|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-240 |
9.48e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.14 E-value: 9.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 1 MEAKTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHS 80
Cdd:COG0666 43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 81 ALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEIC 160
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 161 HFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLK 240
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
3-249 |
6.46e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.05 E-value: 6.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 3 AKTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSAL 82
Cdd:COG0666 12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 83 HLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHF 162
Cdd:COG0666 92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 163 LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTP 242
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
|
....*..
gi 224809476 243 TKPKQHD 249
Cdd:COG0666 252 GLTALLL 258
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-214 |
8.86e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 152.03 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 9 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKN 88
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 89 SHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGA 168
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224809476 169 DVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNAL 214
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
25-232 |
3.33e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 135.85 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 25 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPA 104
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 105 ESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224809476 185 CEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 232
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
3-181 |
3.26e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 3 AKTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSA 81
Cdd:COG0666 111 ADVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 82 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICH 161
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
170 180
....*....|....*....|
gi 224809476 162 FLLDHGADVNSRNKSGRTAL 181
Cdd:COG0666 270 LLLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
82-174 |
4.53e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 94.03 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 82 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 161
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 224809476 162 FLLDHGADVNSRN 174
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
115-207 |
4.86e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 115 LHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHgADVNSRNKsGRTALMLACEIGSSNAVE 194
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 224809476 195 ALIKKGADLNLVD 207
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
49-141 |
6.82e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQsKCPAESVDsSGKTALHYAAAQGCLQAVQ 128
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 224809476 129 ILCEHKSPINLKD 141
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
15-231 |
2.81e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 91.65 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 15 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLRVMITHGVDVTAQDTTGHSALHLAAKNS 89
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 90 --HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEHKSPINLKDldgNIPLLLavqnghseichfllD 165
Cdd:PHA03100 118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYLL--------------S 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809476 166 HGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLS 231
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
3-216 |
1.51e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 89.70 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 3 AKTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLRVMITHGVDVTAQDTTG 78
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 79 HSALHLAAKNSH--HECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI--LCEHKSPINLKDLDGNIPLLLAVQN 154
Cdd:PHA03095 188 RSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVF 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809476 155 GHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDslgyNALHY 216
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
12-174 |
5.07e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 89.54 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 12 DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH 91
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHH 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 92 ECIRKLLQskCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:PLN03192 605 KIFRILYH--FASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
|
...
gi 224809476 172 SRN 174
Cdd:PLN03192 683 KAN 685
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
148-232 |
1.04e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 148 LLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKgADLNLVDSlGYNALHYSKLSENAGIQS 227
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 224809476 228 LLLSK 232
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
21-222 |
3.39e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 82.38 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 21 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLRVMITHGVDVTAQDTTGHSALH--LAAKNSHHECIRKL 97
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 98 LQSKCPAESVDSSGKTALH-YAAAQGC-LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHS--EICHFLLDHGADVNSR 173
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224809476 174 NKSGRTALMLACEIGSSNA--VEALIKKGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
30-206 |
5.89e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 30 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGV---DVTAQDttGHSALHLAAKNSHHECIRKLLQSKCPAES 106
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 107 VDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALM-LAC 185
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 224809476 186 EIGSSNAVEALIKKGADLNLV 206
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
15-102 |
8.57e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 15 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHgVDVTAQDtTGHSALHLAAKNSHHECI 94
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*...
gi 224809476 95 RKLLQSKC 102
Cdd:pfam12796 78 KLLLEKGA 85
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
15-242 |
1.48e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.39 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 15 LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAqdttghsalhLAAKNSHHECI 94
Cdd:PHA02874 39 LIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 95 RKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRN 174
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 175 KSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQsLLLSKIS---QDADLKTP 242
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLINNASindQDIDGSTP 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-938 |
3.98e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 501
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 578
Cdd:PRK03918 256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 579 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 659 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 727
Cdd:PRK03918 382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 728 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 807
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 808 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 224809476 887 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 938
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-886 |
1.22e-13 |
|
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: 75.48 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 594
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 595 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 672
Cdd:TIGR02168 772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 752
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 753 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 832
Cdd:TIGR02168 927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 224809476 833 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:TIGR02168 986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-217 |
4.04e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 9 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-RVMITHGVDVTAQDTTGHSALHLAAK 87
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 88 NSHH-ECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI-LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLD 165
Cdd:PHA02876 317 NGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224809476 166 HGADVNSRNKSGRTALMLA-CEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
23-230 |
2.93e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.48 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 23 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKC 102
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 103 PAESVDSSgktaLHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGH-SEICHFLLDHGADVNSRNKSGRTAL 181
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224809476 182 MLACEIG-SSNAVEALIKKGADLNLVDSLGYNALHY-SKLSENAGIQSLLL 230
Cdd:PHA02876 312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQaSTLDRNKDIVITLL 362
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
585-890 |
3.06e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 585 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 663
Cdd:COG1196 210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 664 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 742
Cdd:COG1196 287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 743 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809476 823 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-926 |
3.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 LvspESMDNYShfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSYCSVIEN 581
Cdd:COG1196 308 E---ERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR--KS 659
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 660 LEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ---------LKQLVDAQKENSVSITEHLQVIT 730
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 731 TLRTAAkemEEKISNLKEHLASKEVEVAKLEKQLLEEKAA-------MTDAMVPRSSYEKLQSSLESEVSVLASKLKESV 803
Cdd:COG1196 535 AYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 804 KEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 224809476 884 TKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
35-209 |
4.47e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 35 GASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTA 114
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 115 LHYAAAQGCLQAVQILCEHKS-------------------------------PINLKDLDGNIPLLLAVQNGHS-EICHF 162
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNhimnkckngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPCDiDIIDI 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224809476 163 LLDHGADVNSRNKSGRTALMLACE-IGSSNAVEALIKKGADLNLVDSL 209
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIANAVLIKEADKL 321
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-911 |
1.01e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenssdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI----------------EELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 LVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSsycsVI 579
Cdd:PRK03918 296 IKLSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKA----KK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASdEAEDMKEAMNRMIDELNKQVSELsqlyKEAQ-------AELE 652
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEEL----KKAKgkcpvcgRELT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 653 DYRKRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMK-SQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIT- 730
Cdd:PRK03918 447 EEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAe 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 731 ---TLRTAAKEMEEKISNLKEHLASKEV---EVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSsLESEVSVLAS----- 797
Cdd:PRK03918 526 eyeKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLdeLEEELAELLKELEELGFESVEE-LEERLKELEPfyney 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 798 -KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFqqAQEELAEMKRYAESSSKLEEDKDKKI 876
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
490 500 510
....*....|....*....|....*....|....*
gi 224809476 877 NEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-891 |
2.37e-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: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 502
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI------------EELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 503 VSPESMDnySHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVErekgtvikppveEYEEMKSSYCSVIENM 582
Cdd:TIGR02169 371 AELEEVD--KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 583 NKekafLFEKYQEAQEEIMKLKDTLKS--QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL 660
Cdd:TIGR02169 437 NE----LEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 661 EDVTAEYIhKAEHEKLMQLTNVSRAKA-----------------EDALSEMKSQYSKV----------LNELTQLKQLVD 713
Cdd:TIGR02169 513 EEVLKASI-QGVHGTVAQLGSVGERYAtaievaagnrlnnvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 714 AQKENSVsITEHLQVIttlrtaakEMEEKISN-----LKEHLASKEVEVAK----------LEKQLLEEKAAMTDAMVPR 778
Cdd:TIGR02169 592 ILSEDGV-IGFAVDLV--------EFDPKYEPafkyvFGDTLVVEDIEAARrlmgkyrmvtLEGELFEKSGAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 779 SSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM 858
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 224809476 859 KRYAES-SSKLEEDK------DKKINEMSKEVTKLKEALN 891
Cdd:TIGR02169 743 EEDLSSlEQEIENVKselkelEARIEELEEDLHKLEEALN 782
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
113-164 |
7.97e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 7.97e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 224809476 113 TALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLL 164
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-891 |
9.56e-11 |
|
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: 66.23 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLksqmtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKEL---------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 659 SLEDVTAEyihkaEHEKLMQLTNVSRAKAEDALSEMKSqyskvlnELTQLKQLVDAQKENSVSITEHLQ----VITTLRT 734
Cdd:TIGR02168 750 AQLSKELT-----ELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelraELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvprSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVV 814
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 815 QIRS--------------EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEM 879
Cdd:TIGR02168 891 LLRSeleelseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970
|
330
....*....|..
gi 224809476 880 SKEVTKLKEALN 891
Cdd:TIGR02168 971 RRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-774 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQ------LQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKevlsvq 495
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA------ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 496 kqmklglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSY 575
Cdd:COG1196 261 --------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------IARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 576 CSVIENMNKEKAFLFEKYQEAQEEIMKLkdtlksqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyR 655
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-L 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 656 KRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA 735
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350
....*....|....*....|....*....|....*....
gi 224809476 736 AKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA 774
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
620-856 |
1.38e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.42 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 620 EDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEyihkaeheklMQLTNVSRAKAEDALSEMKSQYS 699
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----------AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 700 KVLNELTQLKQLVDAQKENSVSITEHlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvpRS 779
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 780 SYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI---RSEVSQVKREKENIQTLLkskeqevNELLQKFQQAQEELA 856
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-------ESLLQRLEEARLAEA 382
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
80-215 |
2.64e-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: 64.26 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 80 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 149
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 150 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 215
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
3-171 |
2.85e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.53 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 3 AKTNEWNKNDDRLLQAVEN-----GDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK--GHVECLRVMITHGVDVTAQD 75
Cdd:PHA03100 59 ADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 76 TTGHSALHLAAKNSHHEC-IRKLLQSK-----------------CPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPI 137
Cdd:PHA03100 139 SDGENLLHLYLESNKIDLkILKLLIDKgvdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218
|
170 180 190
....*....|....*....|....*....|....
