|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-249 |
1.05e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.28 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHD 249
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-240 |
1.28e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.90 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180 190
....*....|....*....|....*....|..
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSKISQDADLK 240
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-242 |
2.38e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666 25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDS 208
Cdd:COG0666 105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAgadvNAKDNDGKTA 222
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
50-214 |
2.16e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI 129
Cdd:COG0666 125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 209
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
|
....*
gi 1370488827 210 GYNAL 214
Cdd:COG0666 285 LLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
61-242 |
1.06e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 108.12 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 61 LRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLK 140
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 141 DLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLS 220
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180
....*....|....*....|....*.
gi 1370488827 221 ENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666 164 GNLEIVKLLLEAgadvNARDNDGETP 189
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
82-174 |
1.36e-23 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 95.57 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 82 LHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKsPINLKDlDGNIPLLLAVQNGHSEICH 161
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370488827 162 FLLDHGADVNSRN 174
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
115-207 |
1.53e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.87 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 115 LHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHgADVNSRNKsGRTALMLACEIGSSNAVE 194
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370488827 195 ALIKKGADLNLVD 207
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
49-141 |
2.23e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQsKCPAESVDsSGKTALHYAAAQGCLQAVQ 128
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1370488827 129 ILCEHKSPINLKD 141
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-181 |
4.08e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 97.72 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQ 128
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 129 ILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 181
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
58-231 |
2.99e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 85.49 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 58 VECLRVMITHGVDVTAQDTTGHSALHLAAKNS--HHECIRKLLQSKCPAESVDSSGKTALHYAAAQGC--LQAVQILCEH 133
Cdd:PHA03100 86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 134 KSPINLKDldgNIPLLLavqnghseichfllDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNA 213
Cdd:PHA03100 166 GVDINAKN---RVNYLL--------------SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
|
170
....*....|....*...
gi 1370488827 214 LHYSKLSENAGIQSLLLS 231
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLN 246
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
148-232 |
3.84e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 148 LLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKgADLNLVDSlGYNALHYSKLSENAGIQS 227
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 1370488827 228 LLLSK 232
Cdd:pfam12796 79 LLLEK 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-938 |
3.43e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlg 501
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREEL---------EKLEKEVKELEELKEEIEELEKELESLEGSKR-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvspesmdnyshfhelrvteeeinVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvIKPPVEEYEEMK---SSYCSV 578
Cdd:PRK03918 256 ------------------------KLEEKIRELEERIEELKKEIEELEEKVKELKE---LKEKAEEYIKLSefyEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDtlKSQMTQEASDEAEDMKEAMNRMidelnKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledvTAEYIHKAEHEklmqLTNVSRAKAE--DALSEMKSQYSKVLNELTQLKQLVDAQKENSVS-------ITEH--LQ 727
Cdd:PRK03918 382 -----TGLTPEKLEKE----LEELEKAKEEieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 728 VITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvpRSSYEKLQSSLESEVSVLASKLKESVKEKE 807
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL----KELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 808 KVHSEVVQIRSEVSQVKREKENIQTLLKSKEqevnELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 887 KEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVY 938
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
49-206 |
9.55e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 80.81 E-value: 9.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGV---DVTAQDttGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQ 125
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 126 AVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALM-LACEIGSSNAVEALIKKGADLN 204
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCN 229
|
..
gi 1370488827 205 LV 206
Cdd:PHA02875 230 IM 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-886 |
1.69e-14 |
|
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: 78.17 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVI-KPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQ 594
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 595 EAQEEIMKLKDTLKSQmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIH--KAE 672
Cdd:TIGR02168 772 EAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQvitTLRTAAKEMEEKISNLKEHLAS 752
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR---ELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 753 KEVEVAKLEKQLLEekaamtdamvprssyekLQSSLESEVSVLaskLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQt 832
Cdd:TIGR02168 927 LELRLEGLEVRIDN-----------------LQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKELG- 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 833 llkskeqEVNEL-LQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKL 886
Cdd:TIGR02168 986 -------PVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
38-214 |
1.91e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 76.93 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 38 VRARPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHY 117
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 118 AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEIChfLLDHGADVNSRNKSGRTALMLA----CEIgssNAV 193
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAinppCDI---DII 271
|
170 180
....*....|....*....|.
gi 1370488827 194 EALIKKGADLNLVDSLGYNAL 214
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
58-216 |
2.14e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.99 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 58 VECLRVMITHGVDVTAQDTTGHSALHLAAKNSH--HECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI--LCEH 133
Cdd:PHA03095 167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 134 KSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDslgyNA 213
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----AT 322
|
...
gi 1370488827 214 LHY 216
Cdd:PHA03095 323 LNT 325
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
52-242 |
1.54e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.84 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH-----------------------ECIRKLLQSKCPAESVD 108
Cdd:PHA02874 42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHdiikllidngvdtsilpipciekDMIKTILDCGIDVNIKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 109 SSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIG 188
Cdd:PHA02874 122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 189 SSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQsLLLSKIS---QDADLKTP 242
Cdd:PHA02874 202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE-LLINNASindQDIDGSTP 257
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
50-174 |
6.75e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.98 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQskCPAESVDSSGKTALHYAAAQGCLQAVQI 129
Cdd:PLN03192 563 HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLCTAAKRNDLTAMKE 640
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRN 174
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-911 |
8.62e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenssdlsQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI----------------EELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE-REKGTVIKPPVEEYEEMKSsycsVI 579
Cdd:PRK03918 296 IKLSEFYEEYlDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKA----KK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASdEAEDMKEAMNRMIDELNKQVSELsqlyKEAQ-------AELE 652
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEEL----KKAKgkcpvcgRELT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 653 DYRKRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMK-SQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIT- 730
Cdd:PRK03918 447 EEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAe 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 731 ---TLRTAAKEMEEKISNLKEHLASKEV---EVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSsLESEVSVLAS----- 797
Cdd:PRK03918 526 eyeKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLdeLEEELAELLKELEELGFESVEE-LEERLKELEPfyney 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 798 -KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFqqAQEELAEMKRYAESSSKLEEDKDKKI 876
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
490 500 510
....*....|....*....|....*....|....*
gi 1370488827 877 NEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
585-890 |
9.20e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 585 EKAflfEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE-AQAELEDYRKRKSLEDV 663
Cdd:COG1196 210 EKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 664 TA-EYIHKAEHEKLmqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsitEHLQVITTLRTAAKEMEEK 742
Cdd:COG1196 287 QAeEYELLAELARL--------EQDIARLEERRRELEERLEELEEELAELEEELE------ELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 743 ISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370488827 823 VKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-926 |
9.60e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LvspESMDNYShfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSYCSVIEN 581
Cdd:COG1196 308 E---ERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR--KS 659
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 LEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQ---------LKQLVDAQKENSVSITEHLQVIT 730
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 731 TLRTAAkemEEKISNLKEHLASKEVEVAKLEKQLLEEKAA-------MTDAMVPRSSYEKLQSSLESEVSVLASKLKESV 803
Cdd:COG1196 535 AYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 804 KEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1370488827 884 TKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
94-238 |
1.10e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 71.59 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 94 IRKLLQSKCPAESVDSSGKTALHY---AAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSE-ICHFLLDHGAD 169
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 170 VNSRNKSGRTALMLACEIGSSNA--VEALIKKGADLNLVDSLGYNALHYSKLSENAGIQ--SLLLSKISQDAD 238
Cdd:PHA03095 110 VNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYA 182
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-222 |
1.22e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 71.21 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 47 HCFHLAAAKghVECLRVMITHGVDVTAQDTTGHSALH--LAAKNSHHECIRKLLQSKCPAESVDSSGKTALH-YAAAQGC 123
Cdd:PHA03095 88 HLYLYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 -LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHS--EICHFLLDHGADVNSRNKSGRTALMLACEIGSSNA--VEALIK 198
Cdd:PHA03095 166 nVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLI 245
|
170 180
....*....|....*....|....
