594 171 LLDHGADVNSRDKNG 185
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
430-897 |
2.42e-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: 51.60 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRL-------ETSEAEKKQLQDELQSQRTDTTCLnNTEISENGS---DLSQKLKDTQSKYEEAMKEVL 499
Cdd:TIGR02168 276 VSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEEL-EAQLEELESkldELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 500 SVQKQMK--------LGLLSHE--------SADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE 563
Cdd:TIGR02168 355 SLEAELEeleaeleeLESRLEEleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 564 KAEATKPSSEVcEEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-QMPQEAPDDSGDMKETMNRMVDELNK 642
Cdd:TIGR02168 435 LKELQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlQARLDSLERLQENLEGFSEGVKALLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 643 QVSELSQL-------------YREA-----QAELEDY--RKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRS 702
Cdd:TIGR02168 514 NQSGLSGIlgvlselisvdegYEAAieaalGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLP-LDSIKGTEIQGNDRE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 703 QYSKVLNELTQLKQLVDAHKENSVSIT---EHLEVITTLRT---MAKEMEEKT--VTLQEHLASKEG------------- 761
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNaleLAKKLRPGYriVTLDGDLVRPGGvitggsaktnssi 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 762 -----EVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENI 836
Cdd:TIGR02168 673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 837 QTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKLEEDkdekINEMTKEVLKLKEALN 897
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE---LAEAEAEIEELEAQ----IEQLKEELKALREALD 806
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
439-861 |
4.24e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 439 DLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGllSHESAD 516
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAAELESELEEAREAVEDR--REEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 517 GDSRLREVRV----TDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYC--------- 583
Cdd:PRK02224 389 LEEEIEELRErfgdAPVDLGNAEDFLEELREERDELREREAELEATL--RTARERVEEAEALLEAGKCPECgqpvegsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 584 -SVIENMNKEKAFLFEKYQQAQEEIMKLKDTLksqmpqeapDDSGDMKETMNRmVDELNKQVSELSQLYREAQAELEDYR 662
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERL---------ERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 663 KR--KSLEDATEYIHRAEHERlmhlsnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH---KENSVSITEHLEVITT 737
Cdd:PRK02224 537 ERaeELRERAAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 738 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEekAAMSDAMVPKASYEKLQASLESEVNALAAklkesvkEKEKAHS 817
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELRE-------ERDDLQA 681
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564335594 818 EVAQVRSEVSQAKREKENIQTL------LKSKEQEVTELVQKFQRAQEEL 861
Cdd:PRK02224 682 EIGAVENELEELEELRERREALenrveaLEALYDEAEELESMYGDLRAEL 731
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
4.67e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 4.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 564335594 145 INLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
431-858 |
5.93e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDttcLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKlgll 510
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL---LQLLPLYQELEALEAELAELPERLEELEERLEELRELEE---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 511 shesaDGDSRLREVRVTDEDVDALKQDL-QRALEESKRDKARVQELETKLVEKEKAEATkpSSEVCEEMRNSYCSVIENM 589
Cdd:COG4717 164 -----ELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEE--AQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 590 NKEKafLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELnkqVSELSQLYREAQAELEDYRKRKSLED 669
Cdd:COG4717 237 EAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 670 ATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLvdahkENSVSITEHLEVITTLRTMAK----EM 745
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----EEELQLEELEQEIAALLAEAGvedeEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 746 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVpkasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSE 825
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430
....*....|....*....|....*....|....*
gi 564335594 826 VSQAKREKE--NIQTLLKSKEQEVTELVQKFQRAQ 858
Cdd:COG4717 462 LEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-213 |
6.02e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.73 E-value: 6.02e-06
10 20 30
....*....|....*....|....*....|
gi 564335594 184 NGRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
162-247 |
7.87e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 162 NGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKI 241
Cdd:PTZ00322 92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
....*.
gi 564335594 242 SQDADL 247
Cdd:PTZ00322 172 QCHFEL 177
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
8.50e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 8.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 105 LLQYKSPA-ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVA 159
Cdd:pfam13857 1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
430-769 |
9.00e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnTEISENGSDLSQKlKDTQSKYEEAMKEVlsvqkqmklgl 509
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVK--------SELKELEARIEEL-EEDLHKLEEALNDL----------- 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 lshESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQeLETKLVEKEKAEATKPSSEvCEEMRNSYCSVIENM 589
Cdd:TIGR02169 785 ---EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENL 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 590 NKEKAFLFEKYQQAQEEIMKLKDTLKSqmpqeapddsgdmketMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLED 669
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 670 ATEyihRAEHERLMHLSNLSRTKAEESLSDMrsQYSKVLNELTQLKQLVDAHKE-NSVSITEHLEVITTLrtmaKEMEEK 748
Cdd:TIGR02169 924 AKL---EALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRL----DELKEK 994
|
330 340
....*....|....*....|.