gi 224809476 138 NLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA03100 219 NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
47-98 |
3.96e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 3.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 224809476 47 TAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLL 98
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
420-891 |
4.08e-10 |
|
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: 63.92 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 LglvspesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTViKPPVEEYEEMKSSYCSVI 579
Cdd:TIGR02168 397 S-------------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKS---------QMTQEASDEAEDMKEAMNRMID------------------- 631
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQlqarldsleRLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegye 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 632 ---------ELNKQVSELSQLYKEAQAELEDYRKRKS----LEDVTAEYIHKAEHEKLMQLTNVSRAKAEdaLSEMKSQY 698
Cdd:TIGR02168 537 aaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 699 SKVLN----------------------------------------------------------ELTQLKQLVDAQKEnsv 720
Cdd:TIGR02168 615 RKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEE--- 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 721 SITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK 800
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 801 ESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 880
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570
....*....|.
gi 224809476 881 KEVTKLKEALN 891
Cdd:TIGR02168 852 EDIESLAAEIE 862
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
431-890 |
5.19e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 431 QDLQKRLESSEAERKQLQVELQSRRAElvCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDN 510
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 511 YSHFHELRVTEEEINV--------LKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENM 582
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKAdaakkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 583 N----KEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAE----- 650
Cdd:PTZ00121 1445 KadeaKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakka 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 651 -----LEDYRK----RKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKVLN--ELTQLKQLVDAQKEN 718
Cdd:PTZ00121 1525 deakkAEEAKKadeaKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEE 1604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 719 SVSITEHLQVITTLRTAAKEM--EEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 795 LASKLK-ESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllksKEQEVNELlqKFQQAQEELAEMKRYAESSSKLEEDKd 873
Cdd:PTZ00121 1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEELK-----KAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEK- 1756
|
490
....*....|....*..
gi 224809476 874 KKINEMSKEVTKLKEAL 890
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEI 1773
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-891 |
9.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMklg 501
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 lvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVIEN 581
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---------EALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL- 660
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLa 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 661 ---------EDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT 731
Cdd:COG1196 524 gavavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 732 LRTAAKEMEEKISNLKEHLASKEVEVA----------KLEKQLLEEKAAMTDAMVPRSSYE----KLQSSLESEVSVLAS 797
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAArleaalrravTLAGRLREVTLEGEGGSAGGSLTGgsrrELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 798 KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKIN 877
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
490
....*....|....
gi 224809476 878 EMSKEVTKLKEALN 891
Cdd:COG1196 764 ELERELERLEREIE 777
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
56-230 |
1.44e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 56 GHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIrKLLQSKCPAESVDSSG-KTALHYAAAQGCLQAVQILCEHK 134
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAI-KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 135 SPINlkDL---DGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY 211
Cdd:PHA02875 92 KFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170
....*....|....*....
gi 224809476 212 NALHYSKLSENAGIQSLLL 230
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLL 188
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
147-197 |
2.92e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 224809476 147 PLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALI 197
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-891 |
3.13e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 528 KQDLQNALEESERNKEKV----RELEEKLVEREKGTVIkppVEEYEEMKSsycsviENMNKEKAFLFEKYQEAQEEIMKL 603
Cdd:TIGR02168 174 RKETERKLERTRENLDRLedilNELERQLKSLERQAEK---AERYKELKA------ELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 604 KDTLKSQMTQEASDEAE-DMKEAMnrmIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEHEKlmqltnv 682
Cdd:TIGR02168 245 QEELKEAEEELEELTAElQELEEK---LEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 683 srakaedalsemksqysKVLNEltQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK 762
Cdd:TIGR02168 305 -----------------QILRE--RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 763 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKEN-----IQTLLKSK 837
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEEL 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 224809476 838 EQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
163-216 |
3.55e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.50 E-value: 3.55e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 224809476 163 LLDHG-ADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHY 216
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
26-184 |
3.66e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.28 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 26 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPA 104
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 105 ESVDSSGKTALHYAAAQgCL--QAVQILCEHKSPINLKD-LDGNIPLLLAVqngHSE-ICHFLLDHGADVNSRNKSGRTA 180
Cdd:PHA02878 228 DARDKCGNTPLHISVGY-CKdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTP 303
|
....
gi 224809476 181 LMLA 184
Cdd:PHA02878 304 LSSA 307
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
517-891 |
5.10e-09 |
|
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: 59.87 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVTAEYihkae 672
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEELKEGY----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLKE 748
Cdd:pfam06160 221 REMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIED 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 749 HLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEVS 821
Cdd:pfam06160 299 YLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQLE 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224809476 822 QVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:pfam06160 375 EIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
78-130 |
1.14e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 224809476 78 GHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQIL 130
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
416-891 |
1.17e-08 |
|
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: 58.88 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 416 TTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLS 493
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 494 VQKQMK--------------------------LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 547
Cdd:TIGR04523 108 INSEIKndkeqknklevelnklekqkkenkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 548 LEEKL-VEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ--EASDEAEDMKE 624
Cdd:TIGR04523 188 NIDKIkNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 625 AMNRMIDEL---NKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV 701
Cdd:TIGR04523 268 QLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 702 LNELTQL---------------KQLVDAQKENSvsitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:TIGR04523 348 KKELTNSesensekqreleekqNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 767 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 224809476 847 KFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
11-188 |
2.48e-08 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 58.17 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 11 NDDRLLQAVENGDAEKVASLLGKKGASAtkhdSEGKTAFHlAAAKGHV----ECLRVMITHGVD------VTAQDTT--- 77
Cdd:TIGR00870 52 GRSALFVAAIENENLELTELLLNLSCRG----AVGDTLLH-AISLEYVdaveAILLHLLAAFRKsgplelANDQYTSeft 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 78 -GHSALHLAAKNSHHECIRKLLQSK-------CPAESVDSSGKTALHY-------AAAQGCLQAVQILCEHKSPINLKDL 142
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADS 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809476 143 DGNIPL-LLAVQNGHSE-----ICH---FLLDHGADVNS-------RNKSGRTALMLACEIG 188
Cdd:TIGR00870 207 LGNTLLhLLVMENEFKAeyeelSCQmynFALSLLDKLRDskeleviLNHQGLTPLKLAAKEG 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-697 |
2.68e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEIsenssDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 495 QKQMKLGLVSPESMDNY---------SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE--------REK 557
Cdd:TIGR02168 746 EERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 558 GTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKS-----QMTQEASDEAEDMKEAMNRMIDE 632
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224809476 633 LNKQVSELSQLYKEAQAELEDYRKRKS---------LEDVTAEYIHKAE-HEKLMQLTNVSRAKAEDALSEMKSQ 697
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEglevridnlQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-911 |
5.53e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 LVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSYCSVIEN 581
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSElSQLYKEAQAELEDYRKRK 658
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 659 SLEDvTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA--A 736
Cdd:PTZ00121 1461 EAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 737 KEMEEKiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI 816
Cdd:PTZ00121 1540 KKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 817 RSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinemSKEVTKLKEALNSLSQL 896
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEA 1693
|
490
....*....|....*
gi 224809476 897 SYSTSSSKRQSQQLE 911
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK 1708
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
27-232 |
5.65e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 56.38 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 27 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQS 100
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 101 KCPAESVDSS-GKTALHyaaaqgclqavqilCEHKSPINLKDLDgniplllavqnghseICHFLLDHGADVNSRNKSGRT 179
Cdd:PHA02798 171 GVDINTHNNKeKYDTLH--------------CYFKYNIDRIDAD---------------ILKLFVDNGFIINKENKSHKK 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224809476 180 ALM--LACEIGSSNAVEA----LIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 232
Cdd:PHA02798 222 KFMeyLNSLLYDNKRFKKnildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
181-243 |
6.11e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 6.11e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809476 181 LMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPT 243
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-891 |
7.49e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 304 FKAEISSIRENKDRLSDSTTGADSLLDISSE--ADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHS 381
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 382 tqtdlgpslgkpgetsppdsksspsvLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL 461
Cdd:TIGR02168 387 --------------------------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 462 NNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQ----------KQMKLGLVSPESM-DNYSHFHE-------------- 516
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEqaldaaerelAQLQARLDSLERLqENLEGFSEgvkallknqsglsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 517 --------LRVTEE-EI---NVLKQDLQNALEEserNKEKVRELEEKLVEREKGTVI----------KPPVEEYEEMKSS 574
Cdd:TIGR02168 521 ilgvlselISVDEGyEAaieAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 575 YCSVIENMNKEKA---------------FLFEKYQEAQEEIMKLK----------DTLKSQ--MTQeASDEAEDMKEAMN 627
Cdd:TIGR02168 598 EGFLGVAKDLVKFdpklrkalsyllggvLVVDDLDNALELAKKLRpgyrivtldgDLVRPGgvITG-GSAKTNSSILERR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 628 RMIDELNKQVSELSQLYKEAQAELEDYrkRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlNELTQ 707
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAEL--RKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE-----QLEER 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 708 LKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvprssyeklqss 787
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------- 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 788 LESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSK 867
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
650 660
....*....|....*....|....