gi 1370488827 199 KGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNN 269
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
59-217 |
1.25e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 59 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPIN 138
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 139 LKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACeIGSSNAVEALIKKgADLNLVDSLGYNALHYS 217
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
52-203 |
1.33e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.82 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILc 131
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL- 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 132 EHKSPINLKDLDGNIpLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 203
Cdd:PLN03192 611 YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
420-891 |
2.14e-12 |
|
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: 71.64 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKEVLSVQKqmk 499
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------EDLRAELEEVDKEFAETRDELKDYRE--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 lglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKssycsvi 579
Cdd:TIGR02169 393 ----------------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAI------AGIEAKINELEEEK------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 enmnKEKAflfEKYQEAQEEIMKLKDTLKSqmtqeASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:TIGR02169 444 ----EDKA---LEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 LEDVTAEYIhKAEHEKLMQLTNVSRAKA-----------------EDALSEMKSQYSKV----------LNELTQLKQLV 712
Cdd:TIGR02169 512 VEEVLKASI-QGVHGTVAQLGSVGERYAtaievaagnrlnnvvveDDAVAKEAIELLKRrkagratflpLNKMRDERRDL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 713 DAQKENSVsITEHLQVIttlrtaakEMEEKISN-----LKEHLASKEVEVAK----------LEKQLLEEKAAMTDAMVP 777
Cdd:TIGR02169 591 SILSEDGV-IGFAVDLV--------EFDPKYEPafkyvFGDTLVVEDIEAARrlmgkyrmvtLEGELFEKSGAMTGGSRA 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 778 RSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAE 857
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1370488827 858 MKRYAES-SSKLEEDK------DKKINEMSKEVTKLKEALN 891
Cdd:TIGR02169 742 LEEDLSSlEQEIENVKselkelEARIEELEEDLHKLEEALN 782
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
59-208 |
3.48e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 59 ECLRVMITHGVDVTAQDT-TGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPI 137
Cdd:PHA02878 148 EITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 138 NLKDLDGNIPLLLAVQNGHS-EICHFLLDHGADVNSRNK-SGRTALMLAceIGSSNAVEALIKKGADLNLVDS 208
Cdd:PHA02878 228 DARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSS--IKSERKLKLLLEYGADINSLNS 298
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-891 |
1.59e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLksqmtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRK 658
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKEL---------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 SLEDVTAEyihkaEHEKLMQLTNVSRAKAEDALSEMKSqyskvlnELTQLKQLVDAQKENSVSITEHLQ----VITTLRT 734
Cdd:TIGR02168 750 AQLSKELT-----ELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDelraELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvprSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVV 814
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 815 QIRS--------------EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLEEDKDKKINEM 879
Cdd:TIGR02168 891 LLRSeleelseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970
|
330
....*....|..
gi 1370488827 880 SKEVTKLKEALN 891
Cdd:TIGR02168 971 RRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-774 |
2.87e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQ------LQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKevlsvq 495
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA------ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 496 kqmklglvspesmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvikppVEEYEEMKSSY 575
Cdd:COG1196 261 --------------------ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------IARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 576 CSVIENMNKEKAFLFEKYQEAQEEIMKLkdtlksqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyR 655
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE-L 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 656 KRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA 735
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350
....*....|....*....|....*....|....*....
gi 1370488827 736 AKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA 774
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
420-891 |
3.76e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LglvspesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTViKPPVEEYEEMKSSYCSVI 579
Cdd:TIGR02168 397 S-------------------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKS---------QMTQEASDEAEDMKEAMNRMID------------------- 631
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQlqarldsleRLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegye 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 632 ---------ELNKQVSELSQLYKEAQAELEDYRKRKS----LEDVTAEYIHKAEHEKLMQLTNVSRAKAEdaLSEMKSQY 698
Cdd:TIGR02168 537 aaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVtflpLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 699 SKVLN----------------------------------------------------------ELTQLKQLVDAQKEnsv 720
Cdd:TIGR02168 615 RKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEE--- 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 721 SITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK 800
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 801 ESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 880
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570
....*....|.
gi 1370488827 881 KEVTKLKEALN 891
Cdd:TIGR02168 852 EDIESLAAEIE 862
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
620-856 |
4.53e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.96 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEyihkaeheklMQLTNVSRAKAEDALSEMKSQYS 699
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----------AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 700 KVLNELTQLKQLVDAQKENSVSITEHlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMtdamvpRS 779
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 SYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI---RSEVSQVKREKENIQTLLkskeqevNELLQKFQQAQEELA 856
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY-------ESLLQRLEEARLAEA 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
431-890 |
7.23e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 431 QDLQKRLESSEAERKQLQVElQSRRAElvclnntEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDN 510
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAE-EAKKAD-------EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 511 YSHFHELRVTEEEINV--------LKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENM 582
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKAdaakkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 583 N----KEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAE----- 650
Cdd:PTZ00121 1445 KadeaKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakka 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 651 -----LEDYRK----RKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKVLN--ELTQLKQLVDAQKEN 718
Cdd:PTZ00121 1525 deakkAEEAKKadeaKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEE 1604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 719 SVSITEHLQVITTLRTAAKEM--EEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 795 LASKLK-ESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllksKEQEVNELlqKFQQAQEELAEMKRYAESSSKLEEDKd 873
Cdd:PTZ00121 1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEELK-----KAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEK- 1756
|
490
....*....|....*..