gi 564335594 749 TVTLQEHLASKEGEVAKLEKQ 769
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
431-897 |
9.42e-06 |
|
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: 49.79 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDElqsqrtdttclnNTEISENGSDLSQKLKDtqskyEEAMKEVLSVQKqmklgll 510
Cdd:pfam01576 71 QELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 511 shesADGDSRLREVrvtDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE-----------KAEATKPSSEV----C 575
Cdd:pfam01576 127 ----VTTEAKIKKL---EEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEekakslsklknKHEAMISDLEErlkkE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 576 EEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-----QMPQEAPDDSGDMKETMNRMVDELNKQVSELSQ- 649
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALARLEEETAQKNNALKKIRELEAQISELQEd 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 650 --LYREAQAELEDYRK---------RKSLED-----ATEYIHRAEHERlmHLSNLSRTKAEES------LSDMRSQYSKV 707
Cdd:pfam01576 280 leSERAARNKAEKQRRdlgeelealKTELEDtldttAAQQELRSKREQ--EVTELKKALEEETrsheaqLQEMRQKHTQA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 708 LNELT-QLKQLvdahKENSVSITEHLEvitTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKAS 786
Cdd:pfam01576 358 LEELTeQLEQA----KRNKANLEKAKQ---ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 787 YEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAK-------REKENIQTLLKSKEQEVTELVQKFQRAQE 859
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 564335594 860 ELAGLKR--------CSETSSKLEEDKD--EKINEMTKEVLKLKEALN 897
Cdd:pfam01576 511 AKRNVERqlstlqaqLSDMKKKLEEDAGtlEALEEGKKRLQRELEALT 558
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
684-866 |
9.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 684 HLSNLSRtkAEESLSDMRSQyskvLNELTQLKQLVDAHKENSVSITEHLEVITTLRtmAKEMEEKTVTLQEHLASKEGEV 763
Cdd:COG4913 233 HFDDLER--AHEALEDAREQ----IELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 764 AKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV----------------- 826
Cdd:COG4913 305 ARLEAELERLEARLDAL---REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaee 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335594 827 -----SQAKREKENIQTLLKSKEQEVTELVQKFQRAQE-------ELAGLKR 866
Cdd:COG4913 382 faalrAEAAALLEALEEELEALEEALAEAEAALRDLRRelreleaEIASLER 433
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-141 |
1.34e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLKVMVTHGVDVTAQDSSG 86
Cdd:PTZ00322 43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564335594 87 HSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
52-81 |
1.64e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.57 E-value: 1.64e-05
10 20 30
....*....|....*....|....*....|
gi 564335594 52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
431-894 |
2.37e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL- 507
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 508 ----GLLSHESADGDSRLREVR----VTDEDVDALKQDLQRALEESKRDKARVQELETKL--VEKEKAEATKPSSEVCEE 577
Cdd:TIGR04523 116 keqkNKLEVELNKLEKQKKENKknidKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnlLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 578 MRNSY--CSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKsQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 655
Cdd:TIGR04523 196 LLKLEllLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 656 AELEDYRKRKSLEDATEYIHraeherlMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVI 735
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLK-------SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS---QNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 736 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKA 815
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335594 816 HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKE 894
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
2.81e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.89 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|...
gi 564335594 184 NGRTALMLACE-TGSANTVEALIKKGADLNLVD 215
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-183 |
3.07e-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: 3.07e-05
10 20 30
....*....|....*....|....*....|....
gi 564335594 151 DGNIPLLVAI-QNGHSEACHFLLDHGADVNSRDK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
598-896 |
4.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 598 EKYQQAQEEIMKLKDTLKSQMPQ-----EAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAT 671
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 672 EYIHRAEHERLMHLSNLSRTKA-----EESLSDMRSQYS---KVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAK 743
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEkirelEERIEELKKEIEeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 744 EMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVR 823
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564335594 824 SEVSQAKREKENIQTLLKSKEQEVTELvqkfQRAQEELAGLKRCSETSSKL--EEDKDEKINEMTKEVLKLKEAL 896
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGREltEEHRKELLEEYTAELKRIEKEL 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
620-832 |
4.98e-05 |
|
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: 46.68 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 620 QEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEE---- 695
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIRALEQELAALEAELAELEKEIaelr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 696 -SLSDMRSQYSKVLNELTQLKQ----LVDAHKENSVSITEHLEVITTL----RTMAKEMEEKTVTLQEHLASKEGEVAKL 766
Cdd:COG4942 97 aELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 767 EKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 832
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
489-897 |
5.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 489 SKYEEAMKEVLSVQKQmKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAT 568
Cdd:COG4717 49 ERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 569 KPSSEVCEEMRNSYCSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSQmpqeapddSGDMKETMNRMVDELNKQVSELS 648
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAEL--------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 649 QLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYsKVLNELTQLKQLVDAHKENSVSI 728
Cdd:COG4717 199 EELEELQQRLAELEEE--LEEAQEELEELEEELEQLENELEAAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 729 TEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK-QLAEEKAAMSDAMVPkasyeklqaslESEVNALAAKLKE 807
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP-----------PDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 808 SVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTK 887
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410
....*....|.
gi 564335594 888 EVLK-LKEALN 897
Cdd:COG4717 425 LDEEeLEEELE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
431-940 |
6.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLetSEAEKKQLQDELQSQRTDTTCLNNTEisengSDLSQKLKDTQSKYEEAMKEVLSVQKQM----- 505
Cdd:TIGR02168 216 KELKAELRELELAL--LVLRLEELREELEELQEELKEAEEEL-----EELTAELQELEEKLEELRLEVSELEEEIeelqk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 506 KLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYCSV 585
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL--EEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 586 IENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEApddsgDMKETMNRMVDELNKQVSELSQLYREAQ-AELEDYRKR 664
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 665 KSLEDATEYIHRAEHERLMH-LSNL--SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH----------KENSVSITEH 731
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEaLEELreELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvkalLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 732 LEVITTLRTMAKEME-EKTVTLQEHLAS----------------KEGEVAKL-----------------EKQLAEEKAAM 777
Cdd:TIGR02168 522 LGVLSELISVDEGYEaAIEAALGGRLQAvvvenlnaakkaiaflKQNELGRVtflpldsikgteiqgndREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 778 SDAMVPKASYEKLQASLES------------EVNALAAKLKE-----------------SVKEKEKAHSEVAQVRSEVSQ 828
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYllggvlvvddldNALELAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 829 AKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKrcsetssKLEEDKDEKINEMTKEVLKL-KEALNSLSQLSYSTS 907
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSK 754
|
570 580 590
....*....|....*....|....*....|...
