|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-248 |
1.53e-48 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 174.37 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVT 80
Cdd:COG0666 35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 81 AQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAV 160
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 161 QNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 240
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
....*...
gi 1034644523 241 ISQDADLK 248
Cdd:COG0666 275 LLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-246 |
1.08e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.28 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVT 80
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 81 AQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAV 160
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 161 QNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 240
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
....*.
gi 1034644523 241 ISQDAD 246
Cdd:COG0666 242 GADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
17-222 |
2.22e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.87 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKN 96
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 97 SHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGA 176
Cdd:COG0666 164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034644523 177 DVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNAL 222
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-240 |
7.79e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 7.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPA 112
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 113 ESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 192
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034644523 193 CEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 240
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
12-189 |
6.11e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSAL 90
Cdd:COG0666 112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 91 HLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHF 170
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
170
....*....|....*....
gi 1034644523 171 LLDHGADVNSRNKSGRTAL 189
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
5.87e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 94.03 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 90 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034644523 170 FLLDHGADVNSRN 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
123-215 |
5.99e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 123 LHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHgADVNSRNKsGRTALMLACEIGSSNAVE 202
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034644523 203 ALIKKGADLNLVD 215
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
8.76e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 8.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 57 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQsKCPAESVDsSGKTALHYAAAQGCLQAVQ 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034644523 137 ILCEHKSPINLKD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
23-239 |
4.43e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.88 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLRVMITHGVDVTAQDTTGHSALHLAAKNS 97
Cdd:PHA03100 39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 98 --HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEHKSPINLKDldgNIPLLLavqnghseichfllD 173
Cdd:PHA03100 118 snSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYLL--------------S 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644523 174 HGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
12-224 |
6.67e-19 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.85 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLRVMITHGVDVTAQDTTGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 88 SALHLAAKNSH--HECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI--LCEHKSPINLKDLDGNIPLLLAVQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFN 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 164 HSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDslgyNALHY 224
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNT 325
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1-182 |
6.98e-19 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 92.24 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 78 DVTAQDTTGHSALHLAAKNSHHECIRKLLQskCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
|
170 180
....*....|....*....|....*
gi 1034644523 158 LAVQNGHSEICHFLLDHGADVNSRN 182
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-240 |
1.24e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 156 LLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKgADLNLVDSlGYNALHYSKLSENAGIQS 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 1034644523 236 LLLSK 240
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-230 |
3.28e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 82.38 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLRVMITHGVDVTAQDTTGHSALH--LAAKNSHHECIRKL 105
Cdd:PHA03095 59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 106 LQSKCPAESVDSSGKTALH-YAAAQGC-LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHS--EICHFLLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAAT 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 182 NKSGRTALMLACEIGSSNA--VEALIKKGADLNLVDSLGYNALHYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-214 |
6.25e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGV---DVTAQDttGHSALHLAAKNSHHECIRKLLQSKCPAES 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 115 VDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|.
gi 1034644523 194 EIGSSNAVEALIKKGADLNLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-110 |
1.08e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHgVDVTAQDtTGHSALHLAAKNSHHECI 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
....*...
gi 1034644523 103 RKLLQSKC 110
Cdd:pfam12796 78 KLLLEKGA 85
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
3-250 |
1.24e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.39 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVD 78
Cdd:PHA02874 15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 79 VTAqdttghsalhLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLL 158
Cdd:PHA02874 94 TSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 159 AVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQsLLL 238
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLI 242
|
250
....*....|....*
gi 1034644523 239 SKIS---QDADLKTP 250
Cdd:PHA02874 243 NNASindQDIDGSTP 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-917 |
8.38e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 480
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 557
Cdd:PRK03918 256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 558 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 637
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 638 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 706
Cdd:PRK03918 382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 707 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 786
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 787 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 865
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 866 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 917
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-865 |
1.46e-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: 75.09 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 495 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 573
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 574 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 651
Cdd:TIGR02168 772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 652 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 731
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 732 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 811
Cdd:TIGR02168 927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 812 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 865
Cdd:TIGR02168 986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-225 |
3.82e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-RVMITHGVDVTAQDTTGHSALHLAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 96 NSHH-ECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI-LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLD 173
Cdd:PHA02876 317 NGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 174 HGADVNSRNKSGRTALMLA-CEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-238 |
2.77e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 70.86 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKC 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 111 PAESVDSSgktaLHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGH-SEICHFLLDHGADVNSRNKSGRTAL 189
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 190 MLACEIG-SSNAVEALIKKGADLNLVDSLGYNALHY-SKLSENAGIQSLLL 238
Cdd:PHA02876 312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQaSTLDRNKDIVITLL 362
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-869 |
3.37e-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: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 564 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 642
Cdd:COG1196 210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 643 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 721
Cdd:COG1196 287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 722 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 801
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644523 802 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 869
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-905 |
3.92e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 480
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 LvspESMDNYShfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSYCSVIEN 560
Cdd:COG1196 308 E---ERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR--KS 638
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 639 LEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ---------LKQLVDAQKENSVSITEHLQVIT 709
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 710 TLRTAAkemEEKISNLKEHLASKEVEVAKLEKQLLEEKAA-------MTDAMVPRSSYEKLQSSLESEVSVLASKLKESV 782
Cdd:COG1196 535 AYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 783 KEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEV 862
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034644523 863 TKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 905
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
43-217 |
4.65e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.22 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 43 GASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 123 LHYAAAQGCLQAVQILCEHKS-------------------------------PINLKDLDGNIPLLLAVQNGHS-EICHF 170
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNhimnkckngftplhnaiihnrsaiellinnaSINDQDIDGSTPLHHAINPPCDiDIIDI 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034644523 171 LLDHGADVNSRNKSGRTALMLACE-IGSSNAVEALIKKGADLNLVDSL 217
Cdd:PHA02874 274 LLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIANAVLIKEADKL 321
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-890 |
1.74e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenssdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 480
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI----------------EELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 LVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSsycsVI 558
Cdd:PRK03918 296 IKLSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKA----KK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 559 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASdEAEDMKEAMNRMIDELNKQVSELsqlyKEAQ-------AELE 631
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEEL----KKAKgkcpvcgRELT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 632 DYRKRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMK-SQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIT- 709
Cdd:PRK03918 447 EEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAe 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 710 ---TLRTAAKEMEEKISNLKEHLASKEV---EVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSsLESEVSVLAS----- 776
Cdd:PRK03918 526 eyeKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLdeLEEELAELLKELEELGFESVEE-LEERLKELEPfyney 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 777 -KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFqqAQEELAEMKRYAESSSKLEEDKDKKI 855
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
490 500 510
....*....|....*....|....*....|....*
gi 1034644523 856 NEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 890
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-870 |
3.12e-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: 67.79 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 402 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGL 481
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI------------EELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 482 VSPESMDnySHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVErekgtvikppveEYEEMKSSYCSVIENM 561
Cdd:TIGR02169 371 AELEEVD--KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 562 NKekafLFEKYQEAQEEIMKLKDTLKS--QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL 639
Cdd:TIGR02169 437 NE----LEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 640 EDVTAEYIhKAEHEKLMQLTNVSRAKA-----------------EDALSEMKSQYSKV----------LNELTQLKQLVD 692
Cdd:TIGR02169 513 EEVLKASI-QGVHGTVAQLGSVGERYAtaievaagnrlnnvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDLS 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 693 AQKENSVsITEHLQVIttlrtaakEMEEKISN-----LKEHLASKEVEVAK----------LEKQLLEEKAAMTDAMVPR 757
Cdd:TIGR02169 592 ILSEDGV-IGFAVDLV--------EFDPKYEPafkyvFGDTLVVEDIEAARrlmgkyrmvtLEGELFEKSGAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 758 SSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM 837
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034644523 838 KRYAES-SSKLEEDK------DKKINEMSKEVTKLKEALN 870
Cdd:TIGR02169 743 EEDLSSlEQEIENVKselkelEARIEELEEDLHKLEEALN 782
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-172 |
7.80e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 7.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 121 TALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLL 172
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-870 |
1.13e-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: 65.85 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 558 IENMNKEKAFLFEKYQEAQEEIMKLKDTLksqmtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRK 637
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKEL---------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 638 SLEDVTAEyihkaEHEKLMQLTNVSRAKAEDALSEMKSqyskvlnELTQLKQLVDAQKENSVSITEHLQ----VITTLRT 713
Cdd:TIGR02168 750 AQLSKELT-----ELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelraELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 714 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvprSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVV 793
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 794 QIRS--------------EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEM 858
Cdd:TIGR02168 891 LLRSeleelseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970
|
330
....*....|..
gi 1034644523 859 SKEVTKLKEALN 870
Cdd:TIGR02168 971 RRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-753 |
1.18e-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: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQ------LQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKevlsvq 474
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA------ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 475 kqmklglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSY 554
Cdd:COG1196 261 --------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------IARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 555 CSVIENMNKEKAFLFEKYQEAQEEIMKLkdtlksqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyR 634
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-L 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 635 KRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA 714
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034644523 715 AKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA 753
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
599-835 |
1.33e-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: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 599 EDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEyihkaeheklMQLTNVSRAKAEDALSEMKSQYS 678
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----------AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 679 KVLNELTQLKQLVDAQKENSVSITEHlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvpRS 758
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 759 SYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI---RSEVSQVKREKENIQTLLkskeqevNELLQKFQQAQEELA 835
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-------ESLLQRLEEARLAEA 382
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1-179 |
1.54e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.30 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 1 MKSLKAKFRKS-DTNEWNKNDDRLLQAVEN-----GDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK--GHVECLRVM 72
Cdd:PHA03100 48 IDVVKILLDNGaDINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 73 ITHGVDVTAQDTTGHSALHLAAKNSHHEC-IRKLLQSK-----------------CPAESVDSSGKTALHYAAAQGCLQA 134
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKgvdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEF 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034644523 135 VQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 179
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
88-223 |
2.57e-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: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 88 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 158 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 223
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
3.88e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 3.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 55 TAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
399-870 |
5.11e-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: 63.54 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 399 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 478
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 LglvspesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTViKPPVEEYEEMKSSYCSVI 558
Cdd:TIGR02168 397 S-------------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 559 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKS---------QMTQEASDEAEDMKEAMNRMID------------------- 610
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQlqarldsleRLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegye 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 611 ---------ELNKQVSELSQLYKEAQAELEDYRKRKS----LEDVTAEYIHKAEHEKLMQLTNVSRAKAEdaLSEMKSQY 677
Cdd:TIGR02168 537 aaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 678 SKVLN----------------------------------------------------------ELTQLKQLVDAQKEnsv 699
Cdd:TIGR02168 615 RKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEE--- 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 700 SITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK 779
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 780 ESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 859
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570
....*....|.