gi 1370488827 874 KKINEMSKEVTKLKEAL 890
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEI 1773
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
113-164 |
7.97e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 7.97e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 113 TALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLL 164
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
416-891 |
1.47e-10 |
|
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: 65.04 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 416 TTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLS 493
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 494 VQKQMK--------------------------LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 547
Cdd:TIGR04523 108 INSEIKndkeqknklevelnklekqkkenkknIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 548 LEEKL-VEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ--EASDEAEDMKE 624
Cdd:TIGR04523 188 NIDKIkNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 625 AMNRMIDEL---NKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV 701
Cdd:TIGR04523 268 QLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 702 LNELTQL---------------KQLVDAQKENSvsitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:TIGR04523 348 KKELTNSesensekqreleekqNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1370488827 847 KFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
422-891 |
2.47e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMklg 501
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVIEN 581
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---------EALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL- 660
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLa 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 ---------EDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT 731
Cdd:COG1196 524 gavavligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 732 LRTAAKEMEEKISNLKEHLASKEVEVA----------KLEKQLLEEKAAMTDAMVPRSSYE----KLQSSLESEVSVLAS 797
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAArleaalrravTLAGRLREVTLEGEGGSAGGSLTGgsrrELLAALLEAEAELEE 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 798 KLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKIN 877
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
490
....*....|....
gi 1370488827 878 EMSKEVTKLKEALN 891
Cdd:COG1196 764 ELERELERLEREIE 777
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
80-215 |
2.64e-10 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 64.26 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 80 SALHLAAKNSHHECIRKLLqsKCPaeSVD-----SSGKTALHYAAAQGCLQAVQILCEH-----KSPINLKDLDGNIPLL 149
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL--KCP--SCDlfqrgALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 150 LAVQNGHSEICHFLLDHGADVNS---------RNKS-----GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALH 215
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
58-231 |
3.98e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 63.12 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 58 VECLRVMITHGVDVTAQDTTGHSALHLaaknshhecirkLLQSKCPAESVDssgktalhyaaaqgclqavqILCEHKSPI 137
Cdd:PHA03095 63 KDIVRLLLEAGADVNAPERCGFTPLHL------------YLYNATTLDVIK--------------------LLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 138 NLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVNSRNKSGRTAlmLACEIGSSNA----VEALIKKGADLNLVDSLGY 211
Cdd:PHA03095 111 NAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188
|
170 180
....*....|....*....|..
gi 1370488827 212 NALHYSKLS--ENAGIQSLLLS 231
Cdd:PHA03095 189 SLLHHHLQSfkPRARIVRELIR 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-891 |
4.23e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 528 KQDLQNALEESERNKEKV----RELEEKLVEREKGTVIkppVEEYEEMKSsycsviENMNKEKAFLFEKYQEAQEEIMKL 603
Cdd:TIGR02168 174 RKETERKLERTRENLDRLedilNELERQLKSLERQAEK---AERYKELKA------ELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 604 KDTLKSQMTQEASDEAE-DMKEAMnrmIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEHEKlmqltnv 682
Cdd:TIGR02168 245 QEELKEAEEELEELTAElQELEEK---LEELRLEVSELEEEIEELQKELYALANE----------ISRLEQQK------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 683 srakaedalsemksqysKVLNEltQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK 762
Cdd:TIGR02168 305 -----------------QILRE--RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 763 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKEN-----IQTLLKSK 837
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEEL 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 838 EQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
517-891 |
4.33e-10 |
|
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: 63.33 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELKDK----------------YRELRKTL--------LANRFSYGPAIDE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVTAEYihkae 672
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPD-----QLEELKEGY----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKISNLKE 748
Cdd:pfam06160 221 REMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE--LDEAEEALEEIEERIDqlydLLEKEVDAKKYVEKNLPEIED 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 749 HLAskevEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVK---EKEKVHSEVV----QIRSEVS 821
Cdd:pfam06160 299 YLE----HAEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVErleEKEVAYSELQeeleEILEQLE 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 822 QVKREKENIQTLLKS---KEQEVNELLQKFQQaqeELAEMKRYAESS--SKLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:pfam06160 375 EIEEEQEEFKESLQSlrkDELEAREKLDEFKL---ELREIKRLVEKSnlPGLPESYLDYFFDVSDEIEDLADELN 446
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
52-230 |
1.01e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.93 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 52 AAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIrKLLQSKCPAESVDSSG-KTALHYAAAQGCLQAVQIL 130
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAI-KLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 131 CEHKSPINlkDL---DGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVD 207
Cdd:PHA02875 88 LDLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165
|
170 180
....*....|....*....|...
gi 1370488827 208 SLGYNALHYSKLSENAGIQSLLL 230
Cdd:PHA02875 166 CCGCTPLIIAMAKGDIAICKMLL 188
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
47-98 |
2.54e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.54e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 47 HCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLL 98
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
163-216 |
2.68e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.89 E-value: 2.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 163 LLDHG-ADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHY 216
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-859 |
2.86e-09 |
|
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: 61.19 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 430 LQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQK----------QMK 499
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisqlneqisQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLVSPESmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSYCSVI 579
Cdd:TIGR04523 349 KELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-------------QNQEKLNQQKDEQI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdmKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrKRKS 659
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI--IKNLDNTRESLETQLKVLSRSINKIKQNLEQ--KQKE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 LEDVTAEyihkaeheklmqltnvsrakaedaLSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvITTLRTAAKEM 739
Cdd:TIGR04523 491 LKSKEKE------------------------LKKLNEEKKELEEKVKDLTKKISSLKEK----------IEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 740 EEKISNLKEHLASKEVEVAK--LEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIR 817
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1370488827 818 SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMK 859
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
147-197 |
2.92e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 147 PLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALI 197
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-891 |
4.47e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 304 FKAEISSIRENKDRLSDSTTGADSLLDISSE--ADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHS 381
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 382 tqtdlgpslgkpgetsppdsksspsvLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL 461
Cdd:TIGR02168 387 --------------------------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 462 NNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQ----------KQMKLGLVSPESM-DNYSHFHE-------------- 516
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEqaldaaerelAQLQARLDSLERLqENLEGFSEgvkallknqsglsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 --------LRVTEE-EI---NVLKQDLQNALEEserNKEKVRELEEKLVEREKGTVI----------KPPVEEYEEMKSS 574
Cdd:TIGR02168 521 ilgvlselISVDEGyEAaieAALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTflpldsikgtEIQGNDREILKNI 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 575 YCSVIENMNKEKA---------------FLFEKYQEAQEEIMKLK----------DTLKSQ--MTQeASDEAEDMKEAMN 627
Cdd:TIGR02168 598 EGFLGVAKDLVKFdpklrkalsyllggvLVVDDLDNALELAKKLRpgyrivtldgDLVRPGgvITG-GSAKTNSSILERR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 628 RMIDELNKQVSELSQLYKEAQAELEDYrkRKSLEDVTAEyIHKAEHEKLMQLTNVSRAKAEDALSEMKSQyskvlNELTQ 707
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAEL--RKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE-----QLEER 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 708 LKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDamvprssyeklqss 787
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------- 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 788 LESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSK 867
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
650 660
....*....|....*....|....