gi 564335594 908 SSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEV 940
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
430-723 |
8.08e-05 |
|
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: 46.87 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtDTTCLNNTEISENGS---DLSQKLKDTQSK---YEEAMKEVLSVQK 503
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 504 QMKLGLLSHESADG---DSRLREVRVTDEdVDALKQDLQRAlEESKRDKARVQELETKLV-EKEKAEATKPSSEVCEEMR 579
Cdd:COG3096 428 LCGLPDLTPENAEDylaAFRAKEQQATEE-VLELEQKLSVA-DAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 580 nSYCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 655
Cdd:COG3096 506 -SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 656 AELEDYR-KRKSLEdATEYIHRAEHERLMHLSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKE 723
Cdd:COG3096 585 QQLEQLRaRIKELA-ARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQ 654
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
431-892 |
8.20e-05 |
|
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: 46.71 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDELQsqrTDTTCLNNTE-----ISENGSDLSQKLKDTQSKYEEamKEVLSVQKQM 505
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQ---AETELCAEAEemrarLAARKQELEEILHELESRLEE--EEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 506 KLGLLSHESADGDSRLrevrvtdEDVDALKQDLQraLEESKRDkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSV 585
Cdd:pfam01576 97 EKKKMQQHIQDLEEQL-------DEEEAARQKLQ--LEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 586 IENMNKEKAFLFEKYQQAQEEIM-----KLKDTLKSQMPQEApddsgdMKETMNRMVDELNKQVSELSQLYREAQAELEd 660
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMIsdleeRLKKEEKGRQELEK------AKRKLEGESTDLQEQIAELQAQIAELRAQLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 661 yRKRKSLEDAteyIHRAEHErlmhlsNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEvitTLRT 740
Cdd:pfam01576 240 -KKEEELQAA---LARLEEE------TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE---ALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 741 MAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEK----AAMSD------------------AMVPKASYEKLQASLESEV 798
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQEVTELKKALEEETrsheAQLQEmrqkhtqaleelteqleqAKRNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 799 NALAAKLK-------ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL-KRCSET 870
Cdd:pfam01576 387 AELQAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLsKDVSSL 466
|
490 500
....*....|....*....|..
gi 564335594 871 SSKLeEDKDEKINEMTKEVLKL 892
Cdd:pfam01576 467 ESQL-QDTQELLQEETRQKLNL 487
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-245 |
1.18e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.64 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLG--KTALHYAAAQGSLQA 134
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVaiKDAFNNRNVEIFKII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 135 VQVLCEHKSPINLKDLDgNIPLLVAIQnghSEACHFLLDHGADVNSRDKN-GRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:PHA02878 121 LTNRYKNIQTIDLVYID-KKSKDDIIE---AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
|
170 180 190
....*....|....*....|....*....|...
gi 564335594 214 VDSLGHNALYYS-KLSENAGIQSLLLSKISQDA 245
Cdd:PHA02878 197 PDKTNNSPLHHAvKHYNKPIVHILLENGASTDA 229
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
624-842 |
1.21e-04 |
|
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: 45.82 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 624 DDSGDMKETMNRMVDELNKQVSELSQLYreaQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNLSRtKAEESLSDM--R 701
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQL---PAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRR-ALEAKRKDPfkS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 702 SQYSKVLNELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKtvtlqehlaskegevakLEKQLAEEKAAMSDAm 781
Cdd:pfam13166 355 IELDSVDAKIESINDLVASINE---LIAKHNEITDNFEEEKNKAKKK-----------------LRLHLVEEFKSEIDE- 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 782 vpkasYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKS 842
Cdd:pfam13166 414 -----YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
536-895 |
1.24e-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: 46.26 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 536 QDLQRALEESKRDKAR--------VQELETKLVEKEK-----AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQ 602
Cdd:pfam15921 88 KDLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMerdamADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLED 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 603 AQEEIMKLKDTLKSQ--MPQEAPDDSGDMKETMNRMVDELNKQV--------SELSQLYREAQAELEDYRKRK-SLEDAT 671
Cdd:pfam15921 168 SNTQIEQLRKMMLSHegVLQEIRSILVDFEEASGKKIYEHDSMStmhfrslgSAISKILRELDTEISYLKGRIfPVEDQL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 672 EYI--------------HRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQlvDAHKENSVSITEHLEVITT 737
Cdd:pfam15921 248 EALksesqnkielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLEST 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 738 LRTMAKEMEEKTVTLqehlaskEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKL----KESVKEKE 813
Cdd:pfam15921 326 VSQLRSELREAKRMY-------EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 814 KAHS----------EVAQVRSEVSQAKREKENIQTLLKSKEQEVT-ELVQKFQRAQEELAGLKRCSETSSKLEEDKD--- 879
Cdd:pfam15921 399 QNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlr 478
|
410
....*....|....*.