gi 224809476 868 LEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELE 918
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
517-891 |
8.92e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.00 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDL----------------YRELRKSL--------LANRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 672
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPD-----QLQEL------KAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 673 HEKLMQ----LTNVsraKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKIS 744
Cdd:PRK04778 239 YRELVEegyhLDHL---DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDqlydILEREVKARKYVEKNSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 745 NLKEHL--ASKEVEVAKLEKQLLEEKAAMTDAMVprSSYEKLQSSLESEVSVLaSKLKESVKEKEKVHSEVV----QIRS 818
Cdd:PRK04778 314 TLPDFLehAKEQNKELKEEIDRVKQSYTLNESEL--ESVRQLEKQLESLEKQY-DEITERIAEQEIAYSELQeeleEILK 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224809476 819 EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS--KLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:PRK04778 391 QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
94-166 |
1.04e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 1.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809476 94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDH 166
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-652 |
1.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 414 KSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteiSENSSDLSQkLKETQSKYEEAmkevls 493
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------KELEARIEE-LEEDLHKLEEA------ 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 494 vqkqmklgLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERnKEKVRELEEKLVEREKGTvIKPPVEEYEEMKS 573
Cdd:TIGR02169 781 --------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224809476 574 SYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
518-888 |
1.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 518 RVTEEEINVLKQ-DLQNALEESERNKEKVRELEEKLVErekgtvIKPPVEEYEEMKSSYCSVIENMNKekafLFEKYQEA 596
Cdd:PRK02224 180 RVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE----VLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 597 QEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrksLEDVTAEYI--HKAEHE 674
Cdd:PRK02224 250 REELETLEAEIED--LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-------LDDADAEAVeaRREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 675 KlmqltnvSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSvsitehlqviTTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PRK02224 321 D-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 755 VEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKE---SVKEKEKVHSEVVQIRSE------------ 819
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 820 ------VSQVKREKENIQTLLKSKEQEVNELLQKFQQAqEELAEMKRYAES-------SSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK02224 464 sphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERleerredLEELIAERRETIEEKRERAEEL 542
|
..
gi 224809476 887 KE 888
Cdd:PRK02224 543 RE 544
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
417-884 |
1.17e-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: 55.89 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 417 TDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVClNNTEISENSSDLSQKLKETQSKYEEAMKEVlsvqk 496
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 497 QMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIkppveeyeemkssyc 576
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI--------------- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 577 sVIENMNKEkaflfekYQEAQEEIMKLKDTLKSqMTQEASDEAEDMKEAMNRMIDELNKqVSELSqlykeAQAELEDYRK 656
Cdd:pfam15921 413 -TIDHLRRE-------LDDRNMEVQRLEALLKA-MKSECQGQMERQMAAIQGKNESLEK-VSSLT-----AQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 657 RKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV-------LNELTQLK----QLVDAQKENS---VSI 722
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKnegdHLRNVQTECEalkLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 723 TEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA------ 796
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvkl 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 797 --------SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEMKRYAES 864
Cdd:pfam15921 638 vnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKS 717
|
490 500
....*....|....*....|
gi 224809476 865 SSKLEEDKDKKINEMSKEVT 884
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQIT 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-890 |
1.18e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 613 QEASDEAEDMKEAMNRMIDELNKQ---VSELSQLYKEAQAELEDYRKRKSledvtaeyIHKAEHEKLMQLTNVSRAK--- 686
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDlss 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 687 AEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHL--QVITTLRTAAKEMEEKISNLKEHLASKEVEVAK--LEK 762
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 763 QLLEEKAA-----MTDAMVPRSSYEKLQSSLESEVSVLASKLKES-------VKEKEKVHSEVVQIRSEVSQVKREKENI 830
Cdd:TIGR02169 829 EYLEKEIQelqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809476 831 QTLLKSKEQEVNELLQKFQQAQEELAEMKR--YAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
523-890 |
1.72e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 523 EINVLKQDLQNALEESERNKEKVRELEEKLVE-----REKGTVIKPPVEEYEEMKSSYcsvienmnKEKAFLFEKYQEAQ 597
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEV--------KELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 598 EEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqaelEDYRKRKSLEDVTAEYIHKAEHE--K 675
Cdd:PRK03918 245 KELESLEGSKRK--LEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRlsR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 676 LMQLTNVSRAKAEDA------LSEMKSQYSKVLNELTQLKQLVDA---------------QKENSVSITEHLQVITTLRT 734
Cdd:PRK03918 319 LEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSY-----EKLQSSLESEVSVLASKLKESVKEKEKV 809
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 810 HSEVVQIRSEVSQVKREKENIQTL--LKSKEQEVNEL-LQKFQQAQEELAEMKRYA---ESSSKLEEDKDKKINEMSKEV 883
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYnLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKL 558
|
....*..
gi 224809476 884 TKLKEAL 890
Cdd:PRK03918 559 AELEKKL 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
422-934 |
1.87e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISEnssdLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSE----LEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 LVSPESMDNyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSSYCSVIE 580
Cdd:TIGR02168 308 RERLANLER-----QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 581 NMNKEKAFLFEKYQEAQEEIMKLKDTLKS------QMTQEASDEAEDMKEAMnrmIDELNKQVSELSQLYKEAQAELEDY 654
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERledrreRLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 655 RKRKSLEDVTAEYIHKAEHEKLMQLTNV-SRAKAEDALSEMKSQYSKVLNELTQ-----------LKQL--VDAQKENSV 720
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvLSELisVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 721 SIT--EHLQ--VITTLRTAAKEmeekISNLKEHLASK-------EVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLE 789
Cdd:TIGR02168 540 EAAlgGRLQavVVENLNAAKKA----IAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 790 SEVSVL----------------ASKLKE-----------------SVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKS 836
Cdd:TIGR02168 616 KALSYLlggvlvvddldnalelAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 837 KEQEVNELLQKFQQAQEELAEMKryaesssKLEEDKDKKINEMSKEVTKL-KEALNSLSQLSYSTSSSKRQSQQLEALQQ 915
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
570
....*....|....*....
gi 224809476 916 QVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEEL 787
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
43-219 |
1.97e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 55.09 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 43 SEGKTAFHLAAAKGHVECLRVMITHG--VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAA 120
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 121 QGCLQAVQILCEHKSPINLKDLD--------------GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS---------- 176
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvd 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224809476 177 ----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKL 219
Cdd:TIGR00870 171 sfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
137-215 |
1.98e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.65 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 137 INLKDLDGNIPLLLAVQNGHS---EICHFLLDHGADVNSRNKSGRTALML----ACEIgssNAVEALIKKGADLNLVDSL 209
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLylynATTL---DVIKLLIKAGADVNAKDKV 116
|
....*.
gi 224809476 210 GYNALH 215
Cdd:PHA03095 117 GRTPLH 122
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
49-217 |
2.50e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS--KCPAESVDSSGKTALHY--------- 117
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 118 ------------------AAAQGCLQA--VQILCEHKSPINLKDLD-GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS 176
Cdd:PHA02878 121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224809476 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-859 |
2.50e-07 |
|
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: 54.64 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 430 LQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQK----------QMK 499
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisqlneqisQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 LGLVSPESmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSYCSVI 579
Cdd:TIGR04523 349 KELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-------------QNQEKLNQQKDEQI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdmKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrKRKS 659
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQ--KQKE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 660 LEDVTAEyihkaeheklmqltnvsrakaedaLSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEM 739
Cdd:TIGR04523 491 LKSKEKE------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK----------IEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 740 EEKISNLKEHLASKEVEVAK--LEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIR 817
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 224809476 818 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK 859
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-889 |
4.87e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 531 LQNALEESERNKEKVRELEekLVEREKGTVIKPPVEEyeemkssycsvienmnKEKAflfEKYQEAQEEIMKLKDTLKSQ 610
Cdd:TIGR02169 172 KEKALEELEEVEENIERLD--LIIDEKRQQLERLRRE----------------REKA---ERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 611 MtqeasdeaedmKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEhEKLMQLTNVSRAKAEDA 690
Cdd:TIGR02169 231 E-----------KEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIE-QLLEELNKKIKDLGEEE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 691 LSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvittlrtaAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaa 770
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERE-----------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEER-- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 771 mtdamvprssyeKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllkskeQEVNELLQKFQQ 850
Cdd:TIGR02169 350 ------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDR 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 224809476 851 AQEEL-----------AEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEA 889
Cdd:TIGR02169 411 LQEELqrlseeladlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
110-221 |
6.02e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.96 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 110 SGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLAC-EIG 188
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCK 246
|
90 100 110
....*....|....*....|....*....|....
gi 224809476 189 SSNAVEALIKKGADLNLVDS-LGYNALHYSKLSE 221
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
35-170 |
6.12e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 53.53 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 35 GASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSH-HECIRKLLQSKCPAESVDSSGKT 113
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLST 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 224809476 114 ALHYAAAQGC-LQAVQILCEHKSPINLKDLDGNIPLLLAVqnGHSEICHFLLDHGADV 170
Cdd:PHA02876 445 PLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
15-75 |
6.74e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 6.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 15 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQD 75
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
124-232 |
7.79e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.91 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 124 LQAVQILCEHKSPINLKDLDGNIPLLLAVQN-----GHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEAL-- 196
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 224809476 197 -IKKGADLNLVDSLGYNALH-YSKLSENAGIQ--SLLLSK 232
Cdd:PHA02798 131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
42-85 |
1.12e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 224809476 42 DSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLA 85
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-112 |
1.22e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 15 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECI 94
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90
....*....|....*...
gi 224809476 95 RKLLQSKCPAESVDSSGK 112
Cdd:PTZ00322 165 QLLSRHSQCHFELGANAK 182
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
143-175 |
1.26e-06 |
|
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: 45.74 E-value: 1.26e-06
10 20 30
....*....|....*....|....*....|....
