|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-248 |
1.59e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 171.29 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
....*...
gi 564335602 241 ISQDADLK 248
Cdd:COG0666 275 LLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-246 |
3.70e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 164.74 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
....*.
gi 564335602 241 ISQDAD 246
Cdd:COG0666 242 GADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
1.08e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 97 GHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564335602 177 DVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-240 |
2.73e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.16 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 113 ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564335602 193 CETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
2.08e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.90 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 91 HIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 564335602 171 LLDHGADVNSRDKNGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-239 |
4.66e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHIAA--K 95
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 96 NGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGS--LQAVQVLCEHKSPINLKDldgNIPLLvaiqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 174 HGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
5.40e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 94.03 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 90 LHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKsPINLKDlDGNIPLLVAIQNGHSEACH 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335602 170 FLLDHGADVNSRD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
2.03e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHgADVNSRDkNGRTALMLACETGSANTVE 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335602 203 ALIKKGADLNLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
8.14e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPaeSVDNLGKTALHYAAAQGSLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 564335602 137 VLCEHKSPINLKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-215 |
3.73e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 94.71 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 88 SALHIAAKNGHP--EYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQV--LCEHKSPINLKDLDGNIPLLVAIQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFN 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVD 215
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-178 |
1.85e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 90.70 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 78 DVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESvdNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180
....*....|....*....|.
gi 564335602 158 VAIQNGHSEACHFLLDHGADV 178
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADV 681
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
27-218 |
1.46e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.62 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 27 VENGDAEKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGH--PEYI 102
Cdd:PHA03095 91 LYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 103 KKLLQYKSPAESVDNLGKTALHYAA--AQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACH--FLLDHGADV 178
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLLIAGISI 250
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564335602 179 NSRDKNGRTALMLAceTGSANTV--EALIKKGADLNLVDSLG 218
Cdd:PHA03095 251 NARNRYGQTPLHYA--AVFNNPRacRRLIALGADINAVSSDG 290
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-222 |
2.19e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 85.79 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 43 GASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQngHSEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTV 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDII 271
|
170 180
....*....|....*....|.
gi 564335602 202 EALIKKGADLNLVDSLGHNAL 222
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
1.25e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.12 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV---DVTAQDssGHSALHIAAKNGHPEYIKKLLQYKSPAES 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 115 VDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 564335602 194 ETGSANTVEALIKKGADLNLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-108 |
6.53e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHgVDVTAQDsSGHSALHIAAKNGHPEYI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*.
gi 564335602 103 KKLLQY 108
Cdd:pfam12796 78 KLLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-230 |
6.57e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.61 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLKVMVTHGVDVTAQDSSGHSALHI--AAKNGHPEYIKKL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 106 LQYKSPAESVDNLGKTALH-YAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF--LLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 182 DKNGRTALMLACETGS--ANTVEALIKKGADLNLVDSLGHNALYYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
7.93e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 156 LLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKgADLNLVDSlGHNALYYSKLSENAGIQS 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 564335602 236 LLLSK 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
2.66e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.24 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 79 VtaqdssghSALHIAAKNGhpEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLV 158
Cdd:PHA02874 94 T--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 159 AIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG----HNALYYsklseNAGIQ 234
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplHNAIIH-----NRSAI 238
|
250
....*....|....*....
gi 564335602 235 SLLLSKIS---QDADLKTP 250
Cdd:PHA02874 239 ELLINNASindQDIDGSTP 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
102-246 |
9.76e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 102 IKKLLQYKSPAESVDNLGKTALHY---AAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEAC-HFLLDHGAD 177
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGAD 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335602 178 VNSRDKNGRTALMlACETG---SANTVEALIKKGADLNLVDSLGHNAL--YYSKLSENAGIQSLLLSKISQDAD 246
Cdd:PHA03095 110 VNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-179 |
2.47e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.24 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 1 MKSLKAKFRKS-DTNEWNKNDDRLLQAVEN-----GDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK--GHVECLKVM 72
Cdd:PHA03100 48 IDVVKILLDNGaDINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 73 VTHGVDVTAQDSSGHSALHIAAKNGHPEY------------------IKKLLQYKSPAESVDNLGKTALHYAAAQGSLQA 134
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564335602 135 VQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
67-225 |
2.60e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.07 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 67 ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPIN 146
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335602 147 LKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACeTGSANTVEALIKKgADLNLVDSLGHNALYYS 225
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-225 |
5.09e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.17 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-KVMVTHGVDVTAQDSSGHSALHIAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 96 NGH-PEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQ-AVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLD 173
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564335602 174 HGADVNSRDKNGRTALMLA-CETGSANTVEALIKKGADLNLVDSLGHNALYYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-238 |
4.54e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.09 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKS 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 111 -----------------------------PAESVDNLGKTALHYAAAQGSL-QAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:PHA02876 236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 161 QNGH-SEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLL 238
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
5.23e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.52 E-value: 5.23e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 55 TAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
70-266 |
1.99e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 70 KVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKD 149
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 150 LDgnipLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGS-ANTVEALIKKGADLNLVDSLGHNALYYskLS 228
Cdd:PHA02876 242 LS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL--MA 315
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564335602 229 ENAGIQSLLLSKISQDADLKTP-----TKAKQAeiSSIQENKD 266
Cdd:PHA02876 316 KNGYDTENIRTLIMLGADVNAAdrlyiTPLHQA--STLDRNKD 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
578-838 |
2.03e-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: 68.17 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 578 MVDELNKQVSELsqlyREAQAELEDYRK-RKSLEDATEYIHRAEHErlmhlsnlsrtKAEESLSDMRSQYSKVLNELTQL 656
Cdd:TIGR02169 192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELLKEKE-----------ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 657 KQLVDAHKENSVSITEHLEVITtlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyEKLQASL 736
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-------EERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 737 ESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKL 816
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260
....*....|....*....|..
gi 564335602 817 EEDKDEKINEMTKEVLKLKEAL 838
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAI 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
579-859 |
3.34e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 579 VDELNKQVSELS------QLYREAQAELEDYRKR-KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLN 651
Cdd:COG1196 195 LGELERQLEPLErqaekaERYRELKEELKELEAElLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 652 ELTQLKQLVDAHKEN----SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpka 727
Cdd:COG1196 275 ELEELELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA----- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 728 syEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLK 807
Cdd:COG1196 350 --EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 808 rcsETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLE 859
Cdd:COG1196 428 ---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-223 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 88 SALHIAAKNGHPEYIKKLLQYKSpaesVDN-----LGKTALHYAAAQGSLQAVQVLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPS----CDLfqrgaLGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 158 VAIQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALY 223
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-838 |
1.87e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKqlqdELQSQRTDTTCLNNTEISENGS--DLSQKLKDTQSKYEEAMKEVLSVQKQMK- 448
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKe 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 449 ----------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE-KEKAEATKPSSEVC 517
Cdd:PRK03918 285 lkelkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 518 EEMRnsycSVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKETMNRMVDELNKQVSEL---- 589
Cdd:PRK03918 365 EEAK----AKKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELkkak 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 590 ---------------SQLYREAQAELEDYRKR-KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSD----MRSQYSKV 649
Cdd:PRK03918 436 gkcpvcgrelteehrKELLEEYTAELKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKY 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 650 -LNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-------------- 714
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlk 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 715 -------EKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQakREKENIQTLLKSKEQ 787
Cdd:PRK03918 596 elepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSR 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 788 EVTELVQKFQRAQEELAGLKRCSEtssKLEEDKdEKINEMTKEVLKLKEAL 838
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKAL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-886 |
2.46e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqmklgl 451
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKEL------------EEVLREINEISSELPELREELEKLEKEVKELEE------ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKrdkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENM 531
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK---KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 532 NKEKAFLFEKYQQAQEEIMKLkdtlkSQMPQEAPDDSGDMKETMNRmVDELNKQVsELSQLYREAQAELEDYRKRKS--- 608
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR-LEELEERH-ELYEEAKAKKEELERLKKRLTglt 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 609 ---LEDATEYIHRAEHERLMHLSNLSRTKAEesLSDMRSQYSKVLNELTQLK--------QLVDAHKENSvsITEHLEVI 677
Cdd:PRK03918 386 pekLEKELEELEKAKEEIEEEISKITARIGE--LKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL--LEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 678 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNALAA-KLKESVKEKEK 756
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA------------EQLKELEEKLKKYNLeELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 757 AHSEVAQVRSEVSQAKREKENIQTLLKSKEqevtELVQKFQRAQEELAGL-KRCSETSSKLEEDKDEKINEMTKEVLKLK 835
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYL 605
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 836 EALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEVVSVY 886
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
6.95e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 6.95e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 121 TALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
572-805 |
7.87e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.73 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 572 KETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihraehERLMHLSNLSRtkAEESLSDMRSQYSKVLN 651
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-------EAKLLLQQLSE--LESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 652 ELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMvpkasyEK 731
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335602 732 LQASLESEVNALAAK---LKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLkskeqevTELVQKFQRAQEELAG 805
Cdd:COG3206 314 ILASLEAELEALQAReasLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-------ESLLQRLEEARLAEAL 383
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-272 |
1.29e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.00 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 9 RKSDTNEWN-KNDDRLLQAVENG-DAEKVASLLgKKGASATKHDSEGKTAFHLAAA-KGHVECLKVMVTHGVDVTAQDSS 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA-AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNG- 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSanTVEALIKKGADLN----LVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRH 532
|
250 260 270
....*....|....*....|....*....|....*
gi 564335602 240 KISQDADlktPTKAKQAEISSIQENKDRL--SDST 272
Cdd:PHA02876 533 DIRNEVN---PLKRVPTRFTSLRESFKEIiqSDDT 564
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
1.83e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 1.83e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564335602 86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
2.06e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 2.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 155 PLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALI 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-874 |
4.37e-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: 60.46 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 579 VDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQ 658
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 659 LVDAHKEN-SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLE 737
Cdd:TIGR02168 779 EAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 738 SEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLK-RCSETSSKL 816
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRI 938
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 564335602 817 EEDKdEKINEmtKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEmlqqqvkqlqNQLAE 874
Cdd:TIGR02168 939 DNLQ-ERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRLE----------NKIKE 983
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-195 |
7.89e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 59.12 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 113 ESVDNLGKTALHYAAAQ-GSLQAVQVLCEHKSPINLKD-LDGNIPLLVAIqngHSE-ACHFLLDHGADVNSRDKNGRTAL 189
Cdd:PHA02878 228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304
|
....*.