gi 564335594 880 EKINEMTKEVLKLKEA 895
Cdd:pfam15921 479 KVVEELTAKKMTLESS 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
433-853 |
1.28e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 433 LQDTLHDLQKRLETSEAEKKQLQDELQSQRTD----TTCLNNTEI--SENGSDLS--QKLKDTQSKYEEAMKEVLSVQKQ 504
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSEleemTKFKNNKEVelEELKKILAedEKLLDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 505 MKLGLLSHESADGDSRLREVRVTDEDVDALKQ--DLQRALEESKRDKARVQELETKLVEKEKaEATKPSSEVCEEMRNSY 582
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENK-ELTQEASDMTLELKKHQ 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 583 CSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSqMPQEAPDDSGDMKETMNRmvDELNKQVSELSQLYREAQAELEDYR 662
Cdd:pfam05483 520 EDIINCKKQEERML-KQIENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 663 ---KRKSLEDATEYIHRAEHERlmhlSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVitT 737
Cdd:pfam05483 596 cnnLKKQIENKNKNIEELHQEN----KALKKKGSAENkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI--S 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 738 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 817
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH---KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 564335594 818 EVAQVRSEVSQAKR----EKENIQTLLKSKEQEVTELVQK 853
Cdd:pfam05483 747 ELSNIKAELLSLKKqleiEKEEKEKLKMEAKENTAILKDK 786
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
523-876 |
1.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 523 EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAtkpssevceEMRNSYCSVIENMNKEKAFL--FEKY 600
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES---------DLEQDYQAASDHLNLVQTALrqQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 601 QQAQEEIMKLKDTLKSQM-----PQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDateyih 675
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE------ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 676 raEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsiTEHLEVITTLRTMAKEME--------- 746
Cdd:PRK04863 425 --RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAYQLVRKIAGEVSrseawdvar 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 747 ------EKTVTLQEHLASKEGEVAKLEKQLAEEKAA--MSDAMVPKASyekLQASLESEVNALAAKLKESVKEKEKAHSE 818
Cdd:PRK04863 500 ellrrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAerLLAEFCKRLG---KNLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335594 819 VAQVRSEVSQAKREkeniqtlLKSKEQEVTELVQKFQRAQEELAGLKRCS----ETSSKLEE 876
Cdd:PRK04863 577 ARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSgeefEDSQDVTE 631
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
634-854 |
1.35e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 46.00 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 634 NRMVD-ELNKQVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHERLMHLSNLS----RTKAEEslsDMRSQYSKVL 708
Cdd:pfam09726 414 SRQTEqELRSQISSLTSLERSLKSELG--QLRQENDLLQTKLHNAVSAKQKDKQTVQqlekRLKAEQ---EARASAEKQL 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 709 NELTQLKQLVDAHKENSVS--ITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKaamsdamvpkaS 786
Cdd:pfam09726 489 AEEKKRKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELR-----------K 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335594 787 YEKLQASLESEVNALAAkLKESVKEKEKAHSEVAQVR----SEVSQAKREKENIQTLLKSKEQEVTELVQKF 854
Cdd:pfam09726 558 YKESEKDTEVLMSALSA-MQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
1.44e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMV 73
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
47-162 |
1.66e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 43.49 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 47 TKHDSEGKTAFHLAAAKGHVECLKVMV------THGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYK-------SPAE 113
Cdd:PHA02741 15 AEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLielgadiNAQE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564335594 114 SVDnlGKTALHYAAAQGSLQAVQVLCEHKSpINLK--DLDGNIPLLVAIQN 162
Cdd:PHA02741 95 MLE--GDTALHLAAHRRDHDLAEWLCCQPG-IDLHfcNADNKSPFELAIDN 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
746-866 |
1.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 746 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAK-----LKESVKEKEKAHSEVA 820
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564335594 821 QVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR 866
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-179 |
1.76e-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: 39.49 E-value: 1.76e-04
10 20
....*....|....*....|....*....
gi 564335594 151 DGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
693-864 |
1.94e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 693 AEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK 768
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 769 QLAEEKAAMSDAMV------------------------------------PKASYEKLQASLEsEVNALAAKLKESVKEK 812
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspedfldavrrlqylkylapaRREQAEELRADLA-ELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335594 813 EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL 864
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
2.02e-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: 39.58 E-value: 2.02e-04
10 20 30
....*....|....*....|....*....|...
gi 564335594 52 EGKTAFHLAAAK-GHVECLKVMVTHGVDVTAQD 83
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-212 |
3.20e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 3.20e-04
10 20
....*....|....*....|....*....
gi 564335594 184 NGRTALMLACETGSANTVEALIKKGADLN 212
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
102-247 |
3.31e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.88 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 102 IKKLLQYKSpAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLkdLDGNIPLLVAIQNGHSEACHFLLDHGADVNSR 181
Cdd:PHA02791 14 LKSFLSSKD-AFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335594 182 DKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG-HNALYYSKLSENAGIQSLLLSKISQDADL 247
Cdd:PHA02791 91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
129-232 |
4.34e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 44.28 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 129 QGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKG 208
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100
....*....|....*....|....*....
gi 564335594 209 A-----DLNLVDSLGHNALYYSKLSENAG 232
Cdd:PHA02876 235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
432-916 |
5.37e-04 |
|
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: 44.19 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 432 QLQDTLHDlqkRLETSEAEKKQLQDELQSQRtdttclnnteISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLS 511
Cdd:TIGR00618 212 CMPDTYHE---RKQVLEKELKHLREALQQTQ----------QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 512 HESADGDSRLR----EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 587
Cdd:TIGR00618 279 LEETQERINRArkaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 588 NMNKEKAFLFEKYQQAQEEIMKLKdtlksqmpqeapddsgDMKETMNRMVDELNKQVSELSQLYRE-AQAELEDYRKrks 666
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIH----------------TLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAF--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 667 ledateyihRAEHERLMHLsnlsRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 746
Cdd:TIGR00618 420 ---------RDLQGQLAHA----KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 747 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESevnalAAKLKESVKEKEkahsevAQVRSEV 826
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQLETSEEDVY------HQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 827 SQAKREKENIQTLlkskEQEVTELVQKFQRAQEELAGLKRCSET----SSKLEEDKDEKINEMTKEVLKLKEALNSLSQL 902
Cdd:TIGR00618 556 KQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490
....*....|....