gi 1034644523 860 KEVTKLKEALN 870
Cdd:TIGR02168 852 EDIESLAAEIE 862
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-869 |
7.31e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 410 QDLQKRLESSEAERKQLQVELQSRRAElvCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDN 489
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 490 YSHFHELRVTEEEINV--------LKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENM 561
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKAdaakkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 562 N----KEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAE----- 629
Cdd:PTZ00121 1445 KadeaKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakka 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 630 -----LEDYRK----RKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKVLN--ELTQLKQLVDAQKEN 697
Cdd:PTZ00121 1525 deakkAEEAKKadeaKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEE 1604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 698 SVSITEHLQVITTLRTAAKEM--EEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSSLESEVSV 773
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 774 LASKLK-ESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllksKEQEVNELlqKFQQAQEELAEMKRYAESSSKLEEDKd 852
Cdd:PTZ00121 1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEELK-----KAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEK- 1756
|
490
....*....|....*..
gi 1034644523 853 KKINEMSKEVTKLKEAL 869
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEI 1773
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-870 |
1.01e-09 |
|
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: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMklg 480
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 lvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVIEN 560
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---------EALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL- 639
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLa 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 640 ---------EDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT 710
Cdd:COG1196 524 gavavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 711 LRTAAKEMEEKISNLKEHLASKEVEVA----------KLEKQLLEEKAAMTDAMVPRSSYE----KLQSSLESEVSVLAS 776
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAArleaalrravTLAGRLREVTLEGEGGSAGGSLTGgsrrELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 777 KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKIN 856
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
490
....*....|....
gi 1034644523 857 EMSKEVTKLKEALN 870
Cdd:COG1196 764 ELERELERLEREIE 777
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
64-238 |
1.52e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 64 GHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIrKLLQSKCPAESVDSSG-KTALHYAAAQGCLQAVQILCEHK 142
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAI-KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 143 SPINlkDL---DGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY 219
Cdd:PHA02875 92 KFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170
....*....|....*....
gi 1034644523 220 NALHYSKLSENAGIQSLLL 238
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLL 188
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
155-205 |
2.85e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.85e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 155 PLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALI 205
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-870 |
3.31e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 507 KQDLQNALEESERNKEKV----RELEEKLVEREKGTVIkppVEEYEEMKSsycsviENMNKEKAFLFEKYQEAQEEIMKL 582
Cdd:TIGR02168 174 RKETERKLERTRENLDRLedilNELERQLKSLERQAEK---AERYKELKA------ELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 583 KDTLKSQMTQEASDEAE-DMKEAMnrmIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEHEKlmqltnv 661
Cdd:TIGR02168 245 QEELKEAEEELEELTAElQELEEK---LEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 662 srakaedalsemksqysKVLNEltQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK 741
Cdd:TIGR02168 305 -----------------QILRE--RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 742 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKEN-----IQTLLKSK 816
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEEL 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 817 EQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 870
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
34-192 |
3.88e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.28 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 113 ESVDSSGKTALHYAAAQgCL--QAVQILCEHKSPINLKD-LDGNIPLLLAVqngHSE-ICHFLLDHGADVNSRNKSGRTA 188
Cdd:PHA02878 228 DARDKCGNTPLHISVGY-CKdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTP 303
|
....
gi 1034644523 189 LMLA 192
Cdd:PHA02878 304 LSSA 307
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-224 |
4.03e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.50 E-value: 4.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 171 LLDHG-ADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHY 224
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
496-870 |
6.31e-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: 59.48 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 496 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 575
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 576 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVTAEYihkae 651
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEELKEGY----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 652 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLKE 727
Cdd:pfam06160 221 REMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIED 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 728 HLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEVS 800
Cdd:pfam06160 299 YLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQLE 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 801 QVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 870
Cdd:pfam06160 375 EIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
1.11e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 86 GHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQIL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
500-870 |
1.98e-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: 58.11 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 500 EEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKSSycsvIENMNKEKAFLFEKYQEAQEEI 579
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLL------SNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 580 MKLKDTLKSQMTQ--EASDEAEDMKEAMNRMIDEL---NKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 654
Cdd:TIGR04523 242 NEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 655 LMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL---------------KQLVDAQKENSvsitEHLQVITTLRTAAKEME 719
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekqreleekqNEIEKLKKENQ----SYKQEIKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 720 EKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 799
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 800 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 870
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
19-196 |
2.76e-08 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 57.78 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 19 NDDRLLQAVENGDAEKVASLLGKKGASAtkhdSEGKTAFHlAAAKGHV----ECLRVMITHGVD------VTAQDTT--- 85
Cdd:TIGR00870 52 GRSALFVAAIENENLELTELLLNLSCRG----AVGDTLLH-AISLEYVdaveAILLHLLAAFRKsgplelANDQYTSeft 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 86 -GHSALHLAAKNSHHECIRKLLQSK-------CPAESVDSSGKTALHY-------AAAQGCLQAVQILCEHKSPINLKDL 150
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADS 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 151 DGNIPL-LLAVQNGHSE-----ICH---FLLDHGADVNS-------RNKSGRTALMLACEIG 196
Cdd:TIGR00870 207 LGNTLLhLLVMENEFKAeyeelSCQmynFALSLLDKLRDskeleviLNHQGLTPLKLAAKEG 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
394-676 |
2.98e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 394 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEIsenssDLSQKLKETQSKYEEAMKEVLSV 473
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 474 QKQMKLGLVSPESMDNY---------SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE--------REK 536
Cdd:TIGR02168 746 EERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 537 GTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKS-----QMTQEASDEAEDMKEAMNRMIDE 611
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 612 LNKQVSELSQLYKEAQAELEDYRKRKS---------LEDVTAEYIHKAE-HEKLMQLTNVSRAKAEDALSEMKSQ 676
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEglevridnlQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
149-281 |
4.13e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.22 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 149 DLDGNIPLLLAVqnghsEICHF-----------LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 217
Cdd:PTZ00322 73 VIDPVVAHMLTV-----ELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 218 GYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQLSDVssPRSITSTPLSGKESVFFAEP 281
Cdd:PTZ00322 148 GKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGK--PPSLEDSPISSHHPDFSAVP 209
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
401-890 |
6.20e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 480
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 LVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSYCSVIEN 560
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MNKEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLyKEAQAELEDYRKRK 637
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 638 SLEDvTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA--A 715
Cdd:PTZ00121 1461 EAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 716 KEMEEKiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI 795
Cdd:PTZ00121 1540 KKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 796 RSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinemSKEVTKLKEALNSLSQL 875
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEA 1693
|
490
....*....|....*
gi 1034644523 876 SYSTSSSKRQSQQLE 890
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK 1708
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
189-251 |
6.91e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.88 E-value: 6.91e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 189 LMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPT 251
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
35-240 |
7.24e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 56.00 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQS 108
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 109 KCPAESVDSS-GKTALHyaaaqgclqavqilCEHKSPINLKDLDgniplllavqnghseICHFLLDHGADVNSRNKSGRT 187
Cdd:PHA02798 171 GVDINTHNNKeKYDTLH--------------CYFKYNIDRIDAD---------------ILKLFVDNGFIINKENKSHKK 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644523 188 ALM--LACEIGSSNAVEA----LIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSK 240
Cdd:PHA02798 222 KFMeyLNSLLYDNKRFKKnildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
51-275 |
8.96e-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: 56.24 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 51 SEGKTAFHLAAAKGHVECLRVMITHG--VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAA 128
Cdd:TIGR00870 15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 129 QGCLQAVQILCEHKSPINLKDLD--------------GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS---------- 184
Cdd:TIGR00870 91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 185 ----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKL-SENA--------GIQSLLLSKISQDADlktpt 251
Cdd:TIGR00870 171 sfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMeNEFKaeyeelscQMYNFALSLLDKLRD----- 245
|
250 260
....*....|....*....|....
gi 1034644523 252 kPKQLSDVSSPRSITSTPLSGKES 275
Cdd:TIGR00870 246 -SKELEVILNHQGLTPLKLAAKEG 268
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
102-174 |
9.30e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 9.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 102 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDH 174
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-870 |
9.31e-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: 56.22 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 283 FKAEISSIRENKDRLSDSTTGADSLLDISSE--ADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHS 360
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 361 tqtdlgpslgkpgetsppdsksspsvLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL 440
Cdd:TIGR02168 387 --------------------------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 441 NNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQ----------KQMKLGLVSPESM-DNYSHFHE-------------- 495
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEqaldaaerelAQLQARLDSLERLqENLEGFSEgvkallknqsglsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 496 --------LRVTEE-EI---NVLKQDLQNALEEserNKEKVRELEEKLVEREKGTVI----------KPPVEEYEEMKSS 553
Cdd:TIGR02168 521 ilgvlselISVDEGyEAaieAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 554 YCSVIENMNKEKA---------------FLFEKYQEAQEEIMKLK----------DTLKSQ--MTQeASDEAEDMKEAMN 606
Cdd:TIGR02168 598 EGFLGVAKDLVKFdpklrkalsyllggvLVVDDLDNALELAKKLRpgyrivtldgDLVRPGgvITG-GSAKTNSSILERR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 607 RMIDELNKQVSELSQLYKEAQAELEDYrkRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlNELTQ 686
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAEL--RKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE-----QLEER 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 687 LKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvprssyeklqss 766
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------- 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 767 LESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSK 846
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
650 660
....*....|....*....|....