gi 224809476 143 DGNIPLLLAV-QNGHSEICHFLLDHGADVNSRNK 175
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
11-199 |
2.13e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 11 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-------CLRVMIThgVDVTAQDTTGHSALH 83
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEaavvlmeAAPELVN--EPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 84 LAAKNSHHECIRKLLQSKCPAESVDSSG------KTALHY--------AAAQGCLQAVQILCEHKSPINLKDLDGNIPL- 148
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLh 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 149 LLAVQNGHSEICH---FLLDHGADVNS------RNKSGRTALMLACEIGSSNAVEALIKK 199
Cdd:cd22192 175 ILVLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-891 |
2.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 591 EKYQEAQEEIMKLKDTLKSQMTQ-----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTA 665
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 666 EYIHKAEHEKLMQLTNVsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLqvitTLRTAAKEMEEKISN 745
Cdd:PRK03918 238 EEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 746 LKEHLASKEVEVAKLEKQLLEekaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVhSEVVQIRSEVSQVKR 825
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKE------------------LEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 826 EKENIQTLLKSKE-QEVNELLQKFQQAQEELAEmkryaesssKLEEDKDkKINEMSKEVTKLKEALN 891
Cdd:PRK03918 373 ELERLKKRLTGLTpEKLEKELEELEKAKEEIEE---------EISKITA-RIGELKKEIKELKKAIE 429
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
516-888 |
2.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSyCSV----IENMNKEKAFLFE 591
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---------EERDDLLAE-AGLddadAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 592 KYQEAQEEIMKlkdtlKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS-LEDVTAEYihk 670
Cdd:PRK02224 322 RDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeIEELEEEI--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 671 AEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL--------------KQLVDAQK----ENSVSITEHLQVITtl 732
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatlrtarerveeaEALLEAGKcpecGQPVEGSPHVETIE-- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 733 rtaakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAmtdamvprssyeklqSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:PRK02224 472 -----EDRERVEELEAELEDLEEEVEEVEERLERAEDL---------------VEAEDRIERLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLE-----EDKDKKINEMSKEVTKL 886
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERL 611
|
..
gi 224809476 887 KE 888
Cdd:PRK02224 612 RE 613
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-198 |
2.75e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 119 AAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIK 198
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
546-766 |
2.98e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 546 RELEEKLVE----REKGTVIKPPVEE-YEEMKSsyCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAE 620
Cdd:PHA02562 153 RKLVEDLLDisvlSEMDKLNKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 621 DMKEAMNRMIDELNKQVSELSQlYKEAQAELEDYRKRKSLEDVTAEYIHK---------------AEHEKLMQltnvsra 685
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDRIT------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 686 KAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITE-------HLQVITTLRTAAKEMEEKISNLKEHLASKEVEVA 758
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
....*...
gi 224809476 759 KLEKQLLE 766
Cdd:PHA02562 383 KLQDELDK 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
515-870 |
3.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 515 HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKA------F 588
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleelrE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 589 LFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 669 HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlvdaqkensVSITEHLQVITTLRTAAKEMEEKISNLKE 748
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 749 HLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKE 828
Cdd:COG4717 310 LPALEELEEEELEELL-----------------AALGLPPDLSPE-ELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 224809476 829 NIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEE 870
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
425-859 |
3.58e-06 |
|
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: 51.27 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 425 QLQEILQDLQKRLESSEAERKQ-----------------LQVELQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKy 484
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEvqrLEALLKAMKSECQGQMERQMAAIQGK- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 485 EEAMKEVLSVQKQMKlglvSPESMdnyshfheLRVTEEEINVLKQdlqnALEESERNkekVRELEEKLVEREKGtvIKPP 564
Cdd:pfam15921 457 NESLEKVSSLTAQLE----STKEM--------LRKVVEELTAKKM----TLESSERT---VSDLTASLQEKERA--IEAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 565 VEEYEEMKSSY---CSVIENMNKEKAFLfeKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:pfam15921 516 NAEITKLRSRVdlkLQELQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 642 QLYKEA---QAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAED--ALSEMKSQYSKVLNE-------LTQLK 709
Cdd:pfam15921 594 QLEKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEvktsrneLNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 710 QLVDAQKENSVSITEHLQVITT-----LRTAAKEMEEKISNLK-----------------EHLASKEVEVAKLEKQLLEE 767
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNklkmqLKSAQSELEQTRNTLKsmegsdghamkvamgmqKQITAKRGQIDALQSKIQFL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 768 KAAMTDAMVPRSSYEKLQSSLESEVSVLASklkesvkEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQK 847
Cdd:pfam15921 754 EEAMTNANKEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDI 826
|
490
....*....|..
gi 224809476 848 FQQAQEELAEMK 859
Cdd:pfam15921 827 IQRQEQESVRLK 838
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-184 |
4.38e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 4.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 224809476 137 INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
108-151 |
4.83e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 4.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 224809476 108 DSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLA 151
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-934 |
4.90e-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: 50.83 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 741 EKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 820
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREE----------------LEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 821 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNslsqlsYST 900
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE------ELK 350
|
170 180 190
....*....|....*....|....*....|....
gi 224809476 901 SSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETL 384
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
141-251 |
5.14e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 141 DLDGNIPLLLAVqnghsEICHF-----------LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 209
Cdd:PTZ00322 73 VIDPVVAHMLTV-----ELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 224809476 210 GYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQV 251
Cdd:PTZ00322 148 GKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGK 189
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
434-885 |
5.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 434 QKRLESSEAERKQLQVELQSRRAELVclNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLglvspESMDNYSH 513
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 514 FHELRVTEEEINVlkQDLQNAleESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEmkssycsvieNMNKEKAFLFEKY 593
Cdd:PTZ00121 1524 ADEAKKAEEAKKA--DEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKAEEAKKA 1589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 594 QEAQ-EEIMKLKDTLKSQMTQEASDEAEDMKEAMN-RMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKA 671
Cdd:PTZ00121 1590 EEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 672 EHEKlmqltnvsRAKAEDALSEMKSQYSKvlneltqlkqlvdaqKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLA 751
Cdd:PTZ00121 1670 AEED--------KKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 752 SKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQ--SSLESEVSVLASKLKESVKE---KEKVHSEVVQIRSEVSQVKRE 826
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDN 1806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYA-ESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQlEEADAFEKHKFNKNNENGEDGNK 1866
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-909 |
5.21e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVElqsrraelvclnNTEISENSSDLSQKLKEtqskyEEAMKEVLSVQKqmklg 501
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 lVSPESmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEYEEMKSSYCSVIEN 581
Cdd:pfam01576 127 -VTTEA--------KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE------KAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MN--------------KEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdMKEAMNRMIDELNKQVSELSQLyKEA 647
Cdd:pfam01576 192 LEerlkkeekgrqeleKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLEEETAQKNNALKKI-REL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 648 QAELEDYRkrkslEDVTAEYIHKAEHEK----LMQLTNVSRAKAEDALSEMKSQY---SKVLNELTQLKQLVDAQKENsv 720
Cdd:pfam01576 270 EAQISELQ-----EDLESERAARNKAEKqrrdLGEELEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRS-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 721 siteHLQVITTLR----TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA 796
Cdd:pfam01576 343 ----HEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 797 SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS----KLEEDK 872
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLStrlrQLEDER 498
|
490 500 510
....*....|....*....|....*....|....*..
gi 224809476 873 DKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
64-118 |
5.93e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 5.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 224809476 64 MITHG-VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYA 118
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
422-933 |
9.46e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVE-------LQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEV 491
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 492 LSVQKQMKLglvsPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-KEKVRELEEKLVEREKGTVIKPPVEEYEE 570
Cdd:TIGR00618 460 HLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 571 MKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 648
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 649 AELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQv 728
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 729 itTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSVLASKLKESVKEKEK 808
Cdd:TIGR00618 690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKELMH 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 809 VHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE----LAEMKryAESSSKLEEDKDKKINEMSKEVT 884
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthlLKTLE--AEIGQEIPSDEDILNLQCETLVQ 828
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 224809476 885 KLKEALNSLSQLSYSTSSSKRQSQQLEalqqqvkqlqnqlaECKKQHQE 933
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYE--------------ECSKQLAQ 863
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
420-600 |
9.74e-06 |
|
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: 48.00 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISENSSDLSQkLKETQSKYEEAMKEVLSvQKQMK 499
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEE-VEARIKKYEEQLGNVRN-NKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 lglvspesmdnySHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVI 579
Cdd:COG1579 93 ------------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 224809476 580 ENMNKEKAFLFEKYQEAQEEI 600
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-133 |
1.40e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 1 MEAKTNEWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLRVMITHGVDVT 72
Cdd:PTZ00322 37 MAAIQEEIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPN 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 73 AQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEH 133
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
56-228 |
1.42e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 48.72 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 56 GHVECLRVMITHgvDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQ----SKCPAESVDSS-------GKTALHYAAAQ 121
Cdd:cd21882 6 GLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDgvnEAIMLLLEaapdSGNPKELVNAPctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 122 GCLQAVQILCEH--------------KSPINLKDLdGNIPLLLAVQNGHSEICHFLLDHGADVNS---RNKSGRTALMLA 184
Cdd:cd21882 84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVLHAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224809476 185 CEIgSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSL 228
Cdd:cd21882 163 VLQ-ADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGL 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-971 |
1.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 516 ELRVTEEeinVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQE 595
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 596 AQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 675
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 676 lmQLTNVSRAKAEDALSEMKSQYSKvlNELTQLKQLVDAQK-ENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PTZ00121 1343 --KAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 755 vEVAKLEKQLLEEKAAmtdamvprssyEKLQSSLESEVSvlASKLKESVKEKEKVHsevvqirsEVSQVKREKENIQTLL 834
Cdd:PTZ00121 1419 -KADEAKKKAEEKKKA-----------DEAKKKAEEAKK--ADEAKKKAEEAKKAE--------EAKKKAEEAKKADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 835 KSKEQ--EVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEA 912
Cdd:PTZ00121 1477 KKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 913 LQQQVKQLQNQLAECKKQHQE--VISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQK 971
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
143-171 |
1.86e-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: 1.86e-05
10 20
....*....|....*....|....*....