gi 564335594 903 SYSTSSSKRQTQQL 916
Cdd:TIGR00618 632 LHLQQCSQELALKL 645
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
664-897 |
5.38e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 664 RKSLEDATEYIHRAEherLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHK-----ENSVSITEHLEVITTL 738
Cdd:PRK05771 15 KSYKDEVLEALHELG---VVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 739 RTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-----------------EKAAMSDAMVPKASYEKLQASLESEVNAL 801
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 802 AAKLKESV-------KEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRcsetssKL 874
Cdd:PRK05771 172 ISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK------KY 245
|
250 260
....*....|....*....|...
gi 564335594 875 EEDKDEKINEMTKEVLKLKEALN 897
Cdd:PRK05771 246 LEELLALYEYLEIELERAEALSK 268
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
430-682 |
6.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnteisengsDLSQKLKDtqskYEEAMKEVLSVQKQMklgl 509
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERR--------------------EALQRLAE----YSWDEIDVASAEREI---- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 lshesADGDSRLREVRVTDEDVDALKQ---DLQRALEESKRDKARVQELETKLvEKEKAEATkpssEVCEEMRNSYCSVI 586
Cdd:COG4913 671 -----AELEAELERLDASSDDLAALEEqleELEAELEELEEELDELKGEIGRL-EKELEQAE----EELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 587 ENMNKEKAFLFEKYQQAQeeimkLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDyrkrkS 666
Cdd:COG4913 741 DLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA-----D 810
|
250
....*....|....*.
gi 564335594 667 LEDATEYihRAEHERL 682
Cdd:COG4913 811 LESLPEY--LALLDRL 824
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
789-896 |
6.58e-04 |
|
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: 42.22 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 789 KLQAsLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE--------- 859
Cdd:COG1579 11 DLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnk 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564335594 860 -------ELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEAL 896
Cdd:COG1579 90 eyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
637-832 |
6.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 637 VDELNKQVSELSQLYREAQAELEDYRKR-----KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDM---RSQYSKVL 708
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEidklqAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgSESFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 709 NELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYE 788
Cdd:COG3883 119 DRLSALSKIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564335594 789 KLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 832
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
423-939 |
6.64e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 423 TADRDVIIQQLQDTLHDLQK------RLETSEAEKKQLQDELQSQRT---DTTCLNNTEISENGSDLSQKLKDTQSKYEE 493
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKlqslckELDILQREQATIDTRTSAFRDlqgQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 494 AMKEVLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQralEESKRDKARVQELETKLVEKEKAEATKPSSE 573
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ---EEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 574 VCEEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLK--SQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLY 651
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 652 REAQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVlnelTQLKQLVDAHKENSVSITEH 731
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI----RVLPKELLASRQLALQKMQS 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 732 LEvitTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLaeekaamsdamvpkasyEKLQASLESEVNALAAKLKESVKE 811
Cdd:TIGR00618 688 EK---EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 812 KEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLK 891
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 564335594 892 LKEA--LNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQE 939
Cdd:TIGR00618 828 QEEEqfLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
620-897 |
7.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 620 QEAPDDSGDMKETMNRMVDELNKQVSELSQLyreaqaeledyrkRKSLEDATEYIHRAEHERLMHLSNLSRTKAEesLSD 699
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDEL-------------SQELSDASRKIGEIEKEIEQLEQEEEKLKER--LEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 700 MRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVITTLRTMAKEMEEKTvtLQEHLASKEGEVAKLEKQLAEEKAAMSD 779
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 780 amvpkasyeklqasLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE 859
Cdd:TIGR02169 817 --------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|....*....
gi 564335594 860 ELAGLKR-CSETSSKLEEDKDeKINEMTKEVLKLKEALN 897
Cdd:TIGR02169 883 RLGDLKKeRDELEAQLRELER-KIEELEAQIEKKRKRLS 920
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
418-891 |
8.19e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 418 PAGTSTADRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNTEISENGSDLsqklKDTQSKYEEAMKE 497
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEM----KDTKISSLERNIR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 498 VLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE--------KEKAEATK 569
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETltnqnsdcKQHIEVLK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 570 PSSEVCEEMRNSYCSVIENMN---KEKAFLFEKYQQAQEEIMKLKDTLKSQMpqeapDDSGDMKETMNRMVDELNKQVSE 646
Cdd:pfam10174 331 ESLTAKEQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEI-----RDLKDMLDVKERKINVLQKKIEN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 647 LSQLYREAQAELEDYRKR-KSLEDATEYihraeherlmhlSNLSRTKAEESLSDMrsqySKVLNELTQLKQLVDahkens 725
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERvKSLQTDSSN------------TDTALTTLEEALSEK----ERIIERLKEQRERED------ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 726 vsiTEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEkqlaEEKAAMSDAMVPKASYEKlqaSLESEVNALAAKL 805
Cdd:pfam10174 464 ---RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLK---SLEIAVEQKKEEC 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 806 KESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEM 885
Cdd:pfam10174 534 SKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
....*.
gi 564335594 886 TKEVLK 891
Cdd:pfam10174 606 ESLTLR 611
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
106-196 |
8.43e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.32 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 106 LQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNG 185
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
|
90
....*....|.