gi 1034644523 847 LEEDKDKKINEMSKEVTKLKEALN 870
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELE 918
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
57-271 |
1.07e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.66 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 57 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS--KCPAESVDSSGKTALHY--------- 125
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 126 ------------------AAAQGCLQA--VQILCEHKSPINLKDLD-GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS 184
Cdd:PHA02878 121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 185 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYS----------KLSENAG----IQSLLLSKISQDADLKTP 250
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyckdydilKLLLEHGvdvnAKSYILGLTALHSSIKSE 280
|
250 260
....*....|....*....|....*
gi 1034644523 251 TKPKQL----SDVSSPRSITSTPLS 271
Cdd:PHA02878 281 RKLKLLleygADINSLNSYKLTPLS 305
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
496-870 |
1.09e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.61 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 496 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 575
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDL----------------YRELRKSL--------LANRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 576 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 651
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPD-----QLQEL------KAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 652 HEKLMQ----LTNVsraKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKIS 723
Cdd:PRK04778 239 YRELVEegyhLDHL---DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDqlydILEREVKARKYVEKNSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 724 NLKEHL--ASKEVEVAKLEKQLLEEKAAMTDAMVprSSYEKLQSSLESEVSVLaSKLKESVKEKEKVHSEVV----QIRS 797
Cdd:PRK04778 314 TLPDFLehAKEQNKELKEEIDRVKQSYTLNESEL--ESVRQLEKQLESLEKQY-DEITERIAEQEIAYSELQeeleEILK 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 798 EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS--KLEEDKDKKINEMSKEVTKLKEALN 870
Cdd:PRK04778 391 QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
396-863 |
1.12e-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: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 396 TDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVClNNTEISENSSDLSQKLKETQSKYEEAMKEVlsvqk 475
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 476 QMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIkppveeyeemkssyc 555
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI--------------- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 556 sVIENMNKEkaflfekYQEAQEEIMKLKDTLKSqMTQEASDEAEDMKEAMNRMIDELNKqVSELSqlykeAQAELEDYRK 635
Cdd:pfam15921 413 -TIDHLRRE-------LDDRNMEVQRLEALLKA-MKSECQGQMERQMAAIQGKNESLEK-VSSLT-----AQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 636 RKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV-------LNELTQLK----QLVDAQKENS---VSI 701
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKnegdHLRNVQTECEalkLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 702 TEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA------ 775
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvkl 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 776 --------SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEMKRYAES 843
Cdd:pfam15921 638 vnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKS 717
|
490 500
....*....|....*....|
gi 1034644523 844 SSKLEEDKDKKINEMSKEVT 863
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQIT 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
497-867 |
1.13e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 497 RVTEEEINVLKQ-DLQNALEESERNKEKVRELEEKLVErekgtvIKPPVEEYEEMKSSYCSVIENMNKekafLFEKYQEA 575
Cdd:PRK02224 180 RVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE----VLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 576 QEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrksLEDVTAEYI--HKAEHE 653
Cdd:PRK02224 250 REELETLEAEIED--LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-------LDDADAEAVeaRREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 654 KlmqltnvSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSvsitehlqviTTLRTAAKEMEEKISNLKEHLASKE 733
Cdd:PRK02224 321 D-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 734 VEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKE---SVKEKEKVHSEVVQIRSE------------ 798
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 799 ------VSQVKREKENIQTLLKSKEQEVNELLQKFQQAqEELAEMKRYAES-------SSKLEEDKDKKINEMSKEVTKL 865
Cdd:PRK02224 464 sphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERleerredLEELIAERRETIEEKRERAEEL 542
|
..
gi 1034644523 866 KE 867
Cdd:PRK02224 543 RE 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-631 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 393 KSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteiSENSSDLSQKlKETQSKYEEAmkevls 472
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------KELEARIEEL-EEDLHKLEEA------ 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 473 vqkqmklgLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERnKEKVRELEEKLVEREKGTvIKPPVEEYEEMKS 552
Cdd:TIGR02169 781 --------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644523 553 SYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 631
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
592-869 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 592 QEASDEAEDMKEAMNRMIDELNKQ---VSELSQLYKEAQAELEDYRKRKSledvtaeyIHKAEHEKLMQLTNVSRAK--- 665
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDlss 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 666 AEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHL--QVITTLRTAAKEMEEKISNLKEHLASKEVEVAK--LEK 741
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 742 QLLEEKAA-----MTDAMVPRSSYEKLQSSLESEVSVLASKLKES-------VKEKEKVHSEVVQIRSEVSQVKREKENI 809
Cdd:TIGR02169 829 EYLEKEIQelqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 810 QTLLKSKEQEVNELLQKFQQAQEELAEMKR--YAESSSKLEEDKDKKINEMSKEVTKLKEAL 869
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
145-223 |
1.92e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 54.65 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 145 INLKDLDGNIPLLLAVQNGHS---EICHFLLDHGADVNSRNKSGRTALML----ACEIgssNAVEALIKKGADLNLVDSL 217
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLylynATTL---DVIKLLIKAGADVNAKDKV 116
|
....*.
gi 1034644523 218 GYNALH 223
Cdd:PHA03095 117 GRTPLH 122
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-913 |
2.47e-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: 55.06 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISEnssdLSQKLKETQSKYEEAMKEVLSVQKQMKLG 480
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSE----LEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 LVSPESMDNyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtVIKPPVEEYEEMKSSYCSVIEN 560
Cdd:TIGR02168 308 RERLANLER-----QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA--ELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MNKEKAFLFEKYQE---AQEEIMKLKDTLKS------QMTQEASDEAEDMKEAMnrmIDELNKQVSELSQLYKEAQAELE 631
Cdd:TIGR02168 381 LETLRSKVAQLELQiasLNNEIERLEARLERledrreRLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 632 DYRKRKSLEDVTAEYIHKAEHEKLMQLTNV-SRAKAEDALSEMKSQYSKVLNELTQ-----------LKQL--VDAQKEN 697
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvLSELisVDEGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 698 SVSIT--EHLQ--VITTLRTAAKEmeekISNLKEHLASK-------EVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSS 766
Cdd:TIGR02168 538 AIEAAlgGRLQavVVENLNAAKKA----IAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 767 LESEVSVL----------------ASKLKE-----------------SVKEKEKVHSEVVQIRSEVSQVKREKENIQTLL 813
Cdd:TIGR02168 614 LRKALSYLlggvlvvddldnalelAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 814 KSKEQEVNELLQKFQQAQEELAEMKryaesssKLEEDKDKKINEMSKEVTKL-KEALNSLSQLSYSTSSSKRQSQQLEAL 892
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580
....*....|....*....|.
gi 1034644523 893 QQQVKQLQNQLAECKKQHQEV 913
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEEL 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
502-869 |
3.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 502 EINVLKQDLQNALEESERNKEKVRELEEKLVE-----REKGTVIKPPVEEYEEMKSSYcsvienmnKEKAFLFEKYQEAQ 576
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEV--------KELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 577 EEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqaelEDYRKRKSLEDVTAEYIHKAEHE--K 654
Cdd:PRK03918 245 KELESLEGSKRK--LEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRlsR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 655 LMQLTNVSRAKAEDA------LSEMKSQYSKVLNELTQLKQLVDA---------------QKENSVSITEHLQVITTLRT 713
Cdd:PRK03918 319 LEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 714 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSY-----EKLQSSLESEVSVLASKLKESVKEKEKV 788
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 789 HSEVVQIRSEVSQVKREKENIQTL--LKSKEQEVNEL-LQKFQQAQEELAEMKRYA---ESSSKLEEDKDKKINEMSKEV 862
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYnLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKL 558
|
....*..
gi 1034644523 863 TKLKEAL 869
Cdd:PRK03918 559 AELEKKL 565
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
409-838 |
4.42e-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: 53.87 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 409 LQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQK----------QMK 478
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisqlneqisQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 LGLVSPESmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSYCSVI 558
Cdd:TIGR04523 349 KELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-------------QNQEKLNQQKDEQI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 559 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdmKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrKRKS 638
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQ--KQKE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 639 LEDVTAEyihkaeheklmqltnvsrakaedaLSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEM 718
Cdd:TIGR04523 491 LKSKEKE------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK----------IEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 719 EEKISNLKEHLASKEVEVAK--LEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIR 796
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1034644523 797 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK 838
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1-120 |
4.61e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 68 CLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
510-868 |
5.61e-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: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 510 LQNALEESERNKEKVRELEekLVEREKGTVIKPPVEEyeemkssycsvienmnKEKAflfEKYQEAQEEIMKLKDTLKSQ 589
Cdd:TIGR02169 172 KEKALEELEEVEENIERLD--LIIDEKRQQLERLRRE----------------REKA---ERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 590 MtqeasdeaedmKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEhEKLMQLTNVSRAKAEDA 669
Cdd:TIGR02169 231 E-----------KEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIE-QLLEELNKKIKDLGEEE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 670 LSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvittlrtaAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaa 749
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERE-----------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEER-- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 750 mtdamvprssyeKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllkskeQEVNELLQKFQQ 829
Cdd:TIGR02169 350 ------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDR 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034644523 830 AQEEL-----------AEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEA 868
Cdd:TIGR02169 411 LQEELqrlseeladlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
43-178 |
5.90e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 53.53 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 43 GASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSH-HECIRKLLQSKCPAESVDSSGKT 121
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLST 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644523 122 ALHYAAAQGC-LQAVQILCEHKSPINLKDLDGNIPLLLAVqnGHSEICHFLLDHGADV 178
Cdd:PHA02876 445 PLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-83 |
7.56e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 7.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQD 83
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
132-240 |
9.57e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.53 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 132 LQAVQILCEHKSPINLKDLDGNIPLLLAVQN-----GHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEAL-- 204
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034644523 205 -IKKGADLNLVDSLGYNALH-YSKLSENAGIQ--SLLLSK 240
Cdd:PHA02798 131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-93 |
1.27e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 1.27e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1034644523 50 DSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLA 93
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
151-183 |
1.35e-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: 45.36 E-value: 1.35e-06
10 20 30
....*....|....*....|....*....|....