gi 564335602 190 MLACET 195
Cdd:PHA02878 305 SSAVKQ 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-823 |
1.04e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 374 QLQDTLHDLQKRLETSEAEKKQLQDELQSQrtdttclnnTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQ--KQMKLGL 451
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKEL---------EEKEERLEELKKKLKELEKRLEELEERHELYEeaKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKA----RVQELETKLVEKEKAEATKP------SSEVCEEMR 521
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGelkkEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 522 NSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgDMKETMNRMVDELNKQVSELSQL-YREAQAEL 600
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE----------SELIKLKELAEQLKELEEKLKKYnLEELEKKA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 601 EDYRKRKSLEDATEYIHRAEHERLMHLSNLSRTKA--EESLSDMRSQYSKVLNELTQ------------LKQLVDAHKE- 665
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAelEKKLDELEEELAELLKELEElgfesveeleerLKELEPFYNEy 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 666 NSVSITEHlEVITTLRTMAKEmEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLqaSLESEVNALAA 745
Cdd:PRK03918 605 LELKDAEK-ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRA 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 746 KLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEqEVTELVQKFQR--AQEELAGLKRCSETSSKL-EEDKDE 822
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKykALLKERALSKVGEIASEIfEELTEG 759
|
.
gi 564335602 823 K 823
Cdd:PRK03918 760 K 760
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-859 |
2.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnteisENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLG- 450
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELR------------LELEELELELEEAQAEEYELLAELARLEQDIARLe 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 451 -LLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 529
Cdd:COG1196 309 eRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 530 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSL 609
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 610 EDATEYIHRAEHERLMHLSNL-SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 688
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAaARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 689 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV 768
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 769 SQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYST 848
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490
....*....|.
gi 564335602 849 SSSKRQTQQLE 859
Cdd:COG1196 709 LAEAEEERLEE 719
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
459-836 |
3.45e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 459 GDSRLREVRVTDEDVDALKQ-DLQRALEESKRDKARVQELETKLVEkekaeaTKPSSEVCEEMRNSYCSVIENMNKekaf 537
Cdd:PRK02224 172 SDARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 538 LFEKYQQAQEEIMKLKdtlksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyih 617
Cdd:PRK02224 242 VLEEHEERREELETLE---------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 618 RAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsitehleviTTLRTMAKEMEEKTVTLQEH 697
Cdd:PRK02224 310 EAVEARREELED-RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 698 LASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKE---SVKEKEKAHSEVAQVRSE------- 767
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 768 -----------VSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE------ELAGLKRCSETSSKLEEDKDEKINEMTKE 830
Cdd:PRK02224 459 qpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRER 538
|
....*.
gi 564335602 831 VLKLKE 836
Cdd:PRK02224 539 AEELRE 544
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-222 |
3.63e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.42 E-value: 3.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 564335602 171 LLDHG-ADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
463-807 |
5.86e-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: 57.00 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 463 LREVRVTDEDVDA----LKQDLQRaLEESKRDKARVQELETklvEKEKAEATKPSSEVcEEMRNSycsvIENMNKEKAFL 538
Cdd:TIGR02169 179 LEEVEENIERLDLiideKRQQLER-LRREREKAERYQALLK---EKREYEGYELLKEK-EALERQ----KEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 539 FEKYQQAQEEIMKLKDTLksqmpqeapddsgdmkETMNRMVDELNKQVSELSqlyreaqaELEDYRKRKSLEDATEYIHR 618
Cdd:TIGR02169 250 EEELEKLTEEISELEKRL----------------EEIEQLLEELNKKIKDLG--------EEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 619 AehERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHL----EVITTLRTMAKEMEEKTVTL 694
Cdd:TIGR02169 306 L--ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 695 QEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 774
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350
....*....|....*....|....*....|...
gi 564335602 775 KENIQTLLKSKEQEVTELVQKFQRAQEELAGLK 807
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-238 |
5.90e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 60 AAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLC 139
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 140 EHKSPINlkDL---DGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDS 216
Cdd:PHA02875 89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
|
170 180
....*....|....*....|..
gi 564335602 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 |
7.73e-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: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTH-----GVDVTAQDSSGHSALHIA 93
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 94 AKNGHPEYIKKLLQY----KSP-------AESVDNL---GKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL-LV 158
Cdd:cd22192 97 VVNQNLNLVRELIARgadvVSPratgtffRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564335602 159 AIQNGHSEACH---FLLDHGADVNS------RDKNGRTALMLACETGSANTVEALIKK 207
Cdd:cd22192 177 VLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
390-838 |
2.17e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 390 EAEKKQLQDELQSQRTDTTCLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVT 469
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 470 DEDVDALKQDLQ--RALEESKR---DKARVQELETKLVEKEKAEATKPSSEvceEMRNSYCSVIENMNKEKAflfEKYQQ 544
Cdd:PTZ00121 1417 KKKADEAKKKAEekKKADEAKKkaeEAKKADEAKKKAEEAKKAEEAKKKAE---EAKKADEAKKKAEEAKKA---DEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 545 AQEEIMKLKDTLKSQMPQEAPDDSGDMKETmNRMVDELNK-----QVSELSQlyREAQAELEDYRKRKSLEDATEYIHRA 619
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE-AKKADEAKKaeeakKADEAKK--AEEKKKADELKKAEELKKAEEKKKAE 1567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 620 EHERLMHLSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLA 699
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEE----AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKE 1642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 700 SKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENiq 779
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-- 1720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 564335602 780 tlLKSKEQEVTELVQKFQRAQEELaglKRCSETSSKLEEDKDeKINEMTKEVLKLKEAL 838
Cdd:PTZ00121 1721 --LKKAEEENKIKAEEAKKEAEED---KKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEI 1773
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-206 |
2.42e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 127 AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIK 206
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
131-240 |
2.96e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.07 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 131 SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQN----GHS-EACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEAL- 204
Cdd:PHA02798 50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILl 129
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564335602 205 --IKKGADLNLVDSLGHNAL-YYSKLSENAGIQ--SLLLSK 240
Cdd:PHA02798 130 fmIENGADTTLLDKDGFTMLqVYLQSNHHIDIEiiKLLLEK 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-93 |
4.46e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 4.46e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 564335602 50 DSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIA 93
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
100-229 |
5.20e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 100 EYIKKLLQYKSPAESVD-NLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564335602 179 NSRDKNGRTALMLAC-ETGSANTVEALIKKGADLNLVDS-LGHNALYYSKLSE 229
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-240 |
5.24e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHP---EYIKKLLQY 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 109 KSPAESVDN-LGKTALHyaaaqgslqavqvlCEHKSpiNLKDLDGNIpllvaiqnghseaCHFLLDHGADVNSRDKNGRT 187
Cdd:PHA02798 171 GVDINTHNNkEKYDTLH--------------CYFKY--NIDRIDADI-------------LKLFVDNGFIINKENKSHKK 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564335602 188 ALM------LACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:PHA02798 222 KFMeylnslLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
569-837 |
5.52e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 569 GDMKETMNRMVDELNKQvSELSQLYREAQAELEDYRKRKSLEDATEYihraeherlmhlsnlsrtkaeeslsdmRSQYSK 648
Cdd:TIGR02168 192 EDILNELERQLKSLERQ-AEKAERYKELKAELRELELALLVLRLEEL---------------------------REELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 649 VLNELTQLKQLVDAHKENsvsITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKAS 728
Cdd:TIGR02168 244 LQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 729 YEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAG--- 805
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnn 400
|
250 260 270
....*....|....*....|....*....|...