gi 1370488827 868 LEEDKDKKINEMSKEVTKLKEALN 891
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-697 |
5.44e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEIsenssDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 495 QKQMKLGLVSPESMDNY---------SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVE--------REK 557
Cdd:TIGR02168 746 EERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 558 GTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKS-----QMTQEASDEAEDMKEAMNRMIDE 632
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 633 LNKQVSELSQLYKEAQAELEDYRKRKS---------LEDVTAEYIHKAE-HEKLMQLTNVSRAKAEDALSEMKSQ 697
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEglevridnlQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
50-230 |
6.59e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.69 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSgktaLHYAAAQGCLQAVQI 129
Cdd:PHA02876 183 HYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 130 LCEHKSPINLKDLDGNIPLLLAVQNGH-SEICHFLLDHGADVNSRNKSGRTALMLACEIG-SSNAVEALIKKGADLNLVD 207
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338
|
170 180
....*....|....*....|....
gi 1370488827 208 SLGYNALHY-SKLSENAGIQSLLL 230
Cdd:PHA02876 339 RLYITPLHQaSTLDRNKDIVITLL 362
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
64-217 |
7.50e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.69 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 64 MITHGVDVTAQDTTGHSALHLAAKNSHH-ECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQI-LCEHKSPINLKD 141
Cdd:PHA02876 293 LLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARD 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 142 LDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA-CEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02876 373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
38-216 |
8.67e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.31 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 38 VRARPRKLKHCFHLAAAKGH-VECLRVMITHGVDVTAQDTTGHSALHLAAK-NSHHECIRKLLQSKCPAESVDSSGKTAL 115
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 116 HYAAAQGCLQAVQILCEHKSPINL--KDLDGNIPLLLAVQNGHSEIcHFLLDHGADVNSRNKSGRTALMLACEIGSS-NA 192
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEAlsQKIGTALHFALCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNCKlDV 458
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370488827 193 VEALIKKGADLNLVD---------SLGYNA-----LHY 216
Cdd:PHA02876 459 IEMLLDNGADVNAINiqnqyplliALEYHGivnilLHY 496
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
517-891 |
1.10e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 59.08 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKlverekgtvikppveeYEEMKSSYcsvienmnKEKAFLFEKYQEA 596
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDL----------------YRELRKSL--------LANRFSFGPALDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSQMTQEASD----EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDyrkrkSLEDVtaeyihKAE 672
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTELPD-----QLQEL------KAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 673 HEKLMQ----LTNVsraKAEDALSEMKSQYSKVLNELTQLKqlVDAQKENSVSITEHLQ----VITTLRTAAKEMEEKIS 744
Cdd:PRK04778 239 YRELVEegyhLDHL---DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDqlydILEREVKARKYVEKNSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 745 NLKEHL--ASKEVEVAKLEKQLLEEKAAMTDAMVprSSYEKLQSSLESEVSVLaSKLKESVKEKEKVHSEVV----QIRS 818
Cdd:PRK04778 314 TLPDFLehAKEQNKELKEEIDRVKQSYTLNESEL--ESVRQLEKQLESLEKQY-DEITERIAEQEIAYSELQeeleEILK 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 819 EVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS--KLEEDKDKKINEMSKEVTKLKEALN 891
Cdd:PRK04778 391 QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNlpGLPEDYLEMFFEVSDEIEALAEELE 465
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
78-130 |
1.14e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 78 GHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQIL 130
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
422-934 |
1.53e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISEnssdLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR-LEVSE----LEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVSPESMDNyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtVIKPPVEEYEEMKSSYCSVIEN 581
Cdd:TIGR02168 308 RERLANLER-----QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA--ELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQE---AQEEIMKLKDTLKS------QMTQEASDEAEDMKEAMnrmIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR02168 381 LETLRSKVAQLELQiasLNNEIERLEARLERledrreRLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 653 DYRKRKSLEDVTAEYIHKAEHEKLMQLTNV-SRAKAEDALSEMKSQYSKVLNELTQ-----------LKQL--VDAQKEN 718
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvLSELisVDEGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 719 SVSIT--EHLQ--VITTLRTAAKEmeekISNLKEHLASK-------EVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSS 787
Cdd:TIGR02168 538 AIEAAlgGRLQavVVENLNAAKKA----IAFLKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 788 LESEVSVL----------------ASKLKE-----------------SVKEKEKVHSEVVQIRSEVSQVKREKENIQTLL 834
Cdd:TIGR02168 614 LRKALSYLlggvlvvddldnalelAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 835 KSKEQEVNELLQKFQQAQEELAEMKryaesssKLEEDKDKKINEMSKEVTKL-KEALNSLSQLSYSTSSSKRQSQQLEAL 913
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580
....*....|....*....|.
gi 1370488827 914 QQQVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEEL 787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-911 |
1.72e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKppvEEYEEMKSSYCSVIEN 581
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQ---EEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSElSQLYKEAQAELEDYRKRK 658
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 SLEDvTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTA--A 736
Cdd:PTZ00121 1461 EAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 737 KEMEEKiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQI 816
Cdd:PTZ00121 1540 KKAEEK-KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 817 RSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinemSKEVTKLKEALNSLSQL 896
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEA 1693
|
490
....*....|....*
gi 1370488827 897 SYSTSSSKRQSQQLE 911
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK 1708
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
518-888 |
2.32e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 518 RVTEEEINVLKQ-DLQNALEESERNKEKVRELEEKLVErekgtvIKPPVEEYEEMKSSYCSVIENMNKekafLFEKYQEA 596
Cdd:PRK02224 180 RVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE----VLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrksLEDVTAEYI--HKAEHE 674
Cdd:PRK02224 250 REELETLEAEIED--LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-------LDDADAEAVeaRREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 675 KlmqltnvSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSvsitehlqviTTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PRK02224 321 D-------RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREAVEDRR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 755 VEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKE---SVKEKEKVHSEVVQIRSE------------ 819
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 820 ------VSQVKREKENIQTLLKSKEQEVNELLQKFQQAqEELAEMKRYAES-------SSKLEEDKDKKINEMSKEVTKL 886
Cdd:PRK02224 464 sphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERleerredLEELIAERRETIEEKRERAEEL 542
|
..