gi 1034644523 151 DGNIPLLLAV-QNGHSEICHFLLDHGADVNSRNK 183
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
19-207 |
2.08e-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: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-------CLRVMIThgVDVTAQDTTGHSALH 91
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEaavvlmeAAPELVN--EPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 92 LAAKNSHHECIRKLLQSKCPAESVDSSG------KTALHY--------AAAQGCLQAVQILCEHKSPINLKDLDGNIPL- 156
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLh 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 157 LLAVQNGHSEICH---FLLDHGADVNS------RNKSGRTALMLACEIGSSNAVEALIKK 207
Cdd:cd22192 175 ILVLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
495-867 |
2.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 495 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSyCSV----IENMNKEKAFLFE 570
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---------EERDDLLAE-AGLddadAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 571 KYQEAQEEIMKlkdtlKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS-LEDVTAEYihk 649
Cdd:PRK02224 322 RDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeIEELEEEI--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 650 AEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL--------------KQLVDAQK----ENSVSITEHLQVITtl 711
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatlrtarerveeaEALLEAGKcpecGQPVEGSPHVETIE-- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 712 rtaakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAmtdamvprssyeklqSSLESEVSVLASKLKESVKEKEKVHSE 791
Cdd:PRK02224 472 -----EDRERVEELEAELEDLEEEVEEVEERLERAEDL---------------VEAEDRIERLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 792 VVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLE-----EDKDKKINEMSKEVTKL 865
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERL 611
|
..
gi 1034644523 866 KE 867
Cdd:PRK02224 612 RE 613
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
127-206 |
2.55e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 127 AAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIK 206
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
525-745 |
3.33e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 525 RELEEKLVE----REKGTVIKPPVEE-YEEMKSsyCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAE 599
Cdd:PHA02562 153 RKLVEDLLDisvlSEMDKLNKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 600 DMKEAMNRMIDELNKQVSELSQlYKEAQAELEDYRKRKSLEDVTAEYIHK---------------AEHEKLMQltnvsra 664
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDRIT------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 665 KAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITE-------HLQVITTLRTAAKEMEEKISNLKEHLASKEVEVA 737
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
....*...
gi 1034644523 738 KLEKQLLE 745
Cdd:PHA02562 383 KLQDELDK 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
404-838 |
3.51e-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: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 404 QLQEILQDLQKRLESSEAERKQ-----------------LQVELQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKy 463
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEvqrLEALLKAMKSECQGQMERQMAAIQGK- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 464 EEAMKEVLSVQKQMKlglvSPESMdnyshfheLRVTEEEINVLKQdlqnALEESERNkekVRELEEKLVEREKGtvIKPP 543
Cdd:pfam15921 457 NESLEKVSSLTAQLE----STKEM--------LRKVVEELTAKKM----TLESSERT---VSDLTASLQEKERA--IEAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 544 VEEYEEMKSSY---CSVIENMNKEKAFLfeKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELS 620
Cdd:pfam15921 516 NAEITKLRSRVdlkLQELQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 621 QLYKEA---QAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAED--ALSEMKSQYSKVLNE-------LTQLK 688
Cdd:pfam15921 594 QLEKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEvktsrneLNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 689 QLVDAQKENSVSITEHLQVITT-----LRTAAKEMEEKISNLK-----------------EHLASKEVEVAKLEKQLLEE 746
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNklkmqLKSAQSELEQTRNTLKsmegsdghamkvamgmqKQITAKRGQIDALQSKIQFL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 747 KAAMTDAMVPRSSYEKLQSSLESEVSVLASklkesvkEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQK 826
Cdd:pfam15921 754 EEAMTNANKEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDI 826
|
490
....*....|..
gi 1034644523 827 FQQAQEELAEMK 838
Cdd:pfam15921 827 IQRQEQESVRLK 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
570-870 |
3.73e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 570 EKYQEAQEEIMKLKDTLKSQMTQ-----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTA 644
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 645 EYIHKAEHEKLMQLTNVsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLqvitTLRTAAKEMEEKISN 724
Cdd:PRK03918 238 EEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 725 LKEHLASKEVEVAKLEKQLLEekaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVhSEVVQIRSEVSQVKR 804
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKE------------------LEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644523 805 EKENIQTLLKSKE-QEVNELLQKFQQAQEELAEmkryaesssKLEEDKDkKINEMSKEVTKLKEALN 870
Cdd:PRK03918 373 ELERLKKRLTGLTpEKLEKELEELEKAKEEIEE---------EISKITA-RIGELKKEIKELKKAIE 429
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
494-849 |
4.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 494 HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKA------F 567
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleelrE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 568 LFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 647
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 648 HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlvdaqkensVSITEHLQVITTLRTAAKEMEEKISNLKE 727
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 728 HLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKE 807
Cdd:COG4717 310 LPALEELEEEELEELL-----------------AALGLPPDLSPE-ELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034644523 808 NIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEE 849
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
116-159 |
5.01e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 5.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1034644523 116 DSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLA 159
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
5.01e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 5.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034644523 145 INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
720-913 |
5.23e-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: 50.44 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 720 EKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 799
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREE----------------LEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 800 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNslsqlsYST 879
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE------ELK 350
|
170 180 190
....*....|....*....|....*....|....
gi 1034644523 880 SSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEV 913
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETL 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
413-864 |
5.86e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 413 QKRLESSEAERKQLQVELQSRRAELVclNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLglvspESMDNYSH 492
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 493 FHELRVTEEEINVlkQDLQNAleESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEmkssycsvieNMNKEKAFLFEKY 572
Cdd:PTZ00121 1524 ADEAKKAEEAKKA--DEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKAEEAKKA 1589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 573 QEAQ-EEIMKLKDTLKSQMTQEASDEAEDMKEAMN-RMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKA 650
Cdd:PTZ00121 1590 EEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 651 EHEKlmqltnvsRAKAEDALSEMKSQYSKvlneltqlkqlvdaqKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLA 730
Cdd:PTZ00121 1670 AEED--------KKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 731 SKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQ--SSLESEVSVLASKLKESVKE---KEKVHSEVVQIRSEVSQVKRE 805
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDN 1806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 806 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYA-ESSSKLEEDKDKKINEMSKEVTK 864
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQlEEADAFEKHKFNKNNENGEDGNK 1866
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
6.59e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 6.59e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644523 72 MITHG-VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYA 126
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
401-888 |
7.42e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVElqsrraelvclnNTEISENSSDLSQKLKEtqskyEEAMKEVLSVQKqmklg 480
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 lVSPESmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEYEEMKSSYCSVIEN 560
Cdd:pfam01576 127 -VTTEA--------KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE------KAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MN--------------KEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdMKEAMNRMIDELNKQVSELSQLyKEA 626
Cdd:pfam01576 192 LEerlkkeekgrqeleKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLEEETAQKNNALKKI-REL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 627 QAELEDYRkrkslEDVTAEYIHKAEHEK----LMQLTNVSRAKAEDALSEMKSQY---SKVLNELTQLKQLVDAQKENsv 699
Cdd:pfam01576 270 EAQISELQ-----EDLESERAARNKAEKqrrdLGEELEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRS-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 700 siteHLQVITTLR----TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA 775
Cdd:pfam01576 343 ----HEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 776 SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS----KLEEDK 851
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLStrlrQLEDER 498
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034644523 852 DKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 888
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
401-912 |
9.37e-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: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVE-------LQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEV 470
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 471 LSVQKQMKLglvsPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-KEKVRELEEKLVEREKGTVIKPPVEEYEE 549
Cdd:TIGR00618 460 HLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 550 MKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 627
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 628 AELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQv 707
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 708 itTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSVLASKLKESVKEKEK 787
Cdd:TIGR00618 690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKELMH 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 788 VHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE----LAEMKryAESSSKLEEDKDKKINEMSKEVT 863
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthlLKTLE--AEIGQEIPSDEDILNLQCETLVQ 828
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034644523 864 KLKEALNSLSQLSYSTSSSKRQSQQLEalqqqvkqlqnqlaECKKQHQE 912
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYE--------------ECSKQLAQ 863
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
399-579 |
1.15e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 399 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISENSSDLSQkLKETQSKYEEAMKEVLSvQKQMK 478
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEE-VEARIKKYEEQLGNVRN-NKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 LGLvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVI 558
Cdd:COG1579 93 ALQ------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 1034644523 559 ENMNKEKAFLFEKYQEAQEEI 579
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-236 |
1.39e-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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 64 GHVECLRVMITHgvDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQ----SKCPAESVDSS-------GKTALHYAAAQ 129
Cdd:cd21882 6 GLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDgvnEAIMLLLEaapdSGNPKELVNAPctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 130 GCLQAVQILCEH--------------KSPINLKDLdGNIPLLLAVQNGHSEICHFLLDHGADVNS---RNKSGRTALMLA 192
Cdd:cd21882 84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVLHAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034644523 193 CEIgSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSL 236
Cdd:cd21882 163 VLQ-ADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGL 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
495-950 |
1.80e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 495 ELRVTEEeinVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQE 574
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 575 AQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 654
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 655 lmQLTNVSRAKAEDALSEMKSQYSKvlNELTQLKQLVDAQK-ENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 733
Cdd:PTZ00121 1343 --KAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 734 vEVAKLEKQLLEEKAAmtdamvprssyEKLQSSLESEVSvlASKLKESVKEKEKVHsevvqirsEVSQVKREKENIQTLL 813
Cdd:PTZ00121 1419 -KADEAKKKAEEKKKA-----------DEAKKKAEEAKK--ADEAKKKAEEAKKAE--------EAKKKAEEAKKADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 814 KSKEQ--EVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEA 891
Cdd:PTZ00121 1477 KKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 892 LQQQVKQLQNQLAECKKQHQE--VISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQK 950
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
151-179 |
1.95e-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: 1.95e-05
10 20
....*....|....*....|....*....