gi 564335602 806 -LKRCSETSSKLEEDKDEKINEMTKEVLKLKEA 837
Cdd:TIGR02168 401 eIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
6.06e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 6.06e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335602 189 LMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKISQDADLKTPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
374-835 |
6.71e-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: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 374 QLQDTLHDLQKRLETSEAEKKQLQ-------------DELQSQRTDttclNNTEISENGSDLSQKLKDTQSKYEEAMKEV 440
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitiDHLRRELDD----RNMEVQRLEALLKAMKSECQGQMERQMAAI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 441 LSvqKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELEtKLVEKEKAEATKPSSEVCEEM 520
Cdd:pfam15921 454 QG--KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 521 RNsycsvIENMNKEKAFLfeKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAEL 600
Cdd:pfam15921 531 QE-----LQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 601 EDYRKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVIT-T 679
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 680 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 759
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 760 EVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLK 835
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
51-227 |
7.56e-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: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVdnlGKTALHyAAA 128
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 129 QGSLQAVQVLCEHKSPINLKDLD--------------GNIPLLVAIQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564335602 184 ---NGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKL 227
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
7.57e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564335602 68 CLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-83 |
7.82e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.80 E-value: 7.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQD 83
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
35-161 |
8.53e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.27 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKngHPEYIKKLLQYKSPAES 114
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIND 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564335602 115 VDNLGKTALHYAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQ 161
Cdd:PHA02874 250 QDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
1.12e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 72 MVTHG-VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-857 |
1.39e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 427 KDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQdlqRALEESKRDKARVQELETKLVEKEK 506
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 507 AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQAqEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQV 586
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 587 SElSQLYREAQAELEDYRKRKSLEDATEYIHRAEHERL----MHLSNLSRTKAEESL--SDMRSQYSKVLNELTQLKQLV 660
Cdd:PTZ00121 1441 EE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeeAKKADEAKKKAEEAKkkADEAKKAAEAKKKADEAKKAE 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 661 DAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSD------AMVPKASYEKLQA 734
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeaKKAEEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 735 SLESEVNALAAKLKESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTElVQKFQRAQEElaGLKRCSETSS 814
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEE--NKIKAAEEAK 1668
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564335602 815 KLEEDKD--EKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQ 857
Cdd:PTZ00121 1669 KAEEDKKkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
91-185 |
1.41e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 91 HIAAkNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 564335602 171 LLDHGADVNSRDKNG 185
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-839 |
1.90e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnnteisengsDLSQKLKDTQSKYEEAMKEVLSVQKQMKLgl 451
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE------------ELEREIEEERKRRDKLTEEYAELKEELED-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEkaeatkpssevcEEMRNSYCSVIENM 531
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL------------ADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 532 NK---EKAFLFEKYQQAQEEIMKLKDTLKSqmpqeAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 608
Cdd:TIGR02169 437 NEleeEKEDKALEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 609 LEDATEYIHRAEHERLMHLSNLSR--TKAEESLSDMRSQYSKV-------------------------LNELTQLKQLVD 661
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNVVVeddavakeaiellkrrkagratflpLNKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 662 AHKENSVsITEHLEVIT---TLRTMAKEMEEKTVTLQEHLASKE--GEV--AKLEKQLAEEKAAMSDAMVPKASYEKLQA 734
Cdd:TIGR02169 592 ILSEDGV-IGFAVDLVEfdpKYEPAFKYVFGDTLVVEDIEAARRlmGKYrmVTLEGELFEKSGAMTGGSRAPRGGILFSR 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 735 SLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETS 813
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLE 750
|
490 500 510
....*....|....*....|....*....|..
gi 564335602 814 SKLEEDKDE------KINEMTKEVLKLKEALN 839
Cdd:TIGR02169 751 QEIENVKSElkeleaRIEELEEDLHKLEEALN 782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-839 |
2.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnntEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQM--KL 449
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELE-----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 450 GLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVI 528
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 529 ENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQA 598
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLeelaeaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 599 ELEDY-------RKRKSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNE---LTQLKQLVDAHKENSV 668
Cdd:COG1196 539 ALEAAlaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdLVASDLREADARYYVL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 669 SITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNALAAKLK 748
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR------------ELLAALLEAEAELEELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 749 ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMT 828
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
490
....*....|.
gi 564335602 829 KEVLKLKEALN 839
Cdd:COG1196 767 RELERLEREIE 777
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
6.57e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 6.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 564335602 145 INLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
162-247 |
7.17e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 162 NGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKI 241
Cdd:PTZ00322 92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
....*.
gi 564335602 242 SQDADL 247
Cdd:PTZ00322 172 QCHFEL 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-839 |
8.21e-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: 50.06 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRL-------ETSEAEKKQLQDELQSQRTDTTCLnNTEISENGS---DLSQKLKDTQSKYEEAMKEVL 441
Cdd:TIGR02168 276 VSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEEL-EAQLEELESkldELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 442 SVQKQMK--------LGLLSHE--------SADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE 505
Cdd:TIGR02168 355 SLEAELEeleaeleeLESRLEEleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 506 KAEATKPSSEVcEEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-QMPQEAPDDSGDMKETMNRMVDELNK 584
Cdd:TIGR02168 435 LKELQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlQARLDSLERLQENLEGFSEGVKALLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 585 QVSELSQL-------------YREA-----QAELEDY--RKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRS 644
Cdd:TIGR02168 514 NQSGLSGIlgvlselisvdegYEAAieaalGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLP-LDSIKGTEIQGNDRE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 645 QYSKVLNELTQLKQLVDAHKENSVSIT---EHLEVITTLRT---MAKEMEEKT--VTLQEHLASKEG------------- 703
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNaleLAKKLRPGYriVTLDGDLVRPGGvitggsaktnssi 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 704 -----EVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENI 778
Cdd:TIGR02168 673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 779 QTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKLEEDkdekINEMTKEVLKLKEALN 839
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE---LAEAEAEIEELEAQ----IEQLKEELKALREALD 806
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
184-213 |
8.22e-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: 43.35 E-value: 8.22e-06
10 20 30
....*....|....*....|....*....|
gi 564335602 184 NGRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-803 |
1.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 381 DLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGllSHESAD 458
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAAELESELEEAREAVEDR--REEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 459 GDSRLREVRV----TDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYC--------- 525
Cdd:PRK02224 389 LEEEIEELRErfgdAPVDLGNAEDFLEELREERDELREREAELEATL--RTARERVEEAEALLEAGKCPECgqpvegsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 526 -SVIENMNKEKAFLFEKYQQAQEEIMKLKDTLksqmpqeapDDSGDMKETMNRmVDELNKQVSELSQLYREAQAELEDYR 604
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERL---------ERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 605 KR--KSLEDATEYIHRAEHERlmhlsnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH---KENSVSITEHLEVITT 679
Cdd:PRK02224 537 ERaeELRERAAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 680 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEekAAMSDAMVPKASYEKLQASLESEVNALAAklkesvkEKEKAHS 759
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELRE-------ERDDLQA 681
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564335602 760 EVAQVRSEVSQAKREKENIQTL------LKSKEQEVTELVQKFQRAQEEL 803
Cdd:PRK02224 682 EIGAVENELEELEELRERREALenrveaLEALYDEAEELESMYGDLRAEL 731
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-141 |
1.19e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLKVMVTHGVDVTAQDSSG 86
Cdd:PTZ00322 43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564335602 87 HSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
105-159 |
1.23e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 105 LLQYKSPA-ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVA 159
Cdd:pfam13857 1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-808 |
1.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 626 HLSNLSRtkAEESLSDMRSQyskvLNELTQLKQLVDAHKENSVSITEHLEVITTLRtmAKEMEEKTVTLQEHLASKEGEV 705
Cdd:COG4913 233 HFDDLER--AHEALEDAREQ----IELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 706 AKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV----------------- 768
Cdd:COG4913 305 ARLEAELERLEARLDAL---REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaee 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 769 -----SQAKREKENIQTLLKSKEQEVTELVQKFQRAQE-------ELAGLKR 808
Cdd:COG4913 382 faalrAEAAALLEALEEELEALEEALAEAEAALRDLRRelreleaEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
372-711 |
1.87e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnTEISENGSDLSQKlKDTQSKYEEAMKEVlsvqkqmklgl 451
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVK--------SELKELEARIEEL-EEDLHKLEEALNDL----------- 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 lshESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQeLETKLVEKEKAEATKPSSEvCEEMRNSYCSVIENM 531
Cdd:TIGR02169 785 ---EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENL 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 532 NKEKAFLFEKYQQAQEEIMKLKDTLKSqmpqeapddsgdmketMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLED 611
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 612 ATEyihRAEHERLMHLSNLSRTKAEESLSDMrsQYSKVLNELTQLKQLVDAHKE-NSVSITEHLEVITTLrtmaKEMEEK 690
Cdd:TIGR02169 924 AKL---EALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRL----DELKEK 994
|
330 340
....*....|....*....|.