gi 224809476 143 DGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
44-73 |
2.02e-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: 2.02e-05
10 20 30
....*....|....*....|....*....|
gi 224809476 44 EGKTAFHLAAAKGHVECLRVMITHGVDVTA 73
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
542-790 |
2.13e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEmksSYCSVIENMNK--EKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEA 619
Cdd:PRK05771 15 KSYKDEVLEALHELGVVHIEDLKEELSNE---RLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 620 EDMKEAMNRMIDELNKQVSEL----SQLYKEAQA---------ELEDYRKRKSLeDVTAEYIHKAEHEKLMQLTN----- 681
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELeneiKELEQEIERlepwgnfdlDLSLLLGFKYV-SVFVGTVPEDKLEELKLESDvenve 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 682 -VSRAKAED-----ALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEH-----L 750
Cdd:PRK05771 171 yISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKyleelL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 224809476 751 ASKEVEVAKLEKQLLEEKAAMTD------AMVPRSSYEKLQSSLES 790
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKTDktfaieGWVPEDRVKKLKELIDK 296
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
422-665 |
2.46e-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: 47.84 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 LGLVSPESMDNYSHFhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSycsvI 579
Cdd:COG4942 108 ELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------------AELAALRAE----L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEamnrmIDELNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*.
gi 224809476 660 LEDVTA 665
Cdd:COG4942 245 AAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-659 |
4.19e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 335 ADQQDLLSLLQAKVASLtlhNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGpslgkpgetSPPDSKSSPSVLIHSLGK 414
Cdd:TIGR02168 687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 495 QKQMKLGLVSPESMDNyshfhELRVTEEEInvlkQDLQNALEESERNKEKV-RELEEKLVEREKGTV-IKPPVEEYEEMK 572
Cdd:TIGR02168 830 ERRIAATERRLEDLEE-----QIEELSEDI----ESLAAEIEELEELIEELeSELEALLNERASLEEaLALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 573 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLK----------DTLKSQMTQEASDEAEDMKEAMN----------RMIDE 632
Cdd:TIGR02168 901 EE----LRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKR 976
|
330 340
....*....|....*....|....*..
gi 224809476 633 LNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-926 |
4.42e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 620 EDMKEAMNR---MIDELNKQVSELsqlykEAQAEL-EDYRK-RKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEM 694
Cdd:COG1196 182 EATEENLERledILGELERQLEPL-----ERQAEKaERYRElKEELKELEAELLLLKLRELEAEL-----EELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 695 KSQyskvLNELTQLKQLVDAQKEnsvsitehlqvitTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQlleekaamtda 774
Cdd:COG1196 252 EAE----LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 775 mvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE 854
Cdd:COG1196 304 ---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809476 855 LAEMKR-YAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196 381 LEELAEeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
579-812 |
5.97e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrk 658
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 659 sledVTAEYIHKAEHEKLMQLTN-------VSRAkaeDALSEMKSQYSKVLNELTQLKQLVDAQKENSVsitehlQVITT 731
Cdd:COG3883 92 ----ARALYRSGGSVSYLDVLLGsesfsdfLDRL---SALSKIADADADLLEELKADKAELEAKKAELE------AKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 732 LRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHS 811
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
.
gi 224809476 812 E 812
Cdd:COG3883 239 A 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
541-934 |
6.99e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 541 NKEKVRELEEK------LVEREkgtVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyqeaqeEIMKLKDTLKSQMTQE 614
Cdd:PTZ00121 1025 NIEKIEELTEYgnnddvLKEKD---IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDF------DFDAKEDNRADEATEE 1095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 615 ASDEAEDMKEAMNRMIDELNKQvselsqlyKEAQAELEDYRK----RKSLEDVTAEYIHKAEHEKLMQLTNvsraKAEDA 690
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIAR----KAEDA 1163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 691 LSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAA 770
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 771 MTDAMVPRSSYEklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSqvkrekeniqtllKSKEQEVNELLQKFQQ 850
Cdd:PTZ00121 1242 AKKAEEERNNEE--IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-------------KADEAKKAEEKKKADE 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 851 AQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQ 930
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
....
gi 224809476 931 HQEV 934
Cdd:PTZ00121 1387 AEEK 1390
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
614-883 |
7.09e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 614 EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYR-KRKSLEDVTAEYIHKA-EHEKLMQLTNVSRAKAEDAL 691
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAqELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 692 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVI--------TTLRTAAKEME--EKISNLKEHLASKEvEVAKLE 761
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKElvEKIKELEKELEKAK-KALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 762 KQLLEEKAAMTDamvprssyeklqssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV 841
Cdd:COG1340 160 EKLKELRAELKE--------------LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 224809476 842 NELLQKFQQAQEELAEM----KRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1340 226 DELHEEIIELQKELRELrkelKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
651-891 |
7.17e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 651 LEDYRKRksledvTAEYIHKaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQK-----ENSVSITEH 725
Cdd:PRK05771 14 LKSYKDE------VLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 726 LQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprsSYEKLQSSLESE-----VSVLASKLK 800
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----------PWGNFDLDLSLLlgfkyVSVFVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 801 ESVKEKEKVHSEVvqirsEVSQVKREKENIQTL----LKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEdkdkKI 876
Cdd:PRK05771 154 EDKLEELKLESDV-----ENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKE----EL 224
|
250
....*....|....*
gi 224809476 877 NEMSKEVTKLKEALN 891
Cdd:PRK05771 225 EEIEKERESLLEELK 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-862 |
7.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 413 GKSTTDNDVRIQQLQEILqdlqKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLK--ETQSKYEEAMKE 490
Cdd:COG4717 63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEEL-----EELEAELEELREELEklEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 491 VLSVQKQMKlglvspesmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTvIKPPVEEYEE 570
Cdd:COG4717 134 LEALEAELA---------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 571 MKSSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA- 649
Cdd:COG4717 204 LQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 650 ----------ELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtNVSRAKAEDALSEM--KSQYSKVLNELTQLKQLVD--AQ 715
Cdd:COG4717 280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPDlsPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 716 KENSVSITEHLQVITTLRTAAK----EMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSsyeklQSSLESE 791
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809476 792 VSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKrekeniqtllksKEQEVNELLQKFQQAQEELAEM-KRYA 862
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKAELRELaEEWA 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
423-860 |
8.71e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 499
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 LGLVSPESMDNYSHF---HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEyeemkssyc 576
Cdd:TIGR00606 666 SQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ--------- 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 577 SVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 653 DYRKRKSLEDVTAEYIHKAEH-----------EKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVS 721
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHEldtvvskielnRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 722 ITEHLQVI-----------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAM-VPRSSYEKLQSSLE 789
Cdd:TIGR00606 897 VQSLIREIkdakeqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnKIQDGKDDYLKQKE 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 790 SEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------------------SQVKREKENIQTLLKS-KEQEVNELLQKF 848
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqerwlqdnltlrkreNELKEVEEELKQHLKEmGQMQVLQMKQEH 1056
|
490
....*....|..
gi 224809476 849 QQAQEELAEMKR 860
Cdd:TIGR00606 1057 QKLEENIDLIKR 1068
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
177-204 |
8.80e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.32 E-value: 8.80e-05
10 20
....*....|....*....|....*...
gi 224809476 177 GRTALMLACEIGSSNAVEALIKKGADLN 204
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
426-872 |
1.01e-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: 46.25 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvsp 505
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM--TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 506 esmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEE---KLVEREKGTVIKPPVEEYEEMKSSYCSVIEN- 581
Cdd:pfam05483 433 ----------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIELTAHCDKLLLENk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 -MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQeasdeAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrKSL 660
Cdd:pfam05483 503 eLTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 661 EDVTAEYIHKAEHEKLMQLTnvsrakaEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT--------L 732
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIkvnkleleL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 733 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESV-KEKEKVHS 811
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdKIIEERDS 725
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 812 EVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDK 872
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
422-717 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVclnNTEISENS-----SDLSQKLKETQSK---YEEAMKEVLS 493
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSlksqlADYQQALDVQQTRaiqYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 494 VQKQMKLGLVSPESMDNYshFHELRVTEEEIN----VLKQDLQNAlEESERNKEKVRELEEKL---VEREK-GTVIKPPV 565
Cdd:COG3096 425 ARALCGLPDLTPENAEDY--LAAFRAKEQQATeevlELEQKLSVA-DAARRQFEKAYELVCKIageVERSQaWQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 566 EEYeemkSSYCSVIENMNKEKAFLFEKYQ--EAQEEIMKLKDTLKSQMTQE--ASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:COG3096 502 RRY----RSQQALAQRLQQLRAQLAELEQrlRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAV 577
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224809476 642 QLYKEAQAELEDYR-KRKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKvLNELTQLKQLVDAQKE 717
Cdd:COG3096 578 EQRSELRQQLEQLRaRIKELAARAPAWLAAQDAlERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
687-859 |
1.32e-04 |
|
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: 45.05 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 687 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 767 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 840
Cdd:cd22656 161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233
|
170
....*....|....*....
gi 224809476 841 VNELLQKFQQAQEELAEMK 859
Cdd:cd22656 234 LDNLLALIGPAIPALEKLQ 252
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
15-65 |
1.35e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 224809476 15 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMI 65
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
44-75 |
1.40e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|...