gi 1034644523 151 DGNIPLLLAVQNGHSEICHFLLDHGADVN 179
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
52-81 |
2.09e-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: 2.09e-05
10 20 30
....*....|....*....|....*....|
gi 1034644523 52 EGKTAFHLAAAKGHVECLRVMITHGVDVTA 81
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
521-769 |
2.73e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 521 KEKVRELEEKLVEREKGTVIKPPVEEYEEmksSYCSVIENMNK--EKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEA 598
Cdd:PRK05771 15 KSYKDEVLEALHELGVVHIEDLKEELSNE---RLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 599 EDMKEAMNRMIDELNKQVSEL----SQLYKEAQA---------ELEDYRKRKSLeDVTAEYIHKAEHEKLMQLTN----- 660
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELeneiKELEQEIERlepwgnfdlDLSLLLGFKYV-SVFVGTVPEDKLEELKLESDvenve 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 661 -VSRAKAED-----ALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEH-----L 729
Cdd:PRK05771 171 yISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKyleelL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034644523 730 ASKEVEVAKLEKQLLEEKAAMTD------AMVPRSSYEKLQSSLES 769
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKTDktfaieGWVPEDRVKKLKELIDK 296
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-644 |
2.73e-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: 47.45 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 478
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 LGLVSPESMDNYSHFhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSycsvI 558
Cdd:COG4942 108 ELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------------AELAALRAE----L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 559 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEamnrmIDELNKQVSELSQLYKEAQAELEDYRKRKS 638
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*.
gi 1034644523 639 LEDVTA 644
Cdd:COG4942 245 AAGFAA 250
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
15-141 |
4.42e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLRVMITHGVDVTAQDTTG 86
Cdd:PTZ00322 43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034644523 87 HSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
599-905 |
4.45e-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: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 599 EDMKEAMNR---MIDELNKQVSELsqlykEAQAEL-EDYRK-RKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEM 673
Cdd:COG1196 182 EATEENLERledILGELERQLEPL-----ERQAEKaERYRElKEELKELEAELLLLKLRELEAEL-----EELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 674 KSQyskvLNELTQLKQLVDAQKEnsvsitehlqvitTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQlleekaamtda 753
Cdd:COG1196 252 EAE----LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 754 mvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE 833
Cdd:COG1196 304 ---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 834 LAEMKR-YAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 905
Cdd:COG1196 381 LEELAEeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
558-791 |
4.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 558 IENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrk 637
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 638 sledVTAEYIHKAEHEKLMQLTN-------VSRAkaeDALSEMKSQYSKVLNELTQLKQLVDAQKENSVsitehlQVITT 710
Cdd:COG3883 92 ----ARALYRSGGSVSYLDVLLGsesfsdfLDRL---SALSKIADADADLLEELKADKAELEAKKAELE------AKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 711 LRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHS 790
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
.
gi 1034644523 791 E 791
Cdd:COG3883 239 A 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-638 |
4.99e-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: 47.36 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 314 ADQQDLLSLLQAKVASLtlhNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGpslgkpgetSPPDSKSSPSVLIHSLGK 393
Cdd:TIGR02168 687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 394 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSV 473
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 474 QKQMKLGLVSPESMDNyshfhELRVTEEEInvlkQDLQNALEESERNKEKV-RELEEKLVEREKGTV-IKPPVEEYEEMK 551
Cdd:TIGR02168 830 ERRIAATERRLEDLEE-----QIEELSEDI----ESLAAEIEELEELIEELeSELEALLNERASLEEaLALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 552 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLK----------DTLKSQMTQEASDEAEDMKEAMN----------RMIDE 611
Cdd:TIGR02168 901 EE----LRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKR 976
|
330 340
....*....|....*....|....*..
gi 1034644523 612 LNKQVSELSQLYKEAQAELEDYRKRKS 638
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
185-212 |
8.61e-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: 8.61e-05
10 20
....*....|....*....|....*...
gi 1034644523 185 GRTALMLACEIGSSNAVEALIKKGADLN 212
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
520-913 |
8.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 520 NKEKVRELEEK------LVEREkgtVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyqeaqeEIMKLKDTLKSQMTQE 593
Cdd:PTZ00121 1025 NIEKIEELTEYgnnddvLKEKD---IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDF------DFDAKEDNRADEATEE 1095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 594 ASDEAEDMKEAMNRMIDELNKQvselsqlyKEAQAELEDYRK----RKSLEDVTAEYIHKAEHEKLMQLTNvsraKAEDA 669
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIAR----KAEDA 1163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 670 LSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAA 749
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 750 MTDAMVPRSSYEKLQssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSqvkrekeniqtllKSKEQEVNELLQKFQQ 829
Cdd:PTZ00121 1242 AKKAEEERNNEEIRK--FEEARMAHFARRQAAIKAEEARKADELKKAEEKK-------------KADEAKKAEEKKKADE 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 830 AQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQ 909
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
....
gi 1034644523 910 HQEV 913
Cdd:PTZ00121 1387 AEEK 1390
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
630-870 |
8.72e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 630 LEDYRKRksledvTAEYIHKaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQK-----ENSVSITEH 704
Cdd:PRK05771 14 LKSYKDE------VLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 705 LQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprsSYEKLQSSLESE-----VSVLASKLK 779
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----------PWGNFDLDLSLLlgfkyVSVFVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 780 ESVKEKEKVHSEVvqirsEVSQVKREKENIQTL----LKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEdkdkKI 855
Cdd:PRK05771 154 EDKLEELKLESDV-----ENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKE----EL 224
|
250
....*....|....*
gi 1034644523 856 NEMSKEVTKLKEALN 870
Cdd:PRK05771 225 EEIEKERESLLEELK 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-841 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 392 GKSTTDNDVRIQQLQEILqdlqKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLK--ETQSKYEEAMKE 469
Cdd:COG4717 63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEEL-----EELEAELEELREELEklEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 470 VLSVQKQMKlglvspesmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTvIKPPVEEYEE 549
Cdd:COG4717 134 LEALEAELA---------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 550 MKSSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA- 628
Cdd:COG4717 204 LQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 629 ----------ELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtNVSRAKAEDALSEM--KSQYSKVLNELTQLKQLVD--AQ 694
Cdd:COG4717 280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPDlsPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 695 KENSVSITEHLQVITTLRTAAK----EMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSsyeklQSSLESE 770
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 771 VSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKrekeniqtllksKEQEVNELLQKFQQAQEELAEM-KRYA 841
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKAELRELaEEWA 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
402-839 |
1.04e-04 |
|
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: 46.19 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 402 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 478
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 LGLVSPESMDNYSHF---HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEyeemkssyc 555
Cdd:TIGR00606 666 SQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ--------- 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 556 SVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 631
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 632 DYRKRKSLEDVTAEYIHKAEH-----------EKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVS 700
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHEldtvvskielnRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 701 ITEHLQVI-----------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAM-VPRSSYEKLQSSLE 768
Cdd:TIGR00606 897 VQSLIREIkdakeqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnKIQDGKDDYLKQKE 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 769 SEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------------------SQVKREKENIQTLLKS-KEQEVNELLQKF 827
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqerwlqdnltlrkreNELKEVEEELKQHLKEmGQMQVLQMKQEH 1056
|
490
....*....|..
gi 1034644523 828 QQAQEELAEMKR 839
Cdd:TIGR00606 1057 QKLEENIDLIKR 1068
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
593-862 |
1.18e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 593 EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYR-KRKSLEDVTAEYIHKA-EHEKLMQLTNVSRAKAEDAL 670
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAqELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 671 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVI--------TTLRTAAKEME--EKISNLKEHLASKEvEVAKLE 740
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKElvEKIKELEKELEKAK-KALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 741 KQLLEEKAAMTDAMVPRSSYEKlqsslesevsvlasKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV 820
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHK--------------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034644523 821 NELLQKFQQAQEELAEM----KRYAESSSKLEEDKDKKINEMSKEV 862
Cdd:COG1340 226 DELHEEIIELQKELRELrkelKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
405-851 |
1.21e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 405 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvsp 484
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM--TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 485 esmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEE---KLVEREKGTVIKPPVEEYEEMKSSYCSVIEN- 560
Cdd:pfam05483 433 ----------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIELTAHCDKLLLENk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 -MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQeasdeAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrKSL 639
Cdd:pfam05483 503 eLTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 640 EDVTAEYIHKAEHEKLMQLTnvsrakaEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT--------L 711
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIkvnkleleL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 712 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESV-KEKEKVHS 790
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdKIIEERDS 725
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 791 EVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDK 851
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
401-696 |
1.29e-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: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVclnNTEISENS-----SDLSQKLKETQSK---YEEAMKEVLS 472
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSlksqlADYQQALDVQQTRaiqYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 473 VQKQMKLGLVSPESMDNYshFHELRVTEEEIN----VLKQDLQNAlEESERNKEKVRELEEKL---VEREK-GTVIKPPV 544
Cdd:COG3096 425 ARALCGLPDLTPENAEDY--LAAFRAKEQQATeevlELEQKLSVA-DAARRQFEKAYELVCKIageVERSQaWQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 545 EEYeemkSSYCSVIENMNKEKAFLFEKYQ--EAQEEIMKLKDTLKSQMTQE--ASDEAEDMKEAMNRMIDELNKQVSELS 620
Cdd:COG3096 502 RRY----RSQQALAQRLQQLRAQLAELEQrlRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAV 577
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034644523 621 QLYKEAQAELEDYR-KRKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKvLNELTQLKQLVDAQKE 696
Cdd:COG3096 578 EQRSELRQQLEQLRaRIKELAARAPAWLAAQDAlERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
23-73 |
1.32e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMI 73
Cdd:pfam13637 5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-83 |
1.47e-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: 1.47e-04
10 20 30
....*....|....*....|....*....|...