gi 564335602 691 TVTLQEHLASKEGEVAKLEKQ 711
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKK 1015
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
52-81 |
2.11e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 2.11e-05
10 20 30
....*....|....*....|....*....|
gi 564335602 52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-800 |
2.29e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDttcLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKlgll 452
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKL---LQLLPLYQELEALEAELAELPERLEELEERLEELRELEE---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 453 shesaDGDSRLREVRVTDEDVDALKQDL-QRALEESKRDKARVQELETKLVEKEKAEATkpSSEVCEEMRNSYCSVIENM 531
Cdd:COG4717 164 -----ELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEE--AQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 532 NKEKafLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELnkqVSELSQLYREAQAELEDYRKRKSLED 611
Cdd:COG4717 237 EAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 612 ATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLvdahkENSVSITEHLEVITTLRTMAK----EM 687
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----EEELQLEELEQEIAALLAEAGvedeEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 688 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVpkasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSE 767
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430
....*....|....*....|....*....|....*
gi 564335602 768 VSQAKREKE--NIQTLLKSKEQEVTELVQKFQRAQ 800
Cdd:COG4717 462 LEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
184-215 |
3.80e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.51 E-value: 3.80e-05
10 20 30
....*....|....*....|....*....|...
gi 564335602 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 |
4.24e-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: 41.12 E-value: 4.24e-05
10 20 30
....*....|....*....|....*....|....
gi 564335602 151 DGNIPLLVAI-QNGHSEACHFLLDHGADVNSRDK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
373-837 |
6.10e-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: 47.09 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLETSEAEKKQLQDElqsqrtdttclnNTEISENGSDLSQKLKDtqskyEEAMKEVLSVQKqmklgll 452
Cdd:pfam01576 71 QELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 453 shesADGDSRLREVrvtDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE-----------KAEATKPSSEV----C 517
Cdd:pfam01576 127 ----VTTEAKIKKL---EEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEekakslsklknKHEAMISDLEErlkkE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 518 EEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-----QMPQEAPDDSGDMKETMNRMVDELNKQVSELSQ- 591
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALARLEEETAQKNNALKKIRELEAQISELQEd 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 592 --LYREAQAELEDYRK---------RKSLED-----ATEYIHRAEHERlmHLSNLSRTKAEES------LSDMRSQYSKV 649
Cdd:pfam01576 280 leSERAARNKAEKQRRdlgeelealKTELEDtldttAAQQELRSKREQ--EVTELKKALEEETrsheaqLQEMRQKHTQA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 650 LNELT-QLKQLvdahKENSVSITEHLEVittLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKAS 728
Cdd:pfam01576 358 LEELTeQLEQA----KRNKANLEKAKQA---LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 729 YEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAK-------REKENIQTLLKSKEQEVTELVQKFQRAQE 801
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
490 500 510
....*....|....*....|....*....|....*.
gi 564335602 802 ELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEA 837
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
373-836 |
7.45e-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: 46.55 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL- 449
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 450 ----GLLSHESADGDSRLREVR----VTDEDVDALKQDLQRALEESKRDKARVQELETKL--VEKEKAEATKPSSEVCEE 519
Cdd:TIGR04523 116 keqkNKLEVELNKLEKQKKENKknidKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnlLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 520 MRNSY--CSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKsQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 597
Cdd:TIGR04523 196 LLKLEllLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 598 AELEDYRKRKSLEDATEYIHraeherlMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVI 677
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLK-------SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS---QNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 678 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKA 757
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335602 758 HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKE 836
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
562-774 |
7.87e-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: 45.91 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 562 QEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEE---- 637
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIRALEQELAALEAELAELEKEIaelr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 638 -SLSDMRSQYSKVLNELTQLKQ----LVDAHKENSVSITEHLEVITTL----RTMAKEMEEKTVTLQEHLASKEGEVAKL 708
Cdd:COG4942 97 aELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 709 EKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 774
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
540-838 |
8.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 540 EKYQQAQEEIMKLKDTLKSQMPQ-----EAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAT 613
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 614 EYIHRAEHERLMHLSNLSRTKA-----EESLSDMRSQYS---KVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAK 685
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEkirelEERIEELKKEIEeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 686 EMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVR 765
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564335602 766 SEVSQAKREKENIQTLLKSKEQEVTELvqkfQRAQEELAGLKRCSETSSKL--EEDKDEKINEMTKEVLKLKEAL 838
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGREltEEHRKELLEEYTAELKRIEKEL 468
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-245 |
1.33e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.64 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLG--KTALHYAAAQGSLQA 134
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVaiKDAFNNRNVEIFKII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 135 VQVLCEHKSPINLKDLDgNIPLLVAIQnghSEACHFLLDHGADVNSRDKN-GRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:PHA02878 121 LTNRYKNIQTIDLVYID-KKSKDDIIE---AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
|
170 180 190
....*....|....*....|....*....|...