gi 1370488827 887 KE 888
Cdd:PRK02224 543 RE 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
523-890 |
2.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 523 EINVLKQDLQNALEESERNKEKVRELEEKLVE-----REKGTVIKPPVEEYEEMKSSYcsvienmnKEKAFLFEKYQEAQ 597
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEV--------KELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 598 EEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqaelEDYRKRKSLEDVTAEYIHKAEHE--K 675
Cdd:PRK03918 245 KELESLEGSKRK--LEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRlsR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 676 LMQLTNVSRAKAEDA------LSEMKSQYSKVLNELTQLKQLVDA---------------QKENSVSITEHLQVITTLRT 734
Cdd:PRK03918 319 LEEEINGIEERIKELeekeerLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 735 AAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSY-----EKLQSSLESEVSVLASKLKESVKEKEKV 809
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 810 HSEVVQIRSEVSQVKREKENIQTL--LKSKEQEVNEL-LQKFQQAQEELAEMKRYA---ESSSKLEEDKDKKINEMSKEV 883
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYnLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKL 558
|
....*..
gi 1370488827 884 TKLKEAL 890
Cdd:PRK03918 559 AELEKKL 565
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
579-890 |
2.79e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMK---EAMNRMIDELNKQVSELSQLYKEAQAELED 653
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEqeeEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 654 YRKRKS-LEDVTAEYihKAEHEKLmqltnvsrakaEDALSEmkSQYSKVLNELTQLKQLVdaqkensvsitehlqvittl 732
Cdd:TIGR02169 763 LEARIEeLEEDLHKL--EEALNDL-----------EARLSH--SRIPEIQAELSKLEEEV-------------------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 733 rtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKES-------VKE 805
Cdd:TIGR02169 808 ----SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 806 KEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR--YAESSSKLEEDKDKKINEMSKEV 883
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkGEDEEIPEEELSLEDVQAELQRV 963
|
....*..
gi 1370488827 884 TKLKEAL 890
Cdd:TIGR02169 964 EEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-652 |
3.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 414 KSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteiSENSSDLSQKlKETQSKYEEAmkevls 493
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL--------KELEARIEEL-EEDLHKLEEA------ 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 494 vqkqmklgLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERnKEKVRELEEKLVEREKGTvIKPPVEEYEEMKS 573
Cdd:TIGR02169 781 --------LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 574 SYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
181-243 |
3.30e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 3.30e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 181 LMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPT 243
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
417-884 |
3.76e-08 |
|
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: 57.44 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 417 TDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVClNNTEISENSSDLSQKLKETQSKYEEAMKEVlsvqk 496
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEEL----- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 497 QMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIkppveeyeemkssyc 576
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI--------------- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 577 sVIENMNKEkaflfekYQEAQEEIMKLKDTLKSqMTQEASDEAEDMKEAMNRMIDELNKqVSELSqlykeAQAELEDYRK 656
Cdd:pfam15921 413 -TIDHLRRE-------LDDRNMEVQRLEALLKA-MKSECQGQMERQMAAIQGKNESLEK-VSSLT-----AQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 657 RKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKV-------LNELTQLK----QLVDAQKENS---VSI 722
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLrsrvdlkLQELQHLKnegdHLRNVQTECEalkLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 723 TEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA------ 796
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvkl 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 797 --------SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEMKRYAES 864
Cdd:pfam15921 638 vnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttNKLKMQLKSAQSELEQTRNTLKS 717
|
490 500
....*....|....*....|
gi 1370488827 865 SSKLEEDKDKKINEMSKEVT 884
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQIT 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-889 |
7.73e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 531 LQNALEESERNKEKVRELEekLVEREKGTVIKPPVEEyeemkssycsvienmnKEKAflfEKYQEAQEEIMKLKDTLKSQ 610
Cdd:TIGR02169 172 KEKALEELEEVEENIERLD--LIIDEKRQQLERLRRE----------------REKA---ERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 611 MtqeasdeaedmKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksledvtaeyIHKAEhEKLMQLTNVSRAKAEDA 690
Cdd:TIGR02169 231 E-----------KEALERQKEAIERQLASLEEELEKLTEEISELEKR----------LEEIE-QLLEELNKKIKDLGEEE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 691 LSEMKSQYSKVLNELTQLKQLVDAQKENsvsitehlqvittlrtaAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaa 770
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERE-----------------LEDAEERLAKLEAEIDKLLAEIEELEREIEEER-- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 771 mtdamvprssyeKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQtllkskeQEVNELLQKFQQ 850
Cdd:TIGR02169 350 ------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDR 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1370488827 851 AQEEL-----------AEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEA 889
Cdd:TIGR02169 411 LQEELqrlseeladlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
94-166 |
1.21e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDH 166
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
49-217 |
1.41e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 49 FHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS--KCPAESVDSSGKTALHY--------- 117
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinKCSVFYTLVAIKDAFNNrnveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 118 ------------------AAAQGCLQA--VQILCEHKSPINLKDLD-GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS 176
Cdd:PHA02878 121 ltnrykniqtidlvyidkKSKDDIIEAeiTKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYS 217
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
35-171 |
3.51e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.90 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 35 NTTVRARPRKLKHCFHLAAAK--GHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHEC-IRKLLQSK---------- 101
Cdd:PHA03100 96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKgvdinaknrv 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 102 -------CPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA03100 176 nyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
124-232 |
3.84e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 LQAVQILCEHKSPINLKDLDGNIPLLLAVQN-----GHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEAL-- 196
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370488827 197 -IKKGADLNLVDSLGYNALH-YSKLSENAGIQ--SLLLSK 232
Cdd:PHA02798 131 mIENGADTTLLDKDGFTMLQvYLQSNHHIDIEiiKLLLEK 170
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
44-184 |
4.12e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 44 KLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQgC 123
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY-C 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 124 L--QAVQILCEHKSPINLKD-LDGNIPLLLAVqngHSE-ICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:PHA02878 246 KdyDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
110-221 |
4.12e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.73 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 110 SGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLAC-EIG 188
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCK 246
|
90 100 110
....*....|....*....|....*....|....
gi 1370488827 189 SSNAVEALIKKGADLNLVDS-LGYNALHYSKLSE 221
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-909 |
4.52e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVElqsrraelvclnNTEISENSSDLSQKLKEtqskyEEAMKEVLSVQKqmklg 501
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lVSPESmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEYEEMKSSYCSVIEN 581
Cdd:pfam01576 127 -VTTEA--------KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE------KAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MN--------------KEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEdMKEAMNRMIDELNKQVSELSQLyKEA 647
Cdd:pfam01576 192 LEerlkkeekgrqeleKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLEEETAQKNNALKKI-REL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 648 QAELEDYRkrkslEDVTAEYIHKAEHEK----LMQLTNVSRAKAEDALSEMKSQY---SKVLNELTQLKQLVDAQKENsv 720
Cdd:pfam01576 270 EAQISELQ-----EDLESERAARNKAEKqrrdLGEELEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRS-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 721 siteHLQVITTLR----TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLA 796
Cdd:pfam01576 343 ----HEAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 797 SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSS----KLEEDK 872
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLStrlrQLEDER 498
|
490 500 510
....*....|....*....|....*....|....*..