gi 224809476 44 EGKTAFHLAAAK-GHVECLRVMITHGVDVTAQD 75
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
458-690 |
1.43e-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: 45.14 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 458 LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNyshfhELRVTEEEINVLKQDLQNALEE 537
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 538 SERNKEKVRELEEKLVEReKGTVIKPPVEEYEEMKSSYCSVI---ENMNK--EKAFLFEKYQEA-QEEIMKLKDTLKSQM 611
Cdd:COG4942 85 LAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLlspEDFLDavRRLQYLKYLAPArREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224809476 612 TQEAsdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDA 690
Cdd:COG4942 164 ALRA--ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
633-891 |
1.85e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 633 LNKQVSE-LSQLYKEAQAELEDYRKRKSledvtAEYIHKAEHEklmqltnvsRAKAEDALSEMKSqYSKVLNELTQLKQL 711
Cdd:PRK05771 14 LKSYKDEvLEALHELGVVHIEDLKEELS-----NERLRKLRSL---------LTKLSEALDKLRS-YLPKLNPLREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 712 VDAQKENSV--SITEHLQVIttlRTAAKEMEEKISNLKEHLASKEVEVAKLE---------KQLLEEK-AAMTDAMVPRS 779
Cdd:PRK05771 79 VSVKSLEELikDVEEELEKI---EKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlSLLLGFKyVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 780 SYEKLQSSLESEVSVLASKLKESV-------KEKEKVHSEVV---------------------QIRSEVSQVKREKENIQ 831
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELkklgferleleeegtpselirEIKEELEEIEKERESLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224809476 832 TLLKSKEQEVNELLqkfQQAQEELAEMKRYAESSSKLEEDKDKKINE---MSKEVTKLKEALN 891
Cdd:PRK05771 236 EELKELAKKYLEEL---LALYEYLEIELERAEALSKFLKTDKTFAIEgwvPEDRVKKLKELID 295
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
177-207 |
1.88e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|..
gi 224809476 177 GRTALMLACEI-GSSNAVEALIKKGADLNLVD 207
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
163-216 |
2.36e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.63 E-value: 2.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 163 LLDHGADVNSRNKSGRTAL--MLACEIG-SSNAVEALIKKGADLNLVDSLGYNALHY 216
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLhlYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHL 89
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
411-890 |
2.65e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESseaERKQLQVELQSRRAELvclnNTEISENSSDLSQK------LKETQSKY 484
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERQETSAELNQ---LLRTLDDQWKEKRDEL----NGELSAADAAVAKDrseleaLEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 485 EEAMKEVLSvQKQMKLGLVSPEsMDNYSHFHELRVT-----EEEINVLKQDLqnaleeSERNKEKVRELEEKLVEREKGT 559
Cdd:pfam12128 335 LDADIETAA-ADQEQLPSWQSE-LENLEERLKALTGkhqdvTAKYNRRRSKI------KEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 560 VIKPPVEE--YEEMKSSYCSVIENMNKEkaflfekYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNrmIDELNKQV 637
Cdd:pfam12128 407 DRQLAVAEddLQALESELREQLEAGKLE-------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--DERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 638 SELSQLYKE---AQAELEDYRKRKSLEDVTAEYIHKAEHE---KLMQLTNVSRAKAEDALSEMKSQ-------YSKVLN- 703
Cdd:pfam12128 478 EEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEErqsALDELELQLFPQAGTLLHFLRKEapdweqsIGKVISp 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 704 EL---TQLKQLVD----AQKENSVSITEHLQVI---------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEE 767
Cdd:pfam12128 558 ELlhrTDLDPEVWdgsvGGELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 768 KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKE-KEKVHSEVVQIRSEVSQVKREkenIQTLLKSKEQEVNELLQ 846
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREART 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 224809476 847 KFQQAQEElaemkryaessskLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam12128 715 EKQAYWQV-------------VEGALDAQLALLKAAIAARRSGA 745
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
512-890 |
2.74e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 512 SHFHELRVTEEEINVLKQDLQnalEESERNKE---KVRELEEKLVEREKGtvikppveeyeemkssycsvienmNKEKAF 588
Cdd:pfam05557 24 EHKRARIELEKKASALKRQLD---RESDRNQElqkRIRLLEKREAEAEEA------------------------LREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 589 LFEKYQEAQEEIMKLKDTLKSQMTqeasdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLA-----DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 669 HK--AEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelTQLKQLVDAQKENSVSITEHLQVITTLRtaakEMEEKISNL 746
Cdd:pfam05557 152 EQlrQNLEKQQSSLAEAEQRIKELEFEIQSQ--------EQDSEIVKNSKSELARIPELEKELERLR----EHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 747 KEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKeKEKVHSEVVQIRSEVSQVKRE 826
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS-PEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224809476 827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
122-206 |
3.61e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.18 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 122 GCLQAVQILCEHKSP-INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKG 200
Cdd:PHA02874 12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
....*.
gi 224809476 201 ADLNLV 206
Cdd:PHA02874 92 VDTSIL 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
418-674 |
3.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNteiSENSSDLSQKLKETQSKYEEAMKEVLSVQKq 497
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR---LAEYSWDEIDVASAEREIAELEAELERLDA- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 498 mklglvspeSMDnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCS 577
Cdd:COG4913 683 ---------SSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---------EELDELQDRLEA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 578 VIENMNKEKAFLFEKYQEAQeeimkLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAEL------ 651
Cdd:COG4913 739 AEDLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLdadles 813
|
250 260
....*....|....*....|....
gi 224809476 652 -EDYRKRksLEDVTAEYIHKAEHE 674
Cdd:COG4913 814 lPEYLAL--LDRLEEDGLPEYEER 835
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
177-205 |
4.85e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 4.85e-04
10 20
....*....|....*....|....*....
gi 224809476 177 GRTALMLACEIGSSNAVEALIKKGADLNL 205
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-858 |
5.55e-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: 43.21 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 613 QEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSledVTAEYIHKAEH-----EKLMQLTNVSRAKA 687
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQelaalEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 688 EDALSEMKSQYSKVLNELTQLKQLVDAQ-KENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLAskevEVAKLEKQLLE 766
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 767 EKaamtdamvprssyeklqsslesevsvlasklkesvKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:COG4942 172 ER-----------------------------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250
....*....|..
gi 224809476 847 KFQQAQEELAEM 858
Cdd:COG4942 217 ELQQEAEELEAL 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
468-860 |
5.64e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 468 ENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSH-FHELRVTEEEINVLKQDLQNALEESERNKEKVR 546
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 547 ELEEKLVEREKGTVIKPP--VEEYEEMKSS---YCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQM------TQEA 615
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDaiKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKS 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 616 SDEAEDMKEAMNRMIDELNKQVSELSQLYKEA--QAELEDYRKRKSLEDVTAEY--IHKAEHEKLMQLTNVSRAK-AEDA 690
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYnkIESARADLEDIKIKINELKdKHDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 691 LSEMKSQY---------SKVLNELTQLKQLVDAQKENSVSITEhlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLE 761
Cdd:PRK01156 548 YEEIKNRYkslkledldSKRTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 762 KQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLAsKLKESVKEKEKVHSEVVQIRSEVSQVKREKENI-------QTLL 834
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTI 704
|
410 420
....*....|....*....|....*.
gi 224809476 835 KSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMKK 730
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
147-171 |
6.92e-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: 38.01 E-value: 6.92e-04
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
132-243 |
7.07e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.12 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 132 EHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSS-----NAVEALIKKGADLNLV 206
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 224809476 207 DSLGYNALHY--SKLSENAGIQSLLLSKISqDADLKTPT 243
Cdd:PHA03100 103 DNNGITPLLYaiSKKSNSYSIVEYLLDNGA-NVNIKNSD 140
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
423-696 |
7.15e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN----------------TEISENSSDLSQKLKETQSKYEE 486
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkelreeaqelrekrDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 487 AMKEVLSVQKQMKLGLVSPESMDnyshfhelrVTEEEINVLKQDLQNA---LEESERNKEKVRELEEKLVEREKGTVIKp 563
Cdd:COG1340 90 LREELDELRKELAELNKAGGSID---------KLRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 564 pvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLksqmtQEASDEAEDMKE---AMNRMIDELNKQVSEL 640
Cdd:COG1340 160 --EKLKELRAELKELRKEAEE----IHKKIKELAEEAQELHEEM-----IELYKEADELRKeadELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 224809476 641 SQLYKEAQAELEDYRKrksledVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKS 696
Cdd:COG1340 229 HEEIIELQKELRELRK------ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
13-76 |
7.43e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.32 E-value: 7.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224809476 13 DRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDT 76
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-891 |
7.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNtEISENSSD----LSQKLKETQSKYEEAMKEVLSVQKQ 497
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDrleqLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 498 MK-LGLVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVR-ELEEKLVERE----KGTVIkPPveEYEE 570
Cdd:COG4913 368 LAaLGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRrELRELEAEIAslerRKSNI-PA--RLLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 571 MKSSYCSVIENMNKEKAFL----------------FEK---------------YQEAQEEI-----------MKLKDTLK 608
Cdd:COG4913 445 LRDALAEALGLDEAELPFVgelievrpeeerwrgaIERvlggfaltllvppehYAAALRWVnrlhlrgrlvyERVRTGLP 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 609 SQMTQEASDE--AEDMKEAMNRMIDELNKQVSELSQLYK-EAQAELEDYRKRksledVTAE---YIHKAEHEKLMQLTNV 682
Cdd:COG4913 525 DPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRA-----ITRAgqvKGNGTRHEKDDRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 683 SR----AKAEDALSEMKSQYSKVLNELTQLKQLVDAqkensvsITEHLQVITTLRTAAKEMEEKISNLKEhLASKEVEVA 758
Cdd:COG4913 600 SRyvlgFDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEID-VASAEREIA 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 759 KLEKQLleekaamtdamvprssyEKLQSSlESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 838
Cdd:COG4913 672 ELEAEL-----------------ERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 224809476 839 QEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKInemSKEVTKLKEALN 891
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLN 783
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
411-655 |
7.82e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQvelqsRRAELVCLNNTE--ISENSSDLSQKLKETQSKYEEAM 488
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAklLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 489 KEVLSVQKQMKLGLVSPESMDNYSHFHELRvteEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppveey 568
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 569 EEMKSSYCSVIENMNKEKAFLfekyQEAQEEIMKLKDTLKSQMTQEASDEAEdmkeamnrmIDELNKQVSELSQLYKEAQ 648
Cdd:COG3206 305 AQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELYESLL 371
|
....*..