gi 1034644523 52 EGKTAFHLAAAK-GHVECLRVMITHGVDVTAQD 83
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-669 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 437 LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNyshfhELRVTEEEINVLKQDLQNALEE 516
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 517 SERNKEKVRELEEKLVEReKGTVIKPPVEEYEEMKSSYCSVI---ENMNK--EKAFLFEKYQEA-QEEIMKLKDTLKSQM 590
Cdd:COG4942 85 LAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLlspEDFLDavRRLQYLKYLAPArREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644523 591 TQEAsdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDA 669
Cdd:COG4942 164 ALRA--ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
666-838 |
1.61e-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: 44.67 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 666 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 745
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 746 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 819
Cdd:cd22656 161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233
|
170
....*....|....*....
gi 1034644523 820 VNELLQKFQQAQEELAEMK 838
Cdd:cd22656 234 LDNLLALIGPAIPALEKLQ 252
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
185-215 |
1.99e-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: 1.99e-04
10 20 30
....*....|....*....|....*....|..
gi 1034644523 185 GRTALMLACEI-GSSNAVEALIKKGADLNLVD 215
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
171-224 |
2.30e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.63 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644523 171 LLDHGADVNSRNKSGRTAL--MLACEIG-SSNAVEALIKKGADLNLVDSLGYNALHY 224
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLhlYLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHL 89
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
612-870 |
2.45e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 612 LNKQVSE-LSQLYKEAQAELEDYRKRKSledvtAEYIHKAEHEklmqltnvsRAKAEDALSEMKSqYSKVLNELTQLKQL 690
Cdd:PRK05771 14 LKSYKDEvLEALHELGVVHIEDLKEELS-----NERLRKLRSL---------LTKLSEALDKLRS-YLPKLNPLREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 691 VDAQKENSV--SITEHLQVIttlRTAAKEMEEKISNLKEHLASKEVEVAKLE---------KQLLEEK-AAMTDAMVPRS 758
Cdd:PRK05771 79 VSVKSLEELikDVEEELEKI---EKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlSLLLGFKyVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 759 SYEKLQSSLESEVSVLASKLKESV-------KEKEKVHSEVV---------------------QIRSEVSQVKREKENIQ 810
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELkklgferleleeegtpselirEIKEELEEIEKERESLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 811 TLLKSKEQEVNELLqkfQQAQEELAEMKRYAESSSKLEEDKDKKINE---MSKEVTKLKEALN 870
Cdd:PRK05771 236 EELKELAKKYLEEL---LALYEYLEIELERAEALSKFLKTDKTFAIEgwvPEDRVKKLKELID 295
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
390-869 |
2.85e-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: 44.83 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 390 SLGKSTTDNDVRIQQLQEILQDLQKRLESseaERKQLQVELQSRRAELvclnNTEISENSSDLSQK------LKETQSKY 463
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERQETSAELNQ---LLRTLDDQWKEKRDEL----NGELSAADAAVAKDrseleaLEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 464 EEAMKEVLSvQKQMKLGLVSPEsMDNYSHFHELRVT-----EEEINVLKQDLqnaleeSERNKEKVRELEEKLVEREKGT 538
Cdd:pfam12128 335 LDADIETAA-ADQEQLPSWQSE-LENLEERLKALTGkhqdvTAKYNRRRSKI------KEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 539 VIKPPVEE--YEEMKSSYCSVIENMNKEkaflfekYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNrmIDELNKQV 616
Cdd:pfam12128 407 DRQLAVAEddLQALESELREQLEAGKLE-------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--DERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 617 SELSQLYKE---AQAELEDYRKRKSLEDVTAEYIHKAEHE---KLMQLTNVSRAKAEDALSEMKSQ-------YSKVLN- 682
Cdd:pfam12128 478 EEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEErqsALDELELQLFPQAGTLLHFLRKEapdweqsIGKVISp 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 683 EL---TQLKQLVD----AQKENSVSITEHLQVI---------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEE 746
Cdd:pfam12128 558 ELlhrTDLDPEVWdgsvGGELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 747 KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKE-KEKVHSEVVQIRSEVSQVKREkenIQTLLKSKEQEVNELLQ 825
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREART 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034644523 826 KFQQAQEElaemkryaessskLEEDKDKKINEMSKEVTKLKEAL 869
Cdd:pfam12128 715 EKQAYWQV-------------VEGALDAQLALLKAAIAARRSGA 745
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
491-869 |
3.00e-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: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 491 SHFHELRVTEEEINVLKQDLQnalEESERNKE---KVRELEEKLVEREKGtvikppveeyeemkssycsvienmNKEKAF 567
Cdd:pfam05557 24 EHKRARIELEKKASALKRQLD---RESDRNQElqkRIRLLEKREAEAEEA------------------------LREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 568 LFEKYQEAQEEIMKLKDTLKSQMTqeasdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 647
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLA-----DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 648 HK--AEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelTQLKQLVDAQKENSVSITEHLQVITTLRtaakEMEEKISNL 725
Cdd:pfam05557 152 EQlrQNLEKQQSSLAEAEQRIKELEFEIQSQ--------EQDSEIVKNSKSELARIPELEKELERLR----EHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 726 KEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKeKEKVHSEVVQIRSEVSQVKRE 805
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS-PEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 806 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 869
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
397-653 |
4.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 397 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNteiSENSSDLSQKLKETQSKYEEAMKEVLSVQKq 476
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR---LAEYSWDEIDVASAEREIAELEAELERLDA- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 477 mklglvspeSMDnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCS 556
Cdd:COG4913 683 ---------SSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---------EELDELQDRLEA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 557 VIENMNKEKAFLFEKYQEAQeeimkLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAEL------ 630
Cdd:COG4913 739 AEDLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLdadles 813
|
250 260
....*....|....*....|....
gi 1034644523 631 -EDYRKRksLEDVTAEYIHKAEHE 653
Cdd:COG4913 814 lPEYLAL--LDRLEEDGLPEYEER 835
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
185-213 |
4.94e-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: 4.94e-04
10 20
....*....|....*....|....*....
gi 1034644523 185 GRTALMLACEIGSSNAVEALIKKGADLNL 213
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-837 |
6.49e-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: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 592 QEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSledVTAEYIHKAEH-----EKLMQLTNVSRAKA 666
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQelaalEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 667 EDALSEMKSQYSKVLNELTQLKQLVDAQ-KENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLAskevEVAKLEKQLLE 745
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 746 EKaamtdamvprssyeklqsslesevsvlasklkesvKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 825
Cdd:COG4942 172 ER-----------------------------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250
....*....|..
gi 1034644523 826 KFQQAQEELAEM 837
Cdd:COG4942 217 ELQQEAEELEAL 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
447-839 |
6.68e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 447 ENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSH-FHELRVTEEEINVLKQDLQNALEESERNKEKVR 525
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 526 ELEEKLVEREKGTVIKPP--VEEYEEMKSS---YCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQM------TQEA 594
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDaiKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKS 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 595 SDEAEDMKEAMNRMIDELNKQVSELSQLYKEA--QAELEDYRKRKSLEDVTAEY--IHKAEHEKLMQLTNVSRAK-AEDA 669
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYnkIESARADLEDIKIKINELKdKHDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 670 LSEMKSQY---------SKVLNELTQLKQLVDAQKENSVSITEhlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLE 740
Cdd:PRK01156 548 YEEIKNRYkslkledldSKRTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 741 KQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLAsKLKESVKEKEKVHSEVVQIRSEVSQVKREKENI-------QTLL 813
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTI 704
|
410 420
....*....|....*....|....*.
gi 1034644523 814 KSKEQEVNELLQKFQQAQEELAEMKR 839
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMKK 730
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
155-179 |
6.77e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.01 E-value: 6.77e-04
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
584-833 |
6.86e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 584 DTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDyrKRKSLEDVTAEyihkaeheklMQLTNVSR 663
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEA--LQAEIDKLQAE----------IAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 664 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQkensvSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQL 743
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 744 LEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL 823
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 1034644523 824 LQKFQQAQEE 833
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
21-84 |
7.24e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.32 E-value: 7.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 21 DRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDT 84
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
390-634 |
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 1034644523 390 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQvelqsRRAELVCLNNTE--ISENSSDLSQKLKETQSKYEEAM 467
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAklLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 468 KEVLSVQKQMKLGLVSPESMDNYSHFHELRvteEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppveey 547
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 548 EEMKSSYCSVIENMNKEKAFLfekyQEAQEEIMKLKDTLKSQMTQEASDEAEdmkeamnrmIDELNKQVSELSQLYKEAQ 627
Cdd:COG3206 305 AQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELYESLL 371
|
....*..