gi 564335594 186 RTALMLACETG 196
Cdd:PLN03192 592 NTALWNAISAK 602
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
513-939 |
8.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 513 ESADGDSRLREVRVTDEDVDAL---KQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVIEN 588
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNhegKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRAdEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 589 MNKEKAFLfEKYQQAQ--EEIMKLKDTLKSQMPQEAPDDSgdMKETMNRMVDELNKQVSELSQLYREAQA---------- 656
Cdd:PTZ00121 1114 ARKAEEAK-KKAEDARkaEEARKAEDARKAEEARKAEDAK--RVEIARKAEDARKAEEARKAEDAKKAEAarkaeevrka 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 657 ----ELEDYRK-----RKSLEDATEYIHRAEHER---LMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKEN 724
Cdd:PTZ00121 1191 eelrKAEDARKaeaarKAEEERKAEEARKAEDAKkaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 725 SVSITEHLEVITTLRTM-------AKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESE 797
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEekkkadeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 798 VNALAAKLKESVKEKEKA---HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKL 874
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKA 1427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335594 875 EE-DKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLA-ECKKQHQE 939
Cdd:PTZ00121 1428 EEkKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEE 1494
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
527-897 |
9.21e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 527 TDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSS------------EVCEEMRNSYCSVIENMNKEKA 594
Cdd:pfam06160 98 IEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSygpaidelekqlAEIEEEFSQFEELTESGDYLEA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 595 flFEKYQQAQEEImklkDTLKSQMPqeapddsgDMKETMNRMVDELNKQVSELSQLYREAQAE---LEDYRKRKSLEDAT 671
Cdd:pfam06160 178 --REVLEKLEEET----DALEELME--------DIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVDKEIQQLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 672 EYIHRAeherLMHLSNLSRTKAEESLSDMRSQyskvLNEL-TQLKQLVDAHKEnsvsITEHLEVITTLRTMAKEMEEKTV 750
Cdd:pfam06160 244 EQLEEN----LALLENLELDEAEEALEEIEER----IDQLyDLLEKEVDAKKY----VEKNLPEIEDYLEHAEEQNKELK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 751 TLQEHLaskegevaKLEKQLAEEKAamsdamvpkASYEKLQASLEsEVNALAAKLKESVKEKEKAHSEvaqVRSEVSQAK 830
Cdd:pfam06160 312 EELERV--------QQSYTLNENEL---------ERVRGLEKQLE-ELEKRYDEIVERLEEKEVAYSE---LQEELEEIL 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 831 REKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETSSKLE--------EDKDEKINEMTKEVLKLKEALN 897
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLeLREIKRLVEksnlpglpESYLDYFFDVSDEIEDLADELN 446
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-189 |
9.82e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 64 GHVECLKVMVTHgvDVTAQDSSGHSALHIAA---KNGHPEYIKKLLQYKSPAESVDNL-----------GKTALHYAAAQ 129
Cdd:cd21882 6 GLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335594 130 GSLQAVQVLCEH--------------KSPINLKDLdGNIPLLVAIQNGHSEACHFLLDHGADVNS---RDKNGRTAL 189
Cdd:cd21882 84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVL 159
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
536-894 |
1.27e-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: 42.79 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 536 QDLQRALEESkRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENMNKEKAfLFEKYQQAQEEIMKLKDTLK 615
Cdd:pfam05483 257 KDLTFLLEES-RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQIATKTICQLTEEKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 616 SQMpqeapDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELED------------YRKRKSLEDATEYIHRAEHErlm 683
Cdd:pfam05483 335 AQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiitmelQKKSSELEEMTKFKNNKEVE--- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 684 hLSNLSRTKAE-ESLSDMRSQYSKVLNEL------------TQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTV 750
Cdd:pfam05483 407 -LEELKKILAEdEKLLDEKKQFEKIAEELkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 751 TLQEhLASKEGEVAKLEKQLAEEKAAMS--------DAMVPKASYEKL----------QASLESEVNALAAKLKESVKEK 812
Cdd:pfam05483 486 KNIE-LTAHCDKLLLENKELTQEASDMTlelkkhqeDIINCKKQEERMlkqienleekEMNLRDELESVREEFIQKGDEV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 813 ----EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKE 888
Cdd:pfam05483 565 kcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
....*.
gi 564335594 889 VLKLKE 894
Cdd:pfam05483 645 LASAKQ 650
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
433-896 |
1.45e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 433 LQDTLHDLQKRLETSEAEKKQLQDELQSqrtdttclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqMKLGLLSH 512
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELES--------TKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEE-MEQGIADE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 513 ESADGDSRLR-----------EVRVTDEDVDALKQDLQRALEESKRDKARVQE--LETKLVEKEKAEATK---PSSEVCE 576
Cdd:pfam05701 118 ASVAAKAQLEvakarhaaavaELKSVKEELESLRKEYASLVSERDIAIKRAEEavSASKEIEKTVEELTIeliATKESLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 577 EMRNSYCSVIEN-----MNKEKAFL-FEK-YQQAQEEIMKLKDTLKSQMPQEAPDDSG-----DMK-ETMNRMVDELNK- 642
Cdd:pfam05701 198 SAHAAHLEAEEHrigaaLAREQDKLnWEKeLKQAEEELQRLNQQLLSAKDLKSKLETAsalllDLKaELAAYMESKLKEe 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 643 --QVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHErlmhlSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDA 720
Cdd:pfam05701 278 adGEGNEKKTSTSIQAALA--SAKKELEEVKANIEKAKDE-----VNCLRVAAAS----LRSELEKEKAELASLRQREGM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 721 HKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHL--ASKEGEVAKLEKQLAEE--KAAMSDAMVPKASYEKLQA 792
Cdd:pfam05701 347 ASIAVSSLEAELNRtkseIALVQAKEKEAREKMVELPKQLqqAAQEAEEAKSLAQAAREelRKAKEEAEQAKAAASTVES 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 793 SLESevnalAAKLKESVKEKEKAHSEVAQV--RSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAqEELAGlKRCSET 870
Cdd:pfam05701 427 RLEA-----VLKEIEAAKASEKLALAAIKAlqESESSAESTNQEDSPRGVTLSLEEYYELSKRAHEA-EELAN-KRVAEA 499
|
490 500 510
....*....|....*....|....*....|..