gi 1370488827 873 DKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-891 |
4.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 591 EKYQEAQEEIMKLKDTLKSQMTQ-----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTA 665
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 666 EYIHKAEHEKLMQLTNVsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLqvitTLRTAAKEMEEKISN 745
Cdd:PRK03918 238 EEIEELEKELESLEGSK--RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 746 LKEHLASKEVEVAKLEKQLLEekaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVhSEVVQIRSEVSQVKR 825
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKE------------------LEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 826 EKENIQTLLKSKE-QEVNELLQKFQQAQEELAEmkryaesssKLEEDKDkKINEMSKEVTKLKEALN 891
Cdd:PRK03918 373 ELERLKKRLTGLTpEKLEKELEELEKAKEEIEE---------EISKITA-RIGELKKEIKELKKAIE 429
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
516-888 |
5.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSyCSV----IENMNKEKAFLFE 591
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE---------EERDDLLAE-AGLddadAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 592 KYQEAQEEIMKlkdtlKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKS-LEDVTAEYihk 670
Cdd:PRK02224 322 RDEELRDRLEE-----CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeIEELEEEI--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 671 AEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQL--------------KQLVDAQK----ENSVSITEHLQVITtl 732
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELeatlrtarerveeaEALLEAGKcpecGQPVEGSPHVETIE-- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 733 rtaakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAmtdamvprssyeklqSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:PRK02224 472 -----EDRERVEELEAELEDLEEEVEEVEERLERAEDL---------------VEAEDRIERLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEM-KRYAESSSKLE-----EDKDKKINEMSKEVTKL 886
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnSKLAELKERIEsleriRTLLAAIADAEDEIERL 611
|
..
gi 1370488827 887 KE 888
Cdd:PRK02224 612 RE 613
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
51-181 |
6.17e-07 |
|
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: 53.48 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 51 LAAAKGHVECLRVMIT-HGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQS-----KCPAESVDSSGKTALHYAAAQGCL 124
Cdd:cd22192 23 LAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 125 QAVQIL---------------CEHKSPINLKDLdGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTAL 181
Cdd:cd22192 103 NLVRELiargadvvspratgtFFRPGPKNLIYY-GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
75-219 |
6.90e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 53.16 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 75 DTTGHSALHLAAKNSHHECIRKLLQSKCPAESVdssGKTALHyAAAQGCLQAVQILCEHKSPINLKDLD----------- 143
Cdd:TIGR00870 49 DRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqytse 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 144 ---GNIPLLLAVQNGHSEICHFLLDHGADVNSRNKS--------------GRTALMLACEIGSSNAVEALIKKGADLNLV 206
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204
|
170
....*....|...
gi 1370488827 207 DSLGYNALHYSKL 219
Cdd:TIGR00870 205 DSLGNTLLHLLVM 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
434-885 |
8.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 434 QKRLESSEAERKQLQVELQSRRAELVclNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLglvspESMDNYSH 513
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 514 FHELRVTEEEINVlkQDLQNAleESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEmkssycsvieNMNKEKAFLFEKY 593
Cdd:PTZ00121 1524 ADEAKKAEEAKKA--DEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKAEEAKKA 1589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 594 QEAQ-EEIMKLKDTLKSQMTQEASDEAEDMKEAMN-RMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKA 671
Cdd:PTZ00121 1590 EEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 672 EHEKlmqltnvsRAKAEDALSEMKSQYSKvlneltqlkqlvdaqKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLA 751
Cdd:PTZ00121 1670 AEED--------KKKAEEAKKAEEDEKKA---------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 752 SKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQ--SSLESEVSVLASKLKESVKE---KEKVHSEVVQIRSEVSQVKRE 826
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEeelDEEDEKRRMEVDKKIKDIFDN 1806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYA-ESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PTZ00121 1807 FANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQlEEADAFEKHKFNKNNENGEDGNK 1866
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
515-870 |
8.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 515 HELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKA------F 588
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleelrE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 589 LFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKqlvdaqkensVSITEHLQVITTLRTAAKEMEEKISNLKE 748
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 749 HLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSvLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKE 828
Cdd:COG4717 310 LPALEELEEEELEELL-----------------AALGLPPDLSPE-ELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1370488827 829 NIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEE 870
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
143-175 |
8.85e-07 |
|
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: 46.13 E-value: 8.85e-07
10 20 30
....*....|....*....|....*....|....
gi 1370488827 143 DGNIPLLLAV-QNGHSEICHFLLDHGADVNSRNK 175
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
546-766 |
9.36e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.71 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 546 RELEEKLVE----REKGTVIKPPVEE-YEEMKSsyCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAE 620
Cdd:PHA02562 153 RKLVEDLLDisvlSEMDKLNKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 621 DMKEAMNRMIDELNKQVSELSQlYKEAQAELEDYRKRKSLEDVTAEYIHK---------------AEHEKLMQltnvsra 685
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDRIT------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 686 KAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITE-------HLQVITTLRTAAKEMEEKISNLKEHLASKEVEVA 758
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElknkistNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
....*...
gi 1370488827 759 KLEKQLLE 766
Cdd:PHA02562 383 KLQDELDK 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
425-859 |
1.06e-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: 52.81 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 425 QLQEILQDLQKRLESSEAERKQ-----------------LQVELQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKy 484
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhLRRELDDRNMEvqrLEALLKAMKSECQGQMERQMAAIQGK- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 485 EEAMKEVLSVQKQMKlglvSPESMdnyshfheLRVTEEEINVLKQdlqnALEESERNkekVRELEEKLVEREKGtvIKPP 564
Cdd:pfam15921 457 NESLEKVSSLTAQLE----STKEM--------LRKVVEELTAKKM----TLESSERT---VSDLTASLQEKERA--IEAT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 565 VEEYEEMKSSY---CSVIENMNKEKAFLfeKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:pfam15921 516 NAEITKLRSRVdlkLQELQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 642 QLYKEA---QAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAED--ALSEMKSQYSKVLNE-------LTQLK 709
Cdd:pfam15921 594 QLEKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlrAVKDIKQERDQLLNEvktsrneLNSLS 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 710 QLVDAQKENSVSITEHLQVITT-----LRTAAKEMEEKISNLK-----------------EHLASKEVEVAKLEK--QLL 765
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNklkmqLKSAQSELEQTRNTLKsmegsdghamkvamgmqKQITAKRGQIDALQSkiQFL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 766 EEkaAMTDAMVPRSSYEKLQSSLESEVSVLASklkesvkEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELL 845
Cdd:pfam15921 754 EE--AMTNANKEKHFLKEEKNKLSQELSTVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQ 824
|
490
....*....|....