gi 564335602 214 VDSLGHNALYYS-KLSENAGIQSLLLSKISQDA 245
Cdd:PHA02878 197 PDKTNNSPLHHAvKHYNKPIVHILLENGASTDA 229
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
372-665 |
1.36e-04 |
|
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: 46.10 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtDTTCLNNTEISENGS---DLSQKLKDTQSK---YEEAMKEVLSVQK 445
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 446 QMKLGLLSHESADG---DSRLREVRVTDEdVDALKQDLQRAlEESKRDKARVQELETKLV-EKEKAEATKPSSEVCEEMR 521
Cdd:COG3096 428 LCGLPDLTPENAEDylaAFRAKEQQATEE-VLELEQKLSVA-DAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 522 nSYCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 597
Cdd:COG3096 506 -SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 598 AELEDYR-KRKSLEdATEYIHRAEHERLMHLSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKE 665
Cdd:COG3096 585 QQLEQLRaRIKELA-ARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQ 654
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
576-796 |
1.36e-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: 45.61 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 576 NRMVD-ELNKQVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHERLMHLSNLS----RTKAEEslsDMRSQYSKVL 650
Cdd:pfam09726 414 SRQTEqELRSQISSLTSLERSLKSELG--QLRQENDLLQTKLHNAVSAKQKDKQTVQqlekRLKAEQ---EARASAEKQL 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 651 NELTQLKQLVDAHKENSVS--ITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKaamsdamvpkaS 728
Cdd:pfam09726 489 AEEKKRKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELR-----------K 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335602 729 YEKLQASLESEVNALAAkLKESVKEKEKAHSEVAQVR----SEVSQAKREKENIQTLLKSKEQEVTELVQKF 796
Cdd:pfam09726 558 YKESEKDTEVLMSALSA-MQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
1.39e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMV 73
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
566-784 |
1.49e-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: 45.44 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 566 DDSGDMKETMNRMVDELNKQVSELSQLYreaQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNLSRtKAEESLSDM--R 643
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQL---PAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRR-ALEAKRKDPfkS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 644 SQYSKVLNELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKtvtlqehlaskegevakLEKQLAEEKAAMSDAm 723
Cdd:pfam13166 355 IELDSVDAKIESINDLVASINE---LIAKHNEITDNFEEEKNKAKKK-----------------LRLHLVEEFKSEIDE- 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 724 vpkasYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKS 784
Cdd:pfam13166 414 -----YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
478-837 |
1.60e-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: 45.49 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 478 QDLQRALEESKRDKAR--------VQELETKLVEKEK-----AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQ 544
Cdd:pfam15921 88 KDLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMerdamADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLED 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 545 AQEEIMKLKDTLKSQ--MPQEAPDDSGDMKETMNRMVDELNKQV--------SELSQLYREAQAELEDYRKRK-SLEDAT 613
Cdd:pfam15921 168 SNTQIEQLRKMMLSHegVLQEIRSILVDFEEASGKKIYEHDSMStmhfrslgSAISKILRELDTEISYLKGRIfPVEDQL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 614 EYI--------------HRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQlvDAHKENSVSITEHLEVITT 679
Cdd:pfam15921 248 EALksesqnkielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLEST 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 680 LRTMAKEMEEKTVTLqehlaskEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKL----KESVKEKE 755
Cdd:pfam15921 326 VSQLRSELREAKRMY-------EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 756 KAHS----------EVAQVRSEVSQAKREKENIQTLLKSKEQEVT-ELVQKFQRAQEELAGLKRCSETSSKLEEDKD--- 821
Cdd:pfam15921 399 QNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlr 478
|
410
....*....|....*.
gi 564335602 822 EKINEMTKEVLKLKEA 837
Cdd:pfam15921 479 KVVEELTAKKMTLESS 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
431-839 |
1.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 431 SKYEEAMKEVLSVQKQmKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAT 510
Cdd:COG4717 49 ERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 511 KPSSEVCEEMRNSYCSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSQmpqeapddSGDMKETMNRMVDELNKQVSELS 590
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAEL--------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 591 QLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYsKVLNELTQLKQLVDAHKENSVSI 670
Cdd:COG4717 199 EELEELQQRLAELEEE--LEEAQEELEELEEELEQLENELEAAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 671 TEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK-QLAEEKAAMSDAMVPkasyeklqaslESEVNALAAKLKE 749
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP-----------PDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 750 SVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTK 829
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410
....*....|.
gi 564335602 830 EVLK-LKEALN 839
Cdd:COG4717 425 LDEEeLEEELE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
373-882 |
1.91e-04 |
|
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: 45.43 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLetSEAEKKQLQDELQSQRTDTTCLNNTEisengSDLSQKLKDTQSKYEEAMKEVLSVQKQM----- 447
Cdd:TIGR02168 216 KELKAELRELELAL--LVLRLEELREELEELQEELKEAEEEL-----EELTAELQELEEKLEELRLEVSELEEEIeelqk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 448 KLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYCSV 527
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL--EEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 528 IENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEApddsgDMKETMNRMVDELNKQVSELSQLYREAQ-AELEDYRKR 606
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 607 KSLEDATEYIHRAEHERLMH-LSNL--SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH----------KENSVSITEH 673
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEaLEELreELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvkalLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 674 LEVITTLRTMAKEME-EKTVTLQEHLAS----------------KEGEVAKL-----------------EKQLAEEKAAM 719
Cdd:TIGR02168 522 LGVLSELISVDEGYEaAIEAALGGRLQAvvvenlnaakkaiaflKQNELGRVtflpldsikgteiqgndREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 720 SDAMVPKASYEKLQASLES------------EVNALAAKLKE-----------------SVKEKEKAHSEVAQVRSEVSQ 770
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYllggvlvvddldNALELAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 771 AKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKrcsetssKLEEDKDEKINEMTKEVLKL-KEALNSLSQLSYSTS 849
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSK 754
|
570 580 590
....*....|....*....|....*....|...
gi 564335602 850 SSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEV 882
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
47-162 |
1.98e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 43.11 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 47 TKHDSEGKTAFHLAAAKGHVECLKVMV------THGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYK-------SPAE 113
Cdd:PHA02741 15 AEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLielgadiNAQE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 114 SVDnlGKTALHYAAAQGSLQAVQVLCEHKSpINLK--DLDGNIPLLVAIQN 162
Cdd:PHA02741 95 MLE--GDTALHLAAHRRDHDLAEWLCCQPG-IDLHfcNADNKSPFELAIDN 142
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-179 |
2.26e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 2.26e-04
10 20
....*....|....*....|....*....
gi 564335602 151 DGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-808 |
2.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 688 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAK-----LKESVKEKEKAHSEVA 762
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564335602 763 QVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR 808
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
465-818 |
2.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 465 EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAtkpssevceEMRNSYCSVIENMNKEKAFL--FEKY 542
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES---------DLEQDYQAASDHLNLVQTALrqQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 543 QQAQEEIMKLKDTLKSQM-----PQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDateyih 617
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE------ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 618 raEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsiTEHLEVITTLRTMAKEME--------- 688
Cdd:PRK04863 425 --RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAYQLVRKIAGEVSrseawdvar 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 689 ------EKTVTLQEHLASKEGEVAKLEKQLAEEKAA--MSDAMVPKASyekLQASLESEVNALAAKLKESVKEKEKAHSE 760
Cdd:PRK04863 500 ellrrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAerLLAEFCKRLG---KNLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335602 761 VAQVRSEVSQAKREkeniqtlLKSKEQEVTELVQKFQRAQEELAGLKRCS----ETSSKLEE 818
Cdd:PRK04863 577 ARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSgeefEDSQDVTE 631
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
2.77e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|...
gi 564335602 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 |
3.02e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 3.02e-04
10 20
....*....|....*....|....*....
gi 564335602 184 NGRTALMLACETGSANTVEALIKKGADLN 212
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
635-806 |
3.42e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 635 AEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK 710
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 711 QLAEEKAAMSDAMV------------------------------------PKASYEKLQASLEsEVNALAAKLKESVKEK 754
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspedfldavrrlqylkylapaRREQAEELRADLA-ELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564335602 755 EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL 806
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
129-232 |
3.93e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 44.28 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 129 QGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKG 208
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
90 100
....*....|....*....|....*....
gi 564335602 209 A-----DLNLVDSLGHNALYYSKLSENAG 232
Cdd:PHA02876 235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
102-247 |
4.06e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 43.49 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 102 IKKLLQYKSpAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLkdLDGNIPLLVAIQNGHSEACHFLLDHGADVNSR 181
Cdd:PHA02791 14 LKSFLSSKD-AFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335602 182 DKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG-HNALYYSKLSENAGIQSLLLSKISQDADL 247
Cdd:PHA02791 91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
373-834 |
4.11e-04 |
|
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: 44.40 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLETSEAEKKQLQDELQsqrTDTTCLNNTE-----ISENGSDLSQKLKDTQSKYEEamKEVLSVQKQM 447
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQ---AETELCAEAEemrarLAARKQELEEILHELESRLEE--EEERSQQLQN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 448 KLGLLSHESADGDSRLrevrvtdEDVDALKQDLQraLEESKRDkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSV 527
Cdd:pfam01576 97 EKKKMQQHIQDLEEQL-------DEEEAARQKLQ--LEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 528 IENMNKEKAFLFEKYQQAQEEIM-----KLKDTLKSQMPQEApddsgdMKETMNRMVDELNKQVSELSQLYREAQAELEd 602
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMIsdleeRLKKEEKGRQELEK------AKRKLEGESTDLQEQIAELQAQIAELRAQLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 603 yRKRKSLEDAteyIHRAEHErlmhlsNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEvitTLRT 682
Cdd:pfam01576 240 -KKEEELQAA---LARLEEE------TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE---ALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 683 MAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAA----------------------MSDAMVPKASYEKLQASLESEV 740
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSheaqlqemrqkhtqaleelteqLEQAKRNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 741 NALAAKLK-------ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL-KRCSET 812
Cdd:pfam01576 387 AELQAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLsKDVSSL 466
|
490 500
....*....|....*....|..