gi 224809476 649 AELEDYR 655
Cdd:COG3206 372 QRLEEAR 378
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
605-854 |
8.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 605 DTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDyrKRKSLEDVTAEyihkaeheklMQLTNVSR 684
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEA--LQAEIDKLQAE----------IAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 685 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQkensvSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQL 764
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 765 LEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL 844
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 224809476 845 LQKFQQAQEE 854
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
465-887 |
1.01e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 465 EISENSSDLSQKLKETQSKYEEAM----KEVLSVQKQMKLGLVSPESMdnyshfHELRVTEEEInvlKQDLQNALEESER 540
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 541 NKEKVRELEEKLVEREKGTVikppvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLKSQmtqeasdEAE 620
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQI-----EQLRKMMLSHEGVLQEIRS----ILVDFEEASGKKIYEHDSMSTM-------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 621 DMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSK 700
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 701 VLNELTQLKQlvDAQKENSVsiteHLQVITTLRTAAKEMEekiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSS 780
Cdd:pfam15921 297 IQSQLEIIQE--QARNQNSM----YMRQLSDLESTVSQLR---SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 781 YEKLQSSLESEVSVLASKL----KESVKEKEKVHS----------EVVQIRSEVSQVKREKENIQTLLKSKEQEV----- 841
Cdd:pfam15921 368 FSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECqgqme 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224809476 842 ---------NELLQK--------------FQQAQEELAEMKRYAESSSKLEED-------KDKKINEMSKEVTKLK 887
Cdd:pfam15921 448 rqmaaiqgkNESLEKvssltaqlestkemLRKVVEELTAKKMTLESSERTVSDltaslqeKERAIEATNAEITKLR 523
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
177-230 |
1.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 224809476 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLL 230
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
418-557 |
1.25e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 42.51 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN---TEISENSSDLSQKLK--ETQSKYEEamkEVL 492
Cdd:pfam15066 388 DINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQEryiTEMQQKNKSVSQCLEmdKTLSKKEE---EVE 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 493 SVQkQMKLGL--VSPESMDNYSHFHELRvtEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK 557
Cdd:pfam15066 465 RLQ-QLKGELekATTSALDLLKREKETR--EQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
424-647 |
1.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 424 QQLQEILQDLQKRLESSEAERKQLQvELQSRRAELvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK---- 499
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyn 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 500 --LGLVSPEsmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtviKPPVEEYEEMKSSYCS 577
Cdd:PRK03918 603 eyLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLE 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224809476 578 VIENMNKEKAFLfEKYQEAQEEIMKLKDTLKSQMT--QEASDEAEDMKEAMNRMiDELNKQVSELSQLYKEA 647
Cdd:PRK03918 671 LSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEerEKAKKELEKLEKALERV-EELREKVKKYKALLKER 740
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
591-865 |
1.80e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 591 EKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAM---NRMIDELN--KQVSEL--SQLYKEAQAELEDYRKRKSLEDV 663
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQKFGRSLKakKRFSLLkkETIYLQSAQRVELAERQLQELKI 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 664 TAEyihKAEHEKLMQLTNVSRakaedaLSEMKSQYSKVLNELTQLKqlvdaqkensvsiTEHlqvITTLRTAAKEMEEKI 743
Cdd:COG5022 890 DVK---SISSLKLVNLELESE------IIELKKSLSSDLIENLEFK-------------TEL---IARLKKLLNNIDLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 744 SnlkehlASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK-----------------ESVKEK 806
Cdd:COG5022 945 G------PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkkelaelskqygalqESTKQL 1018
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224809476 807 EKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEvNELLQKFQQAQEELAEMKRYAESS 865
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLRRENS 1076
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
152-222 |
1.87e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.97 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224809476 152 VQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
3-121 |
2.16e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 3 AKTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK-GHVECLRVMITHGVDVTAQDTT-GHS 80
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLT 271
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 224809476 81 ALHLAAKNShhECIRKLLQSKCPAESVDSSGKTALHYAAAQ 121
Cdd:PHA02878 272 ALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
44-71 |
2.91e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 2.91e-03
10 20
....*....|....*....|....*...
gi 224809476 44 EGKTAFHLAAAKGHVECLRVMITHGVDV 71
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
582-860 |
3.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAF-LFEKYQEAQEeIMKLKDTLKSQMTqeasdEAEDMKEAmnrmIDELNKQVSELSQLYKEAqaeLEDYRKRKSL 660
Cdd:COG4913 188 IGSEKALrLLHKTQSFKP-IGDLDDFVREYML-----EEPDTFEA----ADALVEHFDDLERAHEAL---EDAREQIELL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 661 EDVTAEY-------IHKAEHEKLMQLTNVSRAKAEDALSEmksqyskvlNELTQLKQLVDAQKENsvsitehlqvITTLR 733
Cdd:COG4913 255 EPIRELAeryaaarERLAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAE----------LERLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 734 TAAKEMEEKISNLKEHLASKEVE-VAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKEsvkekekvhse 812
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA----------- 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 224809476 813 vvqirsEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:COG4913 385 ------LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
471-699 |
3.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 471 SDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvspesmdnyshfhelrVTEEEINVLKQDLQNALEESERNKEKVRELEE 550
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELE-------------------ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 551 KLVEREkgtvikppvEEYEE-MKSSY------------------------CSVIENMNKEKAFLFEKYQEAQEEIMKLKD 605
Cdd:COG3883 80 EIEERR---------EELGErARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 606 TLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRA 685
Cdd:COG3883 151 ELEAKL-----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|....
gi 224809476 686 KAEDALSEMKSQYS 699
Cdd:COG3883 226 AAAAAAAAAAAAAA 239
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
94-239 |
3.29e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.80 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 94 IRKLLQSKcPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLkdLDGNIPLLLAVQNGHSEICHFLLDHGADVNSR 173
Cdd:PHA02791 14 LKSFLSSK-DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 174 NKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY-NALHYSKLSENAGIQSLLLSKISQDADL 239
Cdd:PHA02791 91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
94-242 |
3.81e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.81 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 172 SRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN------AGIQSLLLSKISQDADLKTP 242
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
702-857 |
3.94e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 702 LNELTQLKQLVDAQKENSVSitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQ----------LLEEKAAM 771
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKE--RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelsasseeLSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 772 TDAmvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 851
Cdd:pfam07888 121 LAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
....*.
gi 224809476 852 QEELAE 857
Cdd:pfam07888 198 RNSLAQ 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-864 |
4.61e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRraelvclnnTEISENSSDLSQKLKETQSKYEEAMKEVlsvqkqmklg 501
Cdd:pfam01576 20 RQQKAESELKELEKKHQQLCEEKNALQEQLQAE---------TELCAEAEEMRARLAARKQELEEILHEL---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 lvspesmdnyshfhELRVTEEEINVlkQDLQNaleESERNKEKVRELEEKLVEREKGTvikppveeyeemkssycsviEN 581
Cdd:pfam01576 81 --------------ESRLEEEEERS--QQLQN---EKKKMQQHIQDLEEQLDEEEAAR--------------------QK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAFLFEKYQEAQEEIMKLKDTlKSQMTQEASDEAEDMKEAMNRMIDELN--KQVSELSQLYKEAQAELEDYRKRKs 659
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKE- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 660 ledvtaeyihkaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAA--- 736
Cdd:pfam01576 200 --------------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkk 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 737 -KEMEEKISNLKEHLASKEVEVAKLEKQ---LLEE----KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKE- 807
Cdd:pfam01576 266 iRELEAQISELQEDLESERAARNKAEKQrrdLGEElealKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEa 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224809476 808 -------KVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEELAEMKRYAES 864
Cdd:pfam01576 346 qlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELqaeLRTLQQAKQDSEHKRKKLEG 412
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
424-909 |
4.88e-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: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 424 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLV 503
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-----------HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 504 spesmdnyshfhelRVTEEEINVlkQDLQNALEESernKEKVRELEEK--LVEREKGTVIKPPVEEYEEMKSSYCSVIEN 581
Cdd:pfam05483 248 --------------QITEKENKM--KDLTFLLEES---RDKANQLEEKtkLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 582 MNKEKAfLFEKYQEAQEEIMKLKDTLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyRKRKSLE 661
Cdd:pfam05483 309 MSTQKA-LEEDLQIATKTICQLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE--KNEDQLK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 662 DVTAEYIHKA-EHEKLMQLTNVSRAKAEDaLSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV-----------I 729
Cdd:pfam05483 381 IITMELQKKSsELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiqL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 730 TTLRTAAKEMEEKISNLKEHLASKEVEVAKL----------EKQLLEEKAAMTDAMVPRS----SYEKLQSSLESEVSVL 795
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 796 ASKLKESVKEKEKVHSEVVQIRSEVS-QVKREKENIQTL----------LKSKEQEVNELLQK-------FQQAQEELAE 857
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIeyevlkkekqMKILENKCNNLKKQienknknIEELHQENKA 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 224809476 858 MKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
409-789 |
5.07e-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: 40.61 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 469
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRELRKTLlanrfsygPAIDELEKQLA-EIEEEFSQFEELTESgdylearevleKLEEE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 470 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALEESERNK 542
Cdd:pfam06160 188 TDALEELmedipplYEELKTELPDQLEELKEGYREME--------EEGY-ALEHLNV-DKEIQQLEEQLEENLALLENLE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 543 -EKVRELEEKLVERekgtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLF---EKYQEAQEEIMKLKDT-LKSQMTQEASD 617
Cdd:pfam06160 258 lDEAEEALEEIEER-----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEhaeEQNKELKEELERVQQSyTLNENELERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 618 EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyiHKAEHEKLMQLTNVSRaKAEDALSEMKsq 697
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ--LEEIEEE--QEEFKESLQSLRKDEL-EAREKLDEFK-- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 698 yskvlNELTQLKQLVdaQKEN----SVSITEHL-QVITTLRTAAKEMEEKISNLKE-----HLASKEVEVAKLEKQLLEE 767
Cdd:pfam06160 406 -----LELREIKRLV--EKSNlpglPESYLDYFfDVSDEIEDLADELNEVPLNMDEvnrllDEAQDDVDTLYEKTEELID 478
|
410 420
....*....|....*....|....*..