gi 564335594 871 SSKLEEDKD------EKINEMTKEVLKLKEAL 896
Cdd:pfam05701 500 VSQIEEAKEselrslEKLEEVNREMEERKEAL 531
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
101-250 |
1.46e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.35 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 101 YIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL--LVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02946 54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335594 179 NSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSEN------AGIQSLLLSKISQDADLKTP 250
Cdd:PHA02946 134 NNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
431-559 |
1.51e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDtqskyeeaMKEVLSVQKQmklglL 510
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAERSRLQALL------------AELAGAGAAAEGRAGE--------LAQELDSEKQ-----V 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 511 SHESadgdsrLREVRVTDEDVDALKQ---DLQRALEES-KRDK---ARVQELETKL 559
Cdd:PRK09039 132 SARA------LAQVELLNQQIAALRRqlaALEAALDASeKRDResqAKIADLGRRL 181
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
160-230 |
1.90e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.97 E-value: 1.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 160 IQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSEN 230
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
699-865 |
2.11e-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: 41.20 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 699 DMRSQYSKVLNELTQLKQLVDAhKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 778
Cdd:cd22656 88 TIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 779 D------AMVPKASYEKLQASLESEVNALAAKLKESVKEKEKahsEVAQVRSEVSQAKRekenIQTLLKSKEQEVTELVQ 852
Cdd:cd22656 167 DlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA---LIADDEAKLAAALR----LIADLTAADTDLDNLLA 239
|
170
....*....|...
gi 564335594 853 KFQRAQEELAGLK 865
Cdd:cd22656 240 LIGPAIPALEKLQ 252
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
784-891 |
2.32e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 40.00 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 784 KASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVrsevsqakreKENIQTLLKSKEQEVTELVQKF-QRAQEELA 862
Cdd:PRK08475 48 KNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEA----------KEKAELIVETAKKEAYILTQKIeKQTKDDIE 117
|
90 100
....*....|....*....|....*....
gi 564335594 863 GLKRCSETSSKLEEDKDEKinEMTKEVLK 891
Cdd:PRK08475 118 NLIKSFEELMEFEVRKMER--EVVEEVLN 144
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-881 |
3.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 504 QMKLGLLSHESaDGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRnsyc 583
Cdd:COG4913 582 QVKGNGTRHEK-DDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLA---- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 584 svienmnkEKAFLFEKYQQAQEEIMKLKDTLksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEdyRK 663
Cdd:COG4913 655 --------EYSWDEIDVASAEREIAELEAEL------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG--RL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 664 RKSLEDATEYIHRAEhERLMHLSNLSRTKAEESLSDMRSQyskvlneltqlkQLVDAHkensvsitehlevittLRTMAK 743
Cdd:COG4913 719 EKELEQAEEELDELQ-DRLEAAEDLARLELRALLEERFAA------------ALGDAV----------------ERELRE 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 744 EMEEKTVTLQEHLASKEGEVAKLEKQLAEE-KAAMSDAMVPKASYEKLQASLES-EVNALA---AKLKESVKEKEKAhsE 818
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLALLDRlEEDGLPeyeERFKELLNENSIE--F 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 819 VAQVRSEVSQAKRE-KENIQTL----------------LKSKEQEVTElVQKFQRAqeelagLKRCSETSSKLEEDKDEK 881
Cdd:COG4913 848 VADLLSKLRRAIREiKERIDPLndslkripfgpgrylrLEARPRPDPE-VREFRQE------LRAVTSGASLFDEELSEA 920
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-179 |
3.49e-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: 3.49e-03
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
21-81 |
3.52e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.39 E-value: 3.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335594 21 DRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
640-883 |
3.73e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.30 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 640 LNKQVSELSQL-----YREAQAELE-DYRKRKSLEDATEYIHRAEHerlmhlSNLSRTKAEESLSDMRSQYSKVLNELTQ 713
Cdd:pfam18971 596 FNKAVAEAKSTgnydeVKKAQKDLEkSLRKREHLEKEVEKKLESKS------GNKNKMEAKAQANSQKDEIFALINKEAN 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 714 LKQLVDAHKENSVSITEHLEviTTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyeKLQAS 793
Cdd:pfam18971 670 RDARAIAYTQNLKGIKRELS--DKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDL--------GINPE 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 794 LESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE---KENIQTLLKSKEQEVT--ELVQKFQRAQEELAGLKRCS 868
Cdd:pfam18971 740 WISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDviiNQKVTDKVDNLNQAVSvaKAMGDFSRVEQVLADLKNFS 819
|
250
....*....|....*
gi 564335594 869 ETSSKLEEDKDEKIN 883
Cdd:pfam18971 820 KEQLAQQAQKNEDFN 834
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
430-666 |
3.77e-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: 40.90 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL 507
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 508 GLLSHESADGDSRLrEVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKpssevcEEMRNSYCSVIE 587
Cdd:COG4942 109 LLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL------EAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335594 588 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgdmketmNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 666
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAEL----------------AAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-109 |
3.88e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 3.88e-03
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
706-859 |
4.14e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 706 KVLNELT-QLKQLVDAHKensvsitehLEvittlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpk 784
Cdd:PRK09039 53 SALDRLNsQIAELADLLS---------LE-----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 785 asyeklqaslESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLL-----KSKEQEVT--ELVQKF--- 854
Cdd:PRK09039 115 ----------EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekRDRESQAKiaDLGRRLnva 184
|
....*..