gi 1034644523 628 AELEDYR 634
Cdd:COG3206 372 QRLEEAR 378
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
140-251 |
8.19e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.12 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 140 EHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSS-----NAVEALIKKGADLNLV 214
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034644523 215 DSLGYNALHY--SKLSENAGIQSLLLSKISqDADLKTPT 251
Cdd:PHA03100 103 DNNGITPLLYaiSKKSNSYSIVEYLLDNGA-NVNIKNSD 140
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
444-870 |
9.41e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 444 EISENSSDLSQKLKETQSKYEEAM----KEVLSVQKQMKLGLVSPESMdnyshfHELRVTEEEInvlKQDLQNALEESER 519
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 520 NKEKVRELEEKLVEREKGTVikppvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLKSQmtqeasdEAE 599
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQI-----EQLRKMMLSHEGVLQEIRS----ILVDFEEASGKKIYEHDSMSTM-------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 600 DMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSK 679
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 680 VLNELTQLKQlvDAQKENSVsiteHLQVITTLRTAAKEMEekiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSS 759
Cdd:pfam15921 297 IQSQLEIIQE--QARNQNSM----YMRQLSDLESTVSQLR---SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 760 YEKLQSSLESEVSVLASKL----KESVKEKEKVHS----------EVVQIRSEVSQVKREKENIQTLLKSKEQEV----- 820
Cdd:pfam15921 368 FSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECqgqme 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 821 ---------NELLQK--------------FQQAQEELAEMKRYAESSSKLEED-------KDKKINEMSKEVTKLKEALN 870
Cdd:pfam15921 448 rqmaaiqgkNESLEKvssltaqlestkemLRKVVEELTAKKMTLESSERTVSDltaslqeKERAIEATNAEITKLRSRVD 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
401-870 |
9.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 401 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNtEISENSSD----LSQKLKETQSKYEEAMKEVLSVQKQ 476
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDrleqLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 477 MK-LGLVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVR-ELEEKLVERE----KGTVIkPPveEYEE 549
Cdd:COG4913 368 LAaLGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRrELRELEAEIAslerRKSNI-PA--RLLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 550 MKSSYCSVIENMNKEKAFL----------------FEK---------------YQEAQEEI-----------MKLKDTLK 587
Cdd:COG4913 445 LRDALAEALGLDEAELPFVgelievrpeeerwrgaIERvlggfaltllvppehYAAALRWVnrlhlrgrlvyERVRTGLP 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 588 SQMTQEASDE--AEDMKEAMNRMIDELNKQVSELSQLYK-EAQAELEDYRKRksledVTAE---YIHKAEHEKLMQLTNV 661
Cdd:COG4913 525 DPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRA-----ITRAgqvKGNGTRHEKDDRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 662 SR----AKAEDALSEMKSQYSKVLNELTQLKQLVDAqkensvsITEHLQVITTLRTAAKEMEEKISNLKEhLASKEVEVA 737
Cdd:COG4913 600 SRyvlgFDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEID-VASAEREIA 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 738 KLEKQLleekaamtdamvprssyEKLQSSlESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 817
Cdd:COG4913 672 ELEAEL-----------------ERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034644523 818 QEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKInemSKEVTKLKEALN 870
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLN 783
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
185-238 |
1.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 185 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLL 238
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
671-866 |
1.13e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 671 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAM 750
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 751 TDAMVPRSSYEKLQSSLESevsvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 830
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034644523 831 QEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLK 866
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
397-536 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 397 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN---TEISENSSDLSQKLK--ETQSKYEEamkEVL 471
Cdd:pfam15066 388 DINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQEryiTEMQQKNKSVSQCLEmdKTLSKKEE---EVE 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644523 472 SVQkQMKLGL--VSPESMDNYSHFHELRvtEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK 536
Cdd:pfam15066 465 RLQ-QLKGELekATTSALDLLKREKETR--EQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
402-675 |
1.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 402 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN----------------TEISENSSDLSQKLKETQSKYEE 465
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkelreeaqelrekrDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 466 AMKEVLSVQKQMKLGLVSPESMDnyshfhelrVTEEEINVLKQDLQNA---LEESERNKEKVRELEEKLVEREKGTVIKp 542
Cdd:COG1340 90 LREELDELRKELAELNKAGGSID---------KLRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 543 pvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLksqmtQEASDEAEDMKE---AMNRMIDELNKQVSEL 619
Cdd:COG1340 160 --EKLKELRAELKELRKEAEE----IHKKIKELAEEAQELHEEM-----IELYKEADELRKeadELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644523 620 SQLYKEAQAELEDYRKrksledVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKS 675
Cdd:COG1340 229 HEEIIELQKELRELRK------ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
160-230 |
1.82e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.97 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644523 160 VQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN 230
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
570-844 |
2.01e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 570 EKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAM---NRMIDELN--KQVSEL--SQLYKEAQAELEDYRKRKSLEDV 642
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQKFGRSLKakKRFSLLkkETIYLQSAQRVELAERQLQELKI 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 643 TAEyihKAEHEKLMQLTNVSRakaedaLSEMKSQYSKVLNELTQLKqlvdaqkensvsiTEHlqvITTLRTAAKEMEEKI 722
Cdd:COG5022 890 DVK---SISSLKLVNLELESE------IIELKKSLSSDLIENLEFK-------------TEL---IARLKKLLNNIDLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 723 SnlkehlASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK-----------------ESVKEK 785
Cdd:COG5022 945 G------PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkkelaelskqygalqESTKQL 1018
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644523 786 EKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEvNELLQKFQQAQEELAEMKRYAESS 844
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLRRENS 1076
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-626 |
2.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 403 QQLQEILQDLQKRLESSEAERKQLQvELQSRRAELvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK---- 478
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyn 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 479 --LGLVSPEsmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtviKPPVEEYEEMKSSYCS 556
Cdd:PRK03918 603 eyLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLE 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 557 VIENMNKEKAFLfEKYQEAQEEIMKLKDTLKSQMT--QEASDEAEDMKEAMNRMiDELNKQVSELSQLYKEA 626
Cdd:PRK03918 671 LSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEerEKAKKELEKLEKALERV-EELREKVKKYKALLKER 740
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
450-678 |
2.43e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 450 SDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvspesmdnyshfhelrVTEEEINVLKQDLQNALEESERNKEKVRELEE 529
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELE-------------------ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 530 KLVEREkgtvikppvEEYEE-MKSSY------------------------CSVIENMNKEKAFLFEKYQEAQEEIMKLKD 584
Cdd:COG3883 80 EIEERR---------EELGErARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 585 TLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRA 664
Cdd:COG3883 151 ELEAKL-----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|....
gi 1034644523 665 KAEDALSEMKSQYS 678
Cdd:COG3883 226 AAAAAAAAAAAAAA 239
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
52-79 |
2.84e-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: 2.84e-03
10 20
....*....|....*....|....*...
gi 1034644523 52 EGKTAFHLAAAKGHVECLRVMITHGVDV 79
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
609-839 |
3.15e-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: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 609 IDELNKQVSELSQLYKEAqaeLEDYRKRKSLEDVTAEY-------IHKAEHEKLMQLTNVSRAKAEDALSEmksqyskvl 681
Cdd:COG4913 227 ADALVEHFDDLERAHEAL---EDAREQIELLEPIRELAeryaaarERLAELEYLRAALRLWFAQRRLELLE--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 682 NELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEMEEKISNLKEHLASKEVE-VAKLEKQLLEEKAAMTDAMVPRSSY 760
Cdd:COG4913 295 AELEELRAELARLEAE----------LERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034644523 761 EKLQSSLESEVSVLASKLKEsvkekekvhsevvqirsEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR 839
Cdd:COG4913 365 EALLAALGLPLPASAEEFAA-----------------LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
102-247 |
3.66e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.41 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 102 IRKLLQSKcPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLkdLDGNIPLLLAVQNGHSEICHFLLDHGADVNSR 181
Cdd:PHA02791 14 LKSFLSSK-DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644523 182 NKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY-NALHYSKLSENAGIQSLLLSKISQDADL 247
Cdd:PHA02791 91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
681-836 |
3.87e-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: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 681 LNELTQLKQLVDAQKENSVSitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQ----------LLEEKAAM 750
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKE--RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelsasseeLSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 751 TDAmvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 830
Cdd:pfam07888 121 LAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
....*.
gi 1034644523 831 QEELAE 836
Cdd:pfam07888 198 RNSLAQ 203
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
102-250 |
3.88e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.81 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 102 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVN 179
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034644523 180 SRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN------AGIQSLLLSKISQDADLKTP 250
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
578-794 |
5.51e-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: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 578 EIMKLKDTLKSQMTQEASDEAEDMKEAMN------RMIDELNKQVS----------ELSQLYKEAQAELEDYRKRK-SLE 640
Cdd:COG3096 882 QANLLADETLADRLEELREELDAAQEAQAfiqqhgKALAQLEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIfALS 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 641 DVTAEYIHKAEHEKLMQLTNVS----------------RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsiteh 704
Cdd:COG3096 962 EVVQRRPHFSYEDAVGLLGENSdlneklrarleqaeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 705 lqvitTLRTAAKEMEEkisnLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvpRSSYEKLQSSLESEVSVLASKLKESVKE 784
Cdd:COG3096 1034 -----TLQELEQELEE----LGVQADAEAEERARIRRDELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
250
....*....|
gi 1034644523 785 KEKVHSEVVQ 794
Cdd:COG3096 1103 YKQEREQVVQ 1112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
454-843 |
5.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 454 QKLKETQSKYEEAMKEVLSVQKQ-----MKLGLVSPESMDNYSHFHELRVteeEINVLKQDLQNALEESERNKEKVRELE 528
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQlceekNALQEQLQAETELCAEAEEMRA---RLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 529 EKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTlKSQMTQEASDEAEDMKEAMNRM 608
Cdd:pfam01576 92 QQLQNEKKK--MQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERISEFTSNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 609 IDELN--KQVSELSQLYKEAQAELEDYRKRKsledvtaeyihkaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ 686
Cdd:pfam01576 169 AEEEEkaKSLSKLKNKHEAMISDLEERLKKE---------------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 687 LKQLVDAQKENSVSITEHLQVITTLRTAA----KEMEEKISNLKEHLASKEVEVAKLEKQ---LLEE----KAAMTDAMV 755
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNAlkkiRELEAQISELQEDLESERAARNKAEKQrrdLGEElealKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 756 PRSSYEKLQSSLESEVSVLASKLKESVKEKE--------KVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---L 824
Cdd:pfam01576 314 TTAAQQELRSKREQEVTELKKALEEETRSHEaqlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELqaeL 393
|
410
....*....|....*....