gi 564335602 813 SSKLeEDKDEKINEMTKEVLKL 834
Cdd:pfam01576 467 ESQL-QDTQELLQEETRQKLNL 487
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
606-839 |
4.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 606 RKSLEDATEYIHRAEherLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHK-----ENSVSITEHLEVITTL 680
Cdd:PRK05771 15 KSYKDEVLEALHELG---VVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 681 RTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-----------------EKAAMSDAMVPKASYEKLQASLESEVNAL 743
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 744 AAKLKESV-------KEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRcsetssKL 816
Cdd:PRK05771 172 ISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK------KY 245
|
250 260
....*....|....*....|...
gi 564335602 817 EEDKDEKINEMTKEVLKLKEALN 839
Cdd:PRK05771 246 LEELLALYEYLEIELERAEALSK 268
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
375-795 |
5.13e-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: 43.94 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 375 LQDTLHDLQKRLETSEAEKKQLQDELQSQRTD----TTCLNNTEIS----ENGSDLSQKLKDTQSKYEEAMKEVLSVQKQ 446
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSEleemTKFKNNKEVEleelKKILAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 447 MKLGLLSHESADGDSRLREVRVTDEDVDALKQ--DLQRALEESKRDKARVQELETKLVEKEKaEATKPSSEVCEEMRNSY 524
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENK-ELTQEASDMTLELKKHQ 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 525 CSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSqMPQEAPDDSGDMKETMNRmvDELNKQVSELSQLYREAQAELEDYR 604
Cdd:pfam05483 520 EDIINCKKQEERML-KQIENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 605 ---KRKSLEDATEYIHRAEHERlmhlSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVitT 679
Cdd:pfam05483 596 cnnLKKQIENKNKNIEELHQEN----KALKKKGSAENkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI--S 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 680 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 759
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH---KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 564335602 760 EVAQVRSEVSQAKR----EKENIQTLLKSKEQEVTELVQK 795
Cdd:pfam05483 747 ELSNIKAELLSLKKqleiEKEEKEKLKMEAKENTAILKDK 786
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
106-196 |
8.46e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.32 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 106 LQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNG 185
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
|
90
....*....|.
gi 564335602 186 RTALMLACETG 196
Cdd:PLN03192 592 NTALWNAISAK 602
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
160-376 |
8.53e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 160 IQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENagiqsllLS 239
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN-------ID 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 240 KISQDADLKTPTKAKQAEISSIQENKDrLSDSTAGADSLLDVSSEADQQDLLVLLQAKVASLTLHNKELQDK---LQAKS 316
Cdd:PHA02876 226 TIKAIIDNRSNINKNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERgadVNAKN 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 317 PK-ETEADLSFQSFHSTQtDLAPSPSKSSDIPSSDAKSSPPVeHPAGTSTADRDVIIQQLQ 376
Cdd:PHA02876 305 IKgETPLYLMAKNGYDTE-NIRTLIMLGADVNAADRLYITPL-HQASTLDRNKDIVITLLE 363
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-189 |
9.13e-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: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 64 GHVECLKVMVTHgvDVTAQDSSGHSALHIAA---KNGHPEYIKKLLQYKSPAESVDNL-----------GKTALHYAAAQ 129
Cdd:cd21882 6 GLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335602 130 GSLQAVQVLCEH--------------KSPINLKDLdGNIPLLVAIQNGHSEACHFLLDHGADVNS---RDKNGRTAL 189
Cdd:cd21882 84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVL 159
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
572-774 |
9.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 572 KETMNRMVDELNKQVSELSQLYREAQAELEDYRKR-----KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDM---R 643
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEidklqAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 644 SQYSKVLNELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAM 723
Cdd:COG3883 112 ESFSDFLDRLSALSKIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564335602 724 VPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 774
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-624 |
9.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnteisengsDLSQKLKDtqskYEEAMKEVLSVQKQMklgl 451
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERR--------------------EALQRLAE----YSWDEIDVASAEREI---- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 lshesADGDSRLREVRVTDEDVDALKQ---DLQRALEESKRDKARVQELETKLvEKEKAEATkpssEVCEEMRNSYCSVI 528
Cdd:COG4913 671 -----AELEAELERLDASSDDLAALEEqleELEAELEELEEELDELKGEIGRL-EKELEQAE----EELDELQDRLEAAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 529 ENMNKEKAFLFEKYQQAQeeimkLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDyrkrkS 608
Cdd:COG4913 741 DLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA-----D 810
|
250
....*....|....*.
gi 564335602 609 LEDATEYihRAEHERL 624
Cdd:COG4913 811 LESLPEY--LALLDRL 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-839 |
1.30e-03 |
|
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: 42.75 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 562 QEAPDDSGDMKETMNRMVDELNKQVSELSQLyreaqaeledyrkRKSLEDATEYIHRAEHERLMHLSNLSRTKAEesLSD 641
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDEL-------------SQELSDASRKIGEIEKEIEQLEQEEEKLKER--LEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 642 MRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVITTLRTMAKEMEEKTvtLQEHLASKEGEVAKLEKQLAEEKAAMSD 721
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 722 amvpkasyeklqasLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE 801
Cdd:TIGR02169 817 --------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270
....*....|....*....|....*....|....*....
gi 564335602 802 ELAGLKR-CSETSSKLEEDKDeKINEMTKEVLKLKEALN 839
Cdd:TIGR02169 883 RLGDLKKeRDELEAQLRELER-KIEELEAQIEKKRKRLS 920
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
455-881 |
1.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 455 ESADGDSRLREVRVTDEDVDAL---KQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVIEN 530
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNhegKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRAdEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 531 MNKEKAFLfEKYQQAQ--EEIMKLKDTLKSQMPQEAPDDSgdMKETMNRMVDELNKQVSELSQLYREAQA---------- 598
Cdd:PTZ00121 1114 ARKAEEAK-KKAEDARkaEEARKAEDARKAEEARKAEDAK--RVEIARKAEDARKAEEARKAEDAKKAEAarkaeevrka 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 599 ----ELEDYRK-----RKSLEDATEYIHRAEHER---LMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKEN 666
Cdd:PTZ00121 1191 eelrKAEDARKaeaarKAEEERKAEEARKAEDAKkaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 667 SVSITEHLEVITTLRTM-------AKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESE 739
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEekkkadeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 740 VNALAAKLKESVKEKEKA---HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKL 816
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKA 1427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 817 EE-DKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQE 881
Cdd:PTZ00121 1428 EEkKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
731-838 |
1.47e-03 |
|
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: 41.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 731 KLQAsLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE--------- 801
Cdd:COG1579 11 DLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnk 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564335602 802 -------ELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEAL 838
Cdd:COG1579 90 eyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
101-250 |
1.51e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 101 YIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL--LVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02946 54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335602 179 NSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSEN------AGIQSLLLSKISQDADLKTP 250
Cdd:PHA02946 134 NNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
365-881 |
1.64e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 365 TADRDVIIQQLQDTLHDLQK------RLETSEAEKKQLQDELQSQRT---DTTCLNNTEISENGSDLSQKLKDTQSKYEE 435
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKlqslckELDILQREQATIDTRTSAFRDlqgQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 436 AMKEVLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQralEESKRDKARVQELETKLVEKEKAEATKPSSE 515
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ---EEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 516 VCEEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLK--SQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLY 593
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 594 REAQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVlnelTQLKQLVDAHKENSVSITEH 673
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI----RVLPKELLASRQLALQKMQS 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 674 LEvitTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLaeekaamsdamvpkasyEKLQASLESEVNALAAKLKESVKE 753
Cdd:TIGR00618 688 EK---EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 754 KEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLK 833
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 564335602 834 LKEA--LNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQE 881
Cdd:TIGR00618 828 QEEEqfLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
373-501 |
1.87e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 373 QQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDtqskyeeaMKEVLSVQKQmklglL 452
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAERSRLQALL------------AELAGAGAAAEGRAGE--------LAQELDSEKQ-----V 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 453 SHESadgdsrLREVRVTDEDVDALKQ---DLQRALEES-KRDK---ARVQELETKL 501
Cdd:PRK09039 132 SARA------LAQVELLNQQIAALRRqlaALEAALDASeKRDResqAKIADLGRRL 181
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
360-833 |
1.93e-03 |
|
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: 42.12 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 360 PAGTSTADRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNTEISENGSDLsqklKDTQSKYEEAMKE 439
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEM----KDTKISSLERNIR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 440 VLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE--------KEKAEATK 511
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETltnqnsdcKQHIEVLK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 512 PSSEVCEEMRNSYCSVIENMN---KEKAFLFEKYQQAQEEIMKLKDTLKSQMpqeapDDSGDMKETMNRMVDELNKQVSE 588
Cdd:pfam10174 331 ESLTAKEQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEI-----RDLKDMLDVKERKINVLQKKIEN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 589 LSQLYREAQAELEDYRKR-KSLEDATEYihraeherlmhlSNLSRTKAEESLSDMrsqySKVLNELTQLKQLVDahkens 667
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERvKSLQTDSSN------------TDTALTTLEEALSEK----ERIIERLKEQRERED------ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 668 vsiTEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEkqlaEEKAAMSDAMVPKASYEKlqaSLESEVNALAAKL 747
Cdd:pfam10174 464 ---RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLK---SLEIAVEQKKEEC 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 748 KESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEM 827
Cdd:pfam10174 534 SKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605
|
....*.