gi 564335594 855 --QRAQE 859
Cdd:PRK09039 185 laQRVQE 191
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-682 |
4.69e-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: 40.81 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 343 ADQQDLLVLLQAKVASLtlhNKELQDKLQAKSPKETEADLSFQSFHSTQTDLAPSPSKSSDIPSSDAKSSPPVEhpagts 422
Cdd:TIGR02168 687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT------ 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 423 taDRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclnnTEISENGSDLSQKLKDTQSKYEeamkevlsvQ 502
Cdd:TIGR02168 758 --ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAA---------N 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 503 KQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQElETKLVEKEKAEATKPSSEVCEEMRNSY 582
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 583 cSVIENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYR 652
Cdd:TIGR02168 901 -EELRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 564335594 653 E----------AQAELEDYRKR---------------KSLEDATEYIHRAEHERL 682
Cdd:TIGR02168 980 KikelgpvnlaAIEEYEELKERydfltaqkedlteakETLEEAIEEIDREARERF 1034
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
32-124 |
4.74e-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: 40.93 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 32 AEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSS--------------GHSALHIAAKNG 97
Cdd:cd22193 55 AEKTDNLKRFINAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTN 134
|
90 100 110
....*....|....*....|....*....|
gi 564335594 98 HPEYIKKLLQ---YKSPAESVDNLGKTALH 124
Cdd:cd22193 135 QPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
539-861 |
4.96e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 539 QRALEESKRDKARVQELETKLVEKEKAEATKpssevceemrnsycsvienMNKEKAFLFEKYQQAQEEIMKLKDTLKSQM 618
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAE-------------------MDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 619 PQEAPD-DSGDMKETMNRMvDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihRAEHERLMHLSNLSRTKAEESL 697
Cdd:pfam17380 359 KRELERiRQEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQ---RKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 698 SDMRSQYSKVLNELTQLKQlVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKegevaKLEKQLAEEKAAM 777
Cdd:pfam17380 435 REVRRLEEERAREMERVRL-EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK-----ILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 778 SD-----AMVPKASYEKLQASLESEVNALAaklkESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLlkSKEQEVTELVQ 852
Cdd:pfam17380 509 IEeerkrKLLEKEMEERQKAIYEEERRREA----EEERRKQQEMEERRRIQEQMRKATEERSRLEAM--EREREMMRQIV 582
|
....*....
gi 564335594 853 KFQRAQEEL 861
Cdd:pfam17380 583 ESEKARAEY 591
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
431-885 |
4.97e-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: 40.93 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 431 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTD----TTCLNNTE-----ISENGSDLSQKLKDTQSKYEEAMKEVLSV 501
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEgknikLSKDVSSLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 502 QKQMK---------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQR------ALEESKRDKAR-----VQELETKLVE 561
Cdd:pfam01576 488 STRLRqledernslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagtleALEEGKKRLQRelealTQQLEEKAAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 562 KEKAEATKpssevcEEMRNSYCSVIENMNKEKAFL--FEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKE------TM 633
Cdd:pfam01576 568 YDKLEKTK------NRLQQELDDLLVDLDHQRQLVsnLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREketralSL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 634 NRMVDELNKQVSELSQLYREAQAELEDYRKRKslEDATEYIHRAEHerlmhlsnlSRTKAEESLSDMRsqyskvlnelTQ 713
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSK--DDVGKNVHELER---------SKRALEQQVEEMK----------TQ 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 714 LKQLVDahkENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAK----LEKQLAEEKAAMSDAMVPKASYEK 789
Cdd:pfam01576 701 LEELED---ELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKqvreLEAELEDERKQRAQAVAAKKKLEL 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 790 LQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSE 869
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR 857
|
490
....*....|....*.
gi 564335594 870 TSsklEEDKDEKINEM 885
Cdd:pfam01576 858 QA---QQERDELADEI 870
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
430-657 |
4.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 430 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGL 509
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 510 LSHESADGDSRLREVRvtdEDVDALKQDLQRALEESKRDKARVQELETKL--VEKEKAEATKpssEVCEEMRNSYcsvie 587
Cdd:COG3206 254 DALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIaaLRAQLQQEAQ---RILASLEAEL----- 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 588 nmnkekaflfEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEtMNRMVDELNKQVSELSQLYREAQAE 657
Cdd:COG3206 323 ----------EALQAREASLQAQLAQLEARL-AELPELEAELRR-LEREVEVARELYESLLQRLEEARLA 380
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-79 |
6.62e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.93 E-value: 6.62e-03
10 20
....*....|....*....|....*...
gi 564335594 52 EGKTAFHLAAAKGHVECLKVMVTHGVDV 79
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
432-897 |
8.04e-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: 40.00 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 432 QLQDTLHDLQKRLETSEAEKKQLQDELQSQrtdTTCLNNTEisENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKlglls 511
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQ--TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 512 hesaDGDSRLREVRVTDEDVDALK-QDLQRAL-EESKRDKARVQELETKLVEKEKA--EATKPSSEVCEEMRNSycsviE 587
Cdd:TIGR04523 285 ----ELEKQLNQLKSEISDLNNQKeQDWNKELkSELKNQEKKLEEIQNQISQNNKIisQLNEQISQLKKELTNS-----E 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 588 NMNKEKAFLFEKYQQAQEEIMKLKDTLKsqmpqeapddsgDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSL 667
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYK------------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 668 EDAteyihraEHERLMHLsnlsRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVI-TTLRTMAKEME 746
Cdd:TIGR04523 424 LEK-------EIERLKET----IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIkQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335594 747 EKT---VTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHS--EVAQ 821
Cdd:TIGR04523 493 SKEkelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKnkEIEE 572
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335594 822 VRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKleedKDEKINEMTKEVLKLKEALN 897
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK----ENEKLSSIIKNIKSKKNKLK 644
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-146 |
8.89e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 8.89e-03
10 20
....*....|....*....|....*...
gi 564335594 119 GKTALHYAAAQGSLQAVQVLCEHKSPIN 146
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
86-108 |
8.97e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 8.97e-03
|
| |