gi 224809476 768 KAAMTDAMVP-----RSSYEKLQSSLE 789
Cdd:pfam06160 479 NATLAEQLIQyanryRSSNPEVAEALT 505
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
599-815 |
5.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 599 EIMKLKDTLKSQMTQEASDEAEDMKEAMN------RMIDELNKQVS----------ELSQLYKEAQAELEDYRKRK-SLE 661
Cdd:COG3096 882 QANLLADETLADRLEELREELDAAQEAQAfiqqhgKALAQLEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIfALS 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 662 DVTAEYIHKAEHEKLMQLTNVS----------------RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsiteh 725
Cdd:COG3096 962 EVVQRRPHFSYEDAVGLLGENSdlneklrarleqaeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 726 lqvitTLRTAAKEMEEkisnLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvpRSSYEKLQSSLESEVSVLASKLKESVKE 805
Cdd:COG3096 1034 -----TLQELEQELEE----LGVQADAEAEERARIRRDELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
250
....*....|
gi 224809476 806 KEKVHSEVVQ 815
Cdd:COG3096 1103 YKQEREQVVQ 1112
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
418-840 |
5.49e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 418 DNDVRIQQ---LQEILQDL-QKRLESSEaERKQLQVELQSRRAELvcLNNT-----EISENSSDLSQKLKetqskyeeam 488
Cdd:PTZ00108 967 DENGKIKKysdALDILKEFyLVRLDLYK-KRKEYLLGKLERELAR--LSNKvrfikHVINGELVITNAKK---------- 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 489 KEVLSVQKQMKLGLVSP-ESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-------------KEKVRELEEKLVE 554
Cdd:PTZ00108 1034 KDLVKELKKLGYVRFKDiIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAELEK 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 555 REKgtvikppveEYEEMKSsycSVIENMNKekaflfekyqeaqEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELN 634
Cdd:PTZ00108 1114 KEK---------ELEKLKN---TTPKDMWL-------------EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 635 KQVSELSQLyKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDalsemKSQYSKVLNELTQLKQLVDA 714
Cdd:PTZ00108 1169 LRKPKLKKK-EKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG-----SDQEDDEEQKTKPKKSSVKR 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 715 QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAamTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00108 1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVKKRLEGSLAA 1320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 224809476 795 LASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQE 840
Cdd:PTZ00108 1321 LKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
632-866 |
5.63e-03 |
|
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: 40.61 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 632 ELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHEKLMQLTNVS----RAKAEdalSEMKSQYSKVLNELTQ 707
Cdd:pfam09726 420 ELRSQISSLTSLERSLKSELGQLRQEN---DLLQTKLHNAVSAKQKDKQTVQqlekRLKAE---QEARASAEKQLAEEKK 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 708 LKQLVDAQKENSVS--ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaamtdamvpRSSYEKLQ 785
Cdd:pfam09726 494 RKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE-----------LRKYKESE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 786 SSLESEVSVLaSKLKESVKEKEKVHSEVVQIR----SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRY 861
Cdd:pfam09726 563 KDTEVLMSAL-SAMQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPSTSRI 641
|
....*
gi 224809476 862 AESSS 866
Cdd:pfam09726 642 TPVTP 646
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
542-754 |
6.29e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 39.96 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIEnmnkekaflfekyqeaqeeimkLKDTLKSQMTQEASDEAED 621
Cdd:pfam17060 67 KESFSEMFNGLVGNNFKTVINKIFEDCDGIPASFISALE----------------------LKEDVKSSPRSEADSLGTP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 622 MKEAMNRMI--DELNKQVSELSQLYKEAQAELEDYRKRKSLEDvtaEYIHKAEHEkLMQLTNvsrakaedALSEMKSQYS 699
Cdd:pfam17060 125 IKVDLLRNLkpQESPETPRRINRKYKSLELRVESMKDELEFKD---ETIMEKDRE-LTELTS--------TISKLKDKYD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224809476 700 KVLNELTQLKQLVDAQKENSV-SITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:pfam17060 193 FLSREFEFYKQHHEHGGNNSIkTATKHEFIISELKRKLQEQNRLIRILQEQIQFDP 248
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
426-830 |
6.40e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLN-NTEISENSSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 502 LVSPESMD------NYSHFHELRVT-EEEINVLKQDLQNAL-EESERNKEKVRELEEKL------VEREKGTVIKPPVEE 567
Cdd:COG5022 879 LAERQLQElkidvkSISSLKLVNLElESEIIELKKSLSSDLiENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNK 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 568 YEEMKSSY---CSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ-EASDEAEDMKEAMNRMIDELNKqvseLSQL 643
Cdd:COG5022 959 LHEVESKLketSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQyGALQESTKQLKELPVEVAELQS----ASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 644 YKEAQAELedyRKRKSLEDVTAEYIhKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQL-VDAQKENSVS 721
Cdd:COG5022 1035 ISSESTEL---SILKPLQKLKGLLL-LENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKdLEVTNRNLVK 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 722 ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE-EKAAMTDAMVPRSSYEKLQSSLESE---VSVLAS 797
Cdd:COG5022 1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLElDGLFWEANLEALPSPPPFAALSEKRlyqSALYDE 1190
|
410 420 430
....*....|....*....|....*....|....*..
gi 224809476 798 KLKESVKE----KEKVHSEVVQIRSEVSQVKREKENI 830
Cdd:COG5022 1191 KSKLSSSEvndlKNELIALFSKIFSGWPRGDKLKKLI 1227
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
706-885 |
6.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 706 TQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA----------- 774
Cdd:PHA02562 199 TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskieqfqkvi 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 775 ------------MVPRSSYEKLQSSLESEVSVLA---SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQ 839
Cdd:PHA02562 279 kmyekggvcptcTQQISEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224809476 840 EVNELLQKFQQAQeelAEMKRYAESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PHA02562 359 KAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
516-657 |
7.08e-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: 39.14 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK--GTVIKPpvEEYEEMKSSycsvIENMNKEKAFLFEKY 593
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNN--KEYEALQKE----IESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224809476 594 QEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR 657
Cdd:COG1579 113 LELMERIEELEEELA-----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-860 |
7.18e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgTVIKPPVEEYEEMKSSYCSVI---ENMNKEKAFLFEKY 593
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK--EELRQSREKHEELEEKYKELSassEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 594 QEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL-YKEAQAELEDYRKRKSLEdvtaeyihk 670
Cdd:pfam07888 125 AAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqAKLQQTEEELRSLSKEFQ--------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 671 aeheklmqltnvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHL 750
Cdd:pfam07888 196 ---------------ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 751 AS--------------KEVEVAKLEKQLLEEKAAMTDAmvpRSSYEK----LQSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:pfam07888 261 SSmaaqrdrtqaelhqARLQAAQLTLQLADASLALREG---RARWAQeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 224809476 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEELAEMKR 860
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELkasLRVAQKEKEQLQAEKQ 388
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
36-116 |
7.51e-03 |
|
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: 40.25 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 36 ASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTT-------------GHSALHLAAKNSHHECIRKLLQ-SK 101
Cdd:cd21882 64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLEnGA 143
|
90
....*....|....*..
gi 224809476 102 CPA--ESVDSSGKTALH 116
Cdd:cd21882 144 QPAalEAQDSLGNTVLH 160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
627-806 |
8.70e-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: 39.14 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 627 NRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyihKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelt 706
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKE---IKRLELEIEEVEARIKKYEEQLGNVRNN--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 707 qlKQLVDAQKEnsvsITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvprSSYEKLQS 786
Cdd:COG1579 89 --KEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELE 159
|
170 180
....*....|....*....|
gi 224809476 787 SLESEVSVLASKLKESVKEK 806
Cdd:COG1579 160 ELEAEREELAAKIPPELLAL 179
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
409-653 |
8.93e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELV------CLNNTEISENS-----SDLSQKL 477
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLeltrvnELLKAKFSEDGtqkkmSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 478 KETQSKYEEAMKEVLSVQKQMKLGLvspesmdnyshfhelrvteeeinvlkQDLQNALEESernKEKVRELEEKLVEREK 557
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKL--------------------------QVTQKNLEHS---KGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 558 GTVikppVEEYEEMKssycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQV 637
Cdd:pfam15905 213 EKI----EEKSETEK------LLEYITELSCVSEQVEKYKLDIAQLEELLK-----EKNDEIESLKQSLEEKEQELSKQI 277
|
250
....*....|....*.
gi 224809476 638 SELSQLYKEAQAELED 653
Cdd:pfam15905 278 KDLNEKCKLLESEKEE 293
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-757 |
8.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 506 ESMDNYSHFHE-LRVTEEEINVLKQ--DLQNALEESERNKEKVRELEEKLverekgtvikpPVEEYEEMKSSYCSVIENM 582
Cdd:COG4913 232 EHFDDLERAHEaLEDAREQIELLEPirELAERYAAARERLAELEYLRAAL-----------RLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 583 NKEKAFLFEKYQEAQEEIMKLK---DTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA-ELEDYRKRK 658
Cdd:COG4913 301 RAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809476 659 SLEDVTAEYI-HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQlvdaqkeNSVSITEHLQvitTLRTAak 737
Cdd:COG4913 381 EFAALRAEAAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-------RKSNIPARLL---ALRDA-- 448
|
250 260
....*....|....*....|
gi 224809476 738 emeekisnLKEHLASKEVEV 757
Cdd:COG4913 449 --------LAEALGLDEAEL 460
|
|
| |