gi 564335602 828 TKEVLK 833
Cdd:pfam10174 606 ESLTLR 611
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
374-858 |
2.09e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 374 QLQDTLHDlqkRLETSEAEKKQLQDELQSQRtdttclnnteISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLS 453
Cdd:TIGR00618 212 CMPDTYHE---RKQVLEKELKHLREALQQTQ----------QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 454 HESADGDSRLR----EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 529
Cdd:TIGR00618 279 LEETQERINRArkaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 530 NMNKEKAFLFEKYQQAQEEIMKLKdtlksqmpqeapddsgDMKETMNRMVDELNKQVSELSQLYRE-AQAELEDYRKrks 608
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIH----------------TLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAF--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 609 ledateyihRAEHERLMHLsnlsRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 688
Cdd:TIGR00618 420 ---------RDLQGQLAHA----KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 689 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESevnalAAKLKESVKEKEkahsevAQVRSEV 768
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQLETSEEDVY------HQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 769 SQAKREKENIQTLlkskEQEVTELVQKFQRAQEELAGLKRCSET----SSKLEEDKDEKINEMTKEVLKLKEALNSLSQL 844
Cdd:TIGR00618 556 KQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490
....*....|....
gi 564335602 845 SYSTSSSKRQTQQL 858
Cdd:TIGR00618 632 LHLQQCSQELALKL 645
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
726-833 |
3.09e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 39.23 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 726 KASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVrsevsqakreKENIQTLLKSKEQEVTELVQKF-QRAQEELA 804
Cdd:PRK08475 48 KNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEA----------KEKAELIVETAKKEAYILTQKIeKQTKDDIE 117
|
90 100
....*....|....*....|....*....
gi 564335602 805 GLKRCSETSSKLEEDKDEKinEMTKEVLK 833
Cdd:PRK08475 118 NLIKSFEELMEFEVRKMER--EVVEEVLN 144
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-179 |
3.28e-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: 3.28e-03
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
469-839 |
3.49e-03 |
|
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: 40.99 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 469 TDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSS------------EVCEEMRNSYCSVIENMNKEKA 536
Cdd:pfam06160 98 IEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSygpaidelekqlAEIEEEFSQFEELTESGDYLEA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 537 flFEKYQQAQEEImklkDTLKSQMPqeapddsgDMKETMNRMVDELNKQVSELSQLYREAQAE---LEDYRKRKSLEDAT 613
Cdd:pfam06160 178 --REVLEKLEEET----DALEELME--------DIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVDKEIQQLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 614 EYIHRAeherLMHLSNLSRTKAEESLSDMRSQyskvLNEL-TQLKQLVDAHKEnsvsITEHLEVITTLRTMAKEMEEKTV 692
Cdd:pfam06160 244 EQLEEN----LALLENLELDEAEEALEEIEER----IDQLyDLLEKEVDAKKY----VEKNLPEIEDYLEHAEEQNKELK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 693 TLQEHLaskegevaKLEKQLAEEKAamsdamvpkASYEKLQASLEsEVNALAAKLKESVKEKEKAHSEvaqVRSEVSQAK 772
Cdd:pfam06160 312 EELERV--------QQSYTLNENEL---------ERVRGLEKQLE-ELEKRYDEIVERLEEKEVAYSE---LQEELEEIL 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 773 REKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETSSKLE--------EDKDEKINEMTKEVLKLKEALN 839
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLeLREIKRLVEksnlpglpESYLDYFFDVSDEIEDLADELN 446
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
641-807 |
3.60e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 641 DMRSQYSKVLNELTQLKQLVDAhKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 720
Cdd:cd22656 88 TIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 721 D------AMVPKASYEKLQASLESEVNALAAKLKESVKEKEKahsEVAQVRSEVSQAKRekenIQTLLKSKEQEVTELVQ 794
Cdd:cd22656 167 DlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA---LIADDEAKLAAALR----LIADLTAADTDLDNLLA 239
|
170
....*....|...
gi 564335602 795 KFQRAQEELAGLK 807
Cdd:cd22656 240 LIGPAIPALEKLQ 252
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
21-81 |
3.65e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.01 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335602 21 DRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
478-836 |
4.27e-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: 40.86 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 478 QDLQRALEESkRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENMNKEKAfLFEKYQQAQEEIMKLKDTLK 557
Cdd:pfam05483 257 KDLTFLLEES-RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQIATKTICQLTEEKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 558 SQMpqeapDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELED------------YRKRKSLEDATEYIHRAEHErlm 625
Cdd:pfam05483 335 AQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiitmelQKKSSELEEMTKFKNNKEVE--- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 626 hLSNLSRTKAE-ESLSDMRSQYSKVLNEL------------TQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTV 692
Cdd:pfam05483 407 -LEELKKILAEdEKLLDEKKQFEKIAEELkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 693 TLQEhLASKEGEVAKLEKQLAEEKAAMS--------DAMVPKASYEKL----------QASLESEVNALAAKLKESVKEK 754
Cdd:pfam05483 486 KNIE-LTAHCDKLLLENKELTQEASDMTlelkkhqeDIINCKKQEERMlkqienleekEMNLRDELESVREEFIQKGDEV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 755 ----EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKE 830
Cdd:pfam05483 565 kcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
....*.
gi 564335602 831 VLKLKE 836
Cdd:pfam05483 645 LASAKQ 650
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
582-825 |
4.76e-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: 40.91 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 582 LNKQVSELSQL-----YREAQAELE-DYRKRKSLEDATEYIHRAEHerlmhlSNLSRTKAEESLSDMRSQYSKVLNELTQ 655
Cdd:pfam18971 596 FNKAVAEAKSTgnydeVKKAQKDLEkSLRKREHLEKEVEKKLESKS------GNKNKMEAKAQANSQKDEIFALINKEAN 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 656 LKQLVDAHKENSVSITEHLEviTTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyeKLQAS 735
Cdd:pfam18971 670 RDARAIAYTQNLKGIKRELS--DKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDL--------GINPE 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 736 LESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE---KENIQTLLKSKEQEVT--ELVQKFQRAQEELAGLKRCS 810
Cdd:pfam18971 740 WISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDviiNQKVTDKVDNLNQAVSvaKAMGDFSRVEQVLADLKNFS 819
|
250
....*....|....*
gi 564335602 811 ETSSKLEEDKDEKIN 825
Cdd:pfam18971 820 KEQLAQQAQKNEDFN 834
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
32-124 |
4.85e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 40.55 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 32 AEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSS--------------GHSALHIAAKNG 97
Cdd:cd22193 55 AEKTDNLKRFINAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTN 134
|
90 100 110
....*....|....*....|....*....|
gi 564335602 98 HPEYIKKLLQ---YKSPAESVDNLGKTALH 124
Cdd:cd22193 135 QPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-109 |
4.91e-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: 35.26 E-value: 4.91e-03
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
648-801 |
5.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 648 KVLNELT-QLKQLVDAHKensvsitehLEvittlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpk 726
Cdd:PRK09039 53 SALDRLNsQIAELADLLS---------LE-----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 727 asyeklqaslESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLL-----KSKEQEVT--ELVQKF--- 796
Cdd:PRK09039 115 ----------EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekRDRESQAKiaDLGRRLnva 184
|
....*..