gi 1370488827 846 QKFQQAQEELAEMK 859
Cdd:pfam15921 825 DIIQRQEQESVRLK 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
422-933 |
1.50e-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: 52.28 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVE-------LQSRRAE---LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEV 491
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrTSAFRDLqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 492 LSVQKQMKLglvsPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-KEKVRELEEKLVEREKGTVIKPPVEEYEE 570
Cdd:TIGR00618 460 HLQESAQSL----KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 571 MKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 648
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 649 AELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQv 728
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLT-----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 729 itTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLleekaamtdamvprssyEKLQSSLESEVSVLASKLKESVKEKEK 808
Cdd:TIGR00618 690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI-----------------ENASSSLGSDLAAREDALNQSLKELMH 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 809 VHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE----LAEMKryAESSSKLEEDKDKKINEMSKEVT 884
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthlLKTLE--AEIGQEIPSDEDILNLQCETLVQ 828
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1370488827 885 KLKEALNSLSQLSYSTSSSKRQSQQLEalqqqvkqlqnqlaECKKQHQE 933
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYE--------------ECSKQLAQ 863
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
420-600 |
2.05e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNnTEISENSSDLSQkLKETQSKYEEAMKEVLSvQKQMK 499
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEE-VEARIKKYEEQLGNVRN-NKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCSVI 579
Cdd:COG1579 93 ALQ------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEEL 151
|
170 180
....*....|....*....|.
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEI 600
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-934 |
2.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 741 EKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprssyeklQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV 820
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREE----------------LEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 821 SQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNslsqlsYST 900
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE------ELK 350
|
170 180 190
....*....|....*....|....*....|....
gi 1370488827 901 SSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEV 934
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETL 384
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
119-198 |
3.16e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 119 AAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIK 198
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
579-812 |
3.67e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 579 IENMNKEKAFLFEKYQEAQEEIMKLKDTLKSqmTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrk 658
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 sledVTAEYIHKAEHEKLMQLTN-------VSRAkaeDALSEMKSQYSKVLNELTQLKQLVDAQKENSVsitehlQVITT 731
Cdd:COG3883 92 ----ARALYRSGGSVSYLDVLLGsesfsdfLDRL---SALSKIADADADLLEELKADKAELEAKKAELE------AKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 732 LRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHS 811
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
.
gi 1370488827 812 E 812
Cdd:COG3883 239 A 239
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
137-184 |
3.70e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 3.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1370488827 137 INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLA 184
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
108-151 |
3.93e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 3.93e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370488827 108 DSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLA 151
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-971 |
3.95e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEeinVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQE 595
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 596 AQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEK 675
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 676 lmQLTNVSRAKAEDALSEMKSQYSKvlNELTQLKQLVDAQK-ENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:PTZ00121 1343 --KAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 755 vEVAKLEKQLLEEKAAmtdamvprssyEKLQSSLESEVSvlASKLKESVKEKEKvhsevvqirSEVSQVKREKENIQTLL 834
Cdd:PTZ00121 1419 -KADEAKKKAEEKKKA-----------DEAKKKAEEAKK--ADEAKKKAEEAKK---------AEEAKKKAEEAKKADEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 835 KSKEQE---VNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:PTZ00121 1476 KKKAEEakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 912 ALQQQVKQLQNQLAECKKQHQE--VISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQK 971
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
64-118 |
5.02e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 5.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 64 MITHG-VDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYA 118
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
59-232 |
5.52e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 50.22 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 59 ECLRVMITHGVDVTAQDTTGHSALHLAAKNSHH---ECIRKLLQSKCPAESVDSS-GKTALHyaaaqgclqavqilCEHK 134
Cdd:PHA02798 126 EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKeKYDTLH--------------CYFK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 135 SPINLKDLDgniplllavqnghseICHFLLDHGADVNSRNKSGRTALM--LACEIGSSNAVEA----LIKKGADLNLVDS 208
Cdd:PHA02798 192 YNIDRIDAD---------------ILKLFVDNGFIINKENKSHKKKFMeyLNSLLYDNKRFKKnildFIFSYIDINQVDE 256
|
170 180
....*....|....*....|....
gi 1370488827 209 LGYNALHYSKLSENAGIQSLLLSK 232
Cdd:PHA02798 257 LGFNPLYYSVSHNNRKIFEYLLQL 280
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
141-251 |
6.42e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 141 DLDGNIPLLLAVqnghsEICHF-----------LLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSL 209
Cdd:PTZ00322 73 VIDPVVAHMLTV-----ELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370488827 210 GYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQV 251
Cdd:PTZ00322 148 GKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGK 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-659 |
7.55e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 335 ADQQDLLSLLQAKVASLtlhNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGpslgkpgetSPPDSKSSPSVLIHSLGK 414
Cdd:TIGR02168 687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLA---------RLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 415 STTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLKETQSKYEEAMKEVLSV 494
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 495 QKQMKLGLVSPESMDNyshfhELRVTEEEInvlkQDLQNALEESERNKEKV-RELEEKLVEREKGTV-IKPPVEEYEEMK 572
Cdd:TIGR02168 830 ERRIAATERRLEDLEE-----QIEELSEDI----ESLAAEIEELEELIEELeSELEALLNERASLEEaLALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 573 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLK----------DTLKSQMTQEASDEAEDMKEAMN----------RMIDE 632
Cdd:TIGR02168 901 EE----LRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENkieddeeearRRLKR 976
|
330 340
....*....|....*....|....*..
gi 1370488827 633 LNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYD 1003
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
614-883 |
7.94e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 614 EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYR-KRKSLEDVTAEYIHKA-EHEKLMQLTNVSRAKAEDAL 691
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAeKRDELNAQVKELREEAqELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 692 SEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVI--------TTLRTAAKEME--EKISNLKEHLASKEvEVAKLE 761
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKElvEKIKELEKELEKAK-KALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 762 KQLLEEKAAMTDamvprssyeklqssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEV 841
Cdd:COG1340 160 EKLKELRAELKE--------------LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370488827 842 NELLQKFQQAQEELAEM----KRYAESSSKLEEDKDKKINEMSKEV 883
Cdd:COG1340 226 DELHEEIIELQKELRELrkelKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
422-665 |
8.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNT--EISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK 499
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLVSPESMDNYSHFhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgtvikppvEEYEEMKSSycsvI 579
Cdd:COG4942 108 ELLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------------AELAALRAE----L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 580 ENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEamnrmIDELNKQVSELSQLYKEAQAELEDYRKRKS 659
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE-----LAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*.