gi 1034644523 825 QKFQQAQEELAEMKRYAES 843
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEG 412
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
611-845 |
5.78e-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: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 611 ELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHEKLMQLTNVS----RAKAEdalSEMKSQYSKVLNELTQ 686
Cdd:pfam09726 420 ELRSQISSLTSLERSLKSELGQLRQEN---DLLQTKLHNAVSAKQKDKQTVQqlekRLKAE---QEARASAEKQLAEEKK 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 687 LKQLVDAQKENSVS--ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaamtdamvpRSSYEKLQ 764
Cdd:pfam09726 494 RKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE-----------LRKYKESE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 765 SSLESEVSVLaSKLKESVKEKEKVHSEVVQIR----SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRY 840
Cdd:pfam09726 563 KDTEVLMSAL-SAMQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPSTSRI 641
|
....*
gi 1034644523 841 AESSS 845
Cdd:pfam09726 642 TPVTP 646
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
397-819 |
6.08e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 397 DNDVRIQQ---LQEILQDL-QKRLESSEaERKQLQVELQSRRAELvcLNNT-----EISENSSDLSQKLKetqskyeeam 467
Cdd:PTZ00108 967 DENGKIKKysdALDILKEFyLVRLDLYK-KRKEYLLGKLERELAR--LSNKvrfikHVINGELVITNAKK---------- 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 468 KEVLSVQKQMKLGLVSP-ESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-------------KEKVRELEEKLVE 533
Cdd:PTZ00108 1034 KDLVKELKKLGYVRFKDiIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAELEK 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 534 REKgtvikppveEYEEMKSsycSVIENMNKekaflfekyqeaqEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELN 613
Cdd:PTZ00108 1114 KEK---------ELEKLKN---TTPKDMWL-------------EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 614 KQVSELSQLyKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDalsemKSQYSKVLNELTQLKQLVDA 693
Cdd:PTZ00108 1169 LRKPKLKKK-EKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG-----SDQEDDEEQKTKPKKSSVKR 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 694 QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAamTDAMVPRSSYEKLQSSLESEVSV 773
Cdd:PTZ00108 1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVKKRLEGSLAA 1320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034644523 774 LASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQE 819
Cdd:PTZ00108 1321 LKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
403-888 |
6.09e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 403 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLV 482
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-----------HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 483 spesmdnyshfhelRVTEEEINVlkQDLQNALEESernKEKVRELEEK--LVEREKGTVIKPPVEEYEEMKSSYCSVIEN 560
Cdd:pfam05483 248 --------------QITEKENKM--KDLTFLLEES---RDKANQLEEKtkLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 561 MNKEKAfLFEKYQEAQEEIMKLKDTLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyRKRKSLE 640
Cdd:pfam05483 309 MSTQKA-LEEDLQIATKTICQLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE--KNEDQLK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 641 DVTAEYIHKA-EHEKLMQLTNVSRAKAEDaLSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV-----------I 708
Cdd:pfam05483 381 IITMELQKKSsELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiqL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 709 TTLRTAAKEMEEKISNLKEHLASKEVEVAKL----------EKQLLEEKAAMTDAMVPRS----SYEKLQSSLESEVSVL 774
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 775 ASKLKESVKEKEKVHSEVVQIRSEVS-QVKREKENIQTL----------LKSKEQEVNELLQK-------FQQAQEELAE 836
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIeyevlkkekqMKILENKCNNLKKQienknknIEELHQENKA 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034644523 837 MKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 888
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
521-733 |
6.24e-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: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 521 KEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIEnmnkekaflfekyqeaqeeimkLKDTLKSQMTQEASDEAED 600
Cdd:pfam17060 67 KESFSEMFNGLVGNNFKTVINKIFEDCDGIPASFISALE----------------------LKEDVKSSPRSEADSLGTP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 601 MKEAMNRMI--DELNKQVSELSQLYKEAQAELEDYRKRKSLEDvtaEYIHKAEHEkLMQLTNvsrakaedALSEMKSQYS 678
Cdd:pfam17060 125 IKVDLLRNLkpQESPETPRRINRKYKSLELRVESMKDELEFKD---ETIMEKDRE-LTELTS--------TISKLKDKYD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644523 679 KVLNELTQLKQLVDAQKENSV-SITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 733
Cdd:pfam17060 193 FLSREFEFYKQHHEHGGNNSIkTATKHEFIISELKRKLQEQNRLIRILQEQIQFDP 248
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
388-768 |
6.73e-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: 40.22 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 388 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 448
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRELRKTLlanrfsygPAIDELEKQLA-EIEEEFSQFEELTESgdylearevleKLEEE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 449 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALEESERNK 521
Cdd:pfam06160 188 TDALEELmedipplYEELKTELPDQLEELKEGYREME--------EEGY-ALEHLNV-DKEIQQLEEQLEENLALLENLE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 522 -EKVRELEEKLVERekgtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLF---EKYQEAQEEIMKLKDT-LKSQMTQEASD 596
Cdd:pfam06160 258 lDEAEEALEEIEER-----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEhaeEQNKELKEELERVQQSyTLNENELERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 597 EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyiHKAEHEKLMQLTNVSRaKAEDALSEMKsq 676
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ--LEEIEEE--QEEFKESLQSLRKDEL-EAREKLDEFK-- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 677 yskvlNELTQLKQLVdaQKEN----SVSITEHL-QVITTLRTAAKEMEEKISNLKE-----HLASKEVEVAKLEKQLLEE 746
Cdd:pfam06160 406 -----LELREIKRLV--EKSNlpglPESYLDYFfDVSDEIEDLADELNEVPLNMDEvnrllDEAQDDVDTLYEKTEELID 478
|
410 420
....*....|....*....|....*..
gi 1034644523 747 KAAMTDAMVP-----RSSYEKLQSSLE 768
Cdd:pfam06160 479 NATLAEQLIQyanryRSSNPEVAEALT 505
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
496-853 |
7.06e-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: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 496 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgTVIKPPVEEYEEMKSSYCSVI---ENMNKEKAFLFEKY 572
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK--EELRQSREKHEELEEKYKELSassEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 573 QEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL-YKEAQAELEDYRKRKSLEdvtaeyihk 649
Cdd:pfam07888 125 AAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqAKLQQTEEELRSLSKEFQ--------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 650 aeheklmqltnvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHL 729
Cdd:pfam07888 196 ---------------ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 730 AS--------------KEVEVAKLEKQLLEEKAAMTDAmvpRSSYEK----LQSSLESEVSVLASKLKESVKEKEKVHSE 791
Cdd:pfam07888 261 SSmaaqrdrtqaelhqARLQAAQLTLQLADASLALREG---RARWAQeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644523 792 VVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEEL-AEMKRYAESSSKLEEDKDK 853
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELkasLRVAQKEKEQLqAEKQELLEYIRQLEQRLET 403
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
405-809 |
7.21e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 405 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLN-NTEISENSSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLG 480
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 481 LVSPESMD------NYSHFHELRVT-EEEINVLKQDLQNAL-EESERNKEKVRELEEKL------VEREKGTVIKPPVEE 546
Cdd:COG5022 879 LAERQLQElkidvkSISSLKLVNLElESEIIELKKSLSSDLiENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNK 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 547 YEEMKSSY---CSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ-EASDEAEDMKEAMNRMIDELNKqvseLSQL 622
Cdd:COG5022 959 LHEVESKLketSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQyGALQESTKQLKELPVEVAELQS----ASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 623 YKEAQAELedyRKRKSLEDVTAEYIhKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQL-VDAQKENSVS 700
Cdd:COG5022 1035 ISSESTEL---SILKPLQKLKGLLL-LENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKdLEVTNRNLVK 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 701 ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE-EKAAMTDAMVPRSSYEKLQSSLESE---VSVLAS 776
Cdd:COG5022 1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLElDGLFWEANLEALPSPPPFAALSEKRlyqSALYDE 1190
|
410 420 430
....*....|....*....|....*....|....*..
gi 1034644523 777 KLKESVKE----KEKVHSEVVQIRSEVSQVKREKENI 809
Cdd:COG5022 1191 KSKLSSSEvndlKNELIALFSKIFSGWPRGDKLKKLI 1227
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
685-864 |
7.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 685 TQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA----------- 753
Cdd:PHA02562 199 TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskieqfqkvi 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 754 ------------MVPRSSYEKLQSSLESEVSVLA---SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQ 818
Cdd:PHA02562 279 kmyekggvcptcTQQISEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034644523 819 EVNELLQKFQQAQeelAEMKRYAESSSKLEEDKDKKINEMSKEVTK 864
Cdd:PHA02562 359 KAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
44-124 |
7.32e-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: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 44 ASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTT-------------GHSALHLAAKNSHHECIRKLLQ-SK 109
Cdd:cd21882 64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLEnGA 143
|
90
....*....|....*..
gi 1034644523 110 CPA--ESVDSSGKTALH 124
Cdd:cd21882 144 QPAalEAQDSLGNTVLH 160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
495-636 |
8.12e-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: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 495 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK--GTVIKPpvEEYEEMKSSycsvIENMNKEKAFLFEKY 572
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNN--KEYEALQKE----IESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644523 573 QEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR 636
Cdd:COG1579 113 LELMERIEELEEELA-----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
485-736 |
1.00e-02 |
|
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: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 485 ESMDNYSHFHE-LRVTEEEINVLKQ--DLQNALEESERNKEKVRELEEKLverekgtvikpPVEEYEEMKSSYCSVIENM 561
Cdd:COG4913 232 EHFDDLERAHEaLEDAREQIELLEPirELAERYAAARERLAELEYLRAAL-----------RLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 562 NKEKAFLFEKYQEAQEEIMKLK---DTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA-ELEDYRKRK 637
Cdd:COG4913 301 RAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644523 638 SLEDVTAEYI-HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQlvdaqkeNSVSITEHLQvitTLRTAak 716
Cdd:COG4913 381 EFAALRAEAAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-------RKSNIPARLL---ALRDA-- 448
|
250 260
....*....|....*....|
gi 1034644523 717 emeekisnLKEHLASKEVEV 736
Cdd:COG4913 449 --------LAEALGLDEAEL 460
|
|
| |