gi 564335602 797 --QRAQE 801
Cdd:PRK09039 185 laQRVQE 191
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
375-838 |
5.38e-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: 40.40 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 375 LQDTLHDLQKRLETSEAEKKQLQDELQSqrtdttclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqMKLGLLSH 454
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELES--------TKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEE-MEQGIADE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 455 ESADGDSRLR-----------EVRVTDEDVDALKQDLQRALEESKRDKARVQE--LETKLVEKEKAEATK---PSSEVCE 518
Cdd:pfam05701 118 ASVAAKAQLEvakarhaaavaELKSVKEELESLRKEYASLVSERDIAIKRAEEavSASKEIEKTVEELTIeliATKESLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 519 EMRNSYCSVIEN-----MNKEKAFL-FEK-YQQAQEEIMKLKDTLKSQMPQEAPDDSG-----DMK-ETMNRMVDELNK- 584
Cdd:pfam05701 198 SAHAAHLEAEEHrigaaLAREQDKLnWEKeLKQAEEELQRLNQQLLSAKDLKSKLETAsalllDLKaELAAYMESKLKEe 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 585 --QVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHErlmhlSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDA 662
Cdd:pfam05701 278 adGEGNEKKTSTSIQAALA--SAKKELEEVKANIEKAKDE-----VNCLRVAAAS----LRSELEKEKAELASLRQREGM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 663 HKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHL--ASKEGEVAKLEKQLAEE--KAAMSDAMVPKASYEKLQA 734
Cdd:pfam05701 347 ASIAVSSLEAELNRtkseIALVQAKEKEAREKMVELPKQLqqAAQEAEEAKSLAQAAREelRKAKEEAEQAKAAASTVES 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 735 SLESevnalAAKLKESVKEKEKAHSEVAQV--RSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAqEELAGlKRCSET 812
Cdd:pfam05701 427 RLEA-----VLKEIEAAKASEKLALAAIKAlqESESSAESTNQEDSPRGVTLSLEEYYELSKRAHEA-EELAN-KRVAEA 499
|
490 500 510
....*....|....*....|....*....|..
gi 564335602 813 SSKLEEDKD------EKINEMTKEVLKLKEAL 838
Cdd:pfam05701 500 VSQIEEAKEselrslEKLEEVNREMEERKEAL 531
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
481-803 |
5.57e-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: 40.49 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 481 QRALEESKRDKARVQELETKLVEKEKAEATKpssevceemrnsycsvienMNKEKAFLFEKYQQAQEEIMKLKDTLKSQM 560
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAE-------------------MDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 561 PQEAPD-DSGDMKETMNRMvDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihRAEHERLMHLSNLSRTKAEESL 639
Cdd:pfam17380 359 KRELERiRQEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQ---RKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 640 SDMRSQYSKVLNELTQLKQlVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKegevaKLEKQLAEEKAAM 719
Cdd:pfam17380 435 REVRRLEEERAREMERVRL-EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK-----ILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 720 SD-----AMVPKASYEKLQASLESEVNALAaklkESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLlkSKEQEVTELVQ 794
Cdd:pfam17380 509 IEeerkrKLLEKEMEERQKAIYEEERRREA----EEERRKQQEMEERRRIQEQMRKATEERSRLEAM--EREREMMRQIV 582
|
....*....
gi 564335602 795 KFQRAQEEL 803
Cdd:pfam17380 583 ESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-608 |
5.70e-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: 40.13 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL 449
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 450 GLLSHESADGDSRLrEVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKpssevcEEMRNSYCSVIE 529
Cdd:COG4942 109 LLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL------EAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335602 530 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgdmketmNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 608
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAEL----------------AAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-79 |
6.23e-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: 6.23e-03
10 20
....*....|....*....|....*...
gi 564335602 52 EGKTAFHLAAAKGHVECLKVMVTHGVDV 79
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
372-599 |
6.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 372 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGL 451
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 452 LSHESADGDSRLREVRvtdEDVDALKQDLQRALEESKRDKARVQELETKLvEKEKAEATKPSSEVCEEMRNSYcsvienm 531
Cdd:COG3206 254 DALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQI-AALRAQLQQEAQRILASLEAEL------- 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335602 532 nkekaflfEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEtMNRMVDELNKQVSELSQLYREAQAE 599
Cdd:COG3206 323 --------EALQAREASLQAQLAQLEARL-AELPELEAELRR-LEREVEVARELYESLLQRLEEARLA 380
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
72-297 |
6.76e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.04 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 72 MVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGS--LQAVQVLCEHKSPINLK- 148
Cdd:PHA02946 58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 149 DLDGNIPLLvAIQNGHSEACHFLLDHGADVNSRDKNGRTAL--MLACETGSANTVEALIKKGADLNLVDSLGHNALYY-- 224
Cdd:PHA02946 138 DEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIvc 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335602 225 SKLSENAGIQSLLLSKISQDADLK---TPTKAKQAEISSIQENKDRLSDSTAGADSLLDVSSEADQQDLLVLLQAK 297
Cdd:PHA02946 217 SKTVKNVDIINLLLPSTDVNKQNKfgdSPLTLLIKTLSPAHLINKLLSTSNVITDQTVNICIFYDRDDVLEIINDK 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
446-823 |
7.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 446 QMKLGLLSHESaDGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRnsyc 525
Cdd:COG4913 582 QVKGNGTRHEK-DDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLA---- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 526 svienmnkEKAFLFEKYQQAQEEIMKLKDTLksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEdyRK 605
Cdd:COG4913 655 --------EYSWDEIDVASAEREIAELEAEL------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG--RL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 606 RKSLEDATEYIHRAEhERLMHLSNLSRTKAEESLSDMRSQyskvlneltqlkQLVDAHkensvsitehlevittLRTMAK 685
Cdd:COG4913 719 EKELEQAEEELDELQ-DRLEAAEDLARLELRALLEERFAA------------ALGDAV----------------ERELRE 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 686 EMEEKTVTLQEHLASKEGEVAKLEKQLAEE-KAAMSDAMVPKASYEKLQASLESEVN----ALAAKLKESVKEKEKAhsE 760
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLALLDRLEEdglpEYEERFKELLNENSIE--F 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 761 VAQVRSEVSQAKRE-KENIQTL----------------LKSKEQEVTElVQKFQRAqeelagLKRCSETSSKLEEDKDEK 823
Cdd:COG4913 848 VADLLSKLRRAIREiKERIDPLndslkripfgpgrylrLEARPRPDPE-VREFRQE------LRAVTSGASLFDEELSEA 920
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
119-146 |
8.36e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 8.36e-03
10 20
....*....|....*....|....*...
gi 564335602 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 |
8.45e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 8.45e-03
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
156-384 |
8.63e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 39.85 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 156 LLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQS 235
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 236 LL-----LSKISQDADLKTpTKAKQAEISSIQE------NKDrlSDSTAGADSLLDVSSE--ADQQDLLVLLQAKVASLT 302
Cdd:PLN03192 609 ILyhfasISDPHAAGDLLC-TAAKRNDLTAMKEllkqglNVD--SEDHQGATALQVAMAEdhVDMVRLLIMNGADVDKAN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 303 LHNK----ELQDKLQAK----------SPKETEADLSfQSFHSTQTDLAPSPSKSSDIPS-SDAKSSPPVEHPAGTSTAD 367
Cdd:PLN03192 686 TDDDfsptELRELLQKRelghsitivdSVPADEPDLG-RDGGSRPGRLQGTSSDNQCRPRvSIYKGHPLLRNERCCNEAG 764
|
250
....*....|....*..
gi 564335602 368 RDViiqQLQDTLHDLQK 384
Cdd:PLN03192 765 KLI---NLPPSLEELKA 778
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
528-778 |
9.83e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 528 IENMNKEK-AFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAqAELEDyrKR 606
Cdd:PRK05771 33 IEDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI-KELEE--EI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 607 KSLEDATEyIHRAEHERLMHLSNLSrtkaeeslSDMrsqysKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKE 686
Cdd:PRK05771 110 SELENEIK-ELEQEIERLEPWGNFD--------LDL-----SLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335602 687 MEEKT---VTLQEHlaskEGEVAKLEKQLAEEKAAMSDAMVPK---ASYEKLQASLESEVNALAAKLKESVKEKEKahsE 760
Cdd:PRK05771 176 KGYVYvvvVVLKEL----SDEVEEELKKLGFERLELEEEGTPSeliREIKEELEEIEKERESLLEELKELAKKYLE---E 248
|
250
....*....|....*...
gi 564335602 761 VAQVRSEVSQAkREKENI 778
Cdd:PRK05771 249 LLALYEYLEIE-LERAEA 265
|
|
| |