gi 1370488827 660 LEDVTA 665
Cdd:COG4942 245 AAGFAA 250
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
542-790 |
1.07e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEmksSYCSVIENMNK--EKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEA 619
Cdd:PRK05771 15 KSYKDEVLEALHELGVVHIEDLKEELSNE---RLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNRMIDELNKQVSEL----SQLYKEAQA---------ELEDYRKRKSLeDVTAEYIHKAEHEKLMQLTN----- 681
Cdd:PRK05771 92 EEELEKIEKEIKELEEEISELeneiKELEQEIERlepwgnfdlDLSLLLGFKYV-SVFVGTVPEDKLEELKLESDvenve 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 682 -VSRAKAED-----ALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEH-----L 750
Cdd:PRK05771 171 yISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKyleelL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370488827 751 ASKEVEVAKLEKQLLEEKAAMTD------AMVPRSSYEKLQSSLES 790
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKTDktfaieGWVPEDRVKKLKELIDK 296
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-862 |
1.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 413 GKSTTDNDVRIQQLQEILqdlqKRLESSEAERKQLQVELQSRRAELvclnnTEISENSSDLSQKLK--ETQSKYEEAMKE 490
Cdd:COG4717 63 GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEEL-----EELEAELEELREELEklEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 491 VLSVQKQMKlglvspesmDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTvIKPPVEEYEE 570
Cdd:COG4717 134 LEALEAELA---------ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 571 MKSSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA- 649
Cdd:COG4717 204 LQQR----LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 650 ----------ELEDYRKRKSLEDVTAEYIHKAEHEKLMQLtNVSRAKAEDALSEM--KSQYSKVLNELTQLKQLVD--AQ 715
Cdd:COG4717 280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-ELEELLAALGLPPDlsPEELLELLDRIEELQELLReaEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 716 KENSVSITEHLQVITTLRTAAK----EMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSsyeklQSSLESE 791
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 792 VSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKrekeniqtllksKEQEVNELLQKFQQAQEELAEM-KRYA 862
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKAELRELaEEWA 493
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
27-85 |
1.24e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 27 ARRGPVPPNTTvrarPRKLKHCFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLA 85
Cdd:pfam13857 2 LEHGPIDLNRL----DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
426-872 |
1.41e-05 |
|
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: 48.95 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLnnTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvsp 505
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM--TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 506 esmdnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEE---KLVEREKGTVIKPPVEEYEEMKSSYCSVIEN- 581
Cdd:pfam05483 433 ----------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhylKEVEDLKTELEKEKLKNIELTAHCDKLLLENk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 -MNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQeasdeAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrKSL 660
Cdd:pfam05483 503 eLTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 EDVTAEYIHKAEHEKLMQLTnvsrakaEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITT--------L 732
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKIL-------ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIkvnkleleL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 733 RTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESV-KEKEKVHS 811
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYdKIIEERDS 725
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 812 EVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDK 872
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
143-171 |
1.44e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.57 E-value: 1.44e-05
10 20
....*....|....*....|....*....
gi 1370488827 143 DGNIPLLLAVQNGHSEICHFLLDHGADVN 171
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
541-934 |
1.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 541 NKEKVRELEEK------LVEREkgtVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyqeaqeEIMKLKDTLKSQMTQE 614
Cdd:PTZ00121 1025 NIEKIEELTEYgnnddvLKEKD---IIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDF------DFDAKEDNRADEATEE 1095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 615 ASDEAEDMKEAMNRMIDELNKQvselsqlyKEAQAELEDYRK----RKSLEDVTAEYIHKAEHEKLMQLTNvsraKAEDA 690
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIAR----KAEDA 1163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 691 LSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAakEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAA 770
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 771 MTDAMVPRSSYEKLQssLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSqvkrekeniqtllKSKEQEVNELLQKFQQ 850
Cdd:PTZ00121 1242 AKKAEEERNNEEIRK--FEEARMAHFARRQAAIKAEEARKADELKKAEEKK-------------KADEAKKAEEKKKADE 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 851 AQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQ 930
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
....
gi 1370488827 931 HQEV 934
Cdd:PTZ00121 1387 AEEK 1390
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-926 |
2.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 620 EDMKEAMNR---MIDELNKQVSELsqlykEAQAEL-EDYRK-RKSLEDVTAEYIHKAEHEKLMQLtnvsrAKAEDALSEM 694
Cdd:COG1196 182 EATEENLERledILGELERQLEPL-----ERQAEKaERYRElKEELKELEAELLLLKLRELEAEL-----EELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 695 KSQyskvLNELTQLKQLVDAQKEnsvsitehlqvitTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQlleekaamtda 774
Cdd:COG1196 252 EAE----LEELEAELAELEAELE-------------ELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 mvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEE 854
Cdd:COG1196 304 ---IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 855 LAEMKR-YAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAE 926
Cdd:COG1196 381 LEELAEeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
687-859 |
2.11e-05 |
|
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: 47.75 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKQLVDaQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATD-DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTD------AMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKvhsevvQIRSEVSQVKREKeNIQTLLKSKEQE 840
Cdd:cd22656 161 LEKALKDlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA------LIADDEAKLAAAL-RLIADLTAADTD 233
|
170
....*....|....*....
gi 1370488827 841 VNELLQKFQQAQEELAEMK 859
Cdd:cd22656 234 LDNLLALIGPAIPALEKLQ 252
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
423-860 |
2.17e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSS-DLSQKLKETQSKYEEAMKE--VLSVQKQMK 499
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSqDEESDLERLKEEIEKSSKQraMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 LGLVSPESMDNYS---HFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEyeemkssyc 576
Cdd:TIGR00606 666 SQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ--------- 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 577 SVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ----EASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELE 652
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 653 DYRKRKSLEDVTAEYIHKAEH-----------EKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVS 721
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHEldtvvskielnRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 722 ITEHLQVI-----------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAM-VPRSSYEKLQSSLE 789
Cdd:TIGR00606 897 VQSLIREIkdakeqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEnKIQDGKDDYLKQKE 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 790 SEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------------------SQVKREKENIQTLLKS-KEQEVNELLQKF 848
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqerwlqdnltlrkreNELKEVEEELKQHLKEmGQMQVLQMKQEH 1056
|
490
....*....|..
gi 1370488827 849 QQAQEELAEMKR 860
Cdd:TIGR00606 1057 QKLEENIDLIKR 1068
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
651-891 |
3.75e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 651 LEDYRKRksledvTAEYIHKaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQK-----ENSVSITEH 725
Cdd:PRK05771 14 LKSYKDE------VLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 726 LQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKaamtdamvprsSYEKLQSSLESE-----VSVLASKLK 800
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-----------PWGNFDLDLSLLlgfkyVSVFVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 801 ESVKEKEKVHSEVvqirsEVSQVKREKENIQTL----LKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEdkdkKI 876
Cdd:PRK05771 154 EDKLEELKLESDV-----ENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKE----EL 224
|
250
....*....|....*
gi 1370488827 877 NEMSKEVTKLKEALN 891
Cdd:PRK05771 225 EEIEKERESLLEELK 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
411-890 |
4.54e-05 |
|
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: 47.53 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESseaERKQLQVELQSRRAELvclnNTEISENSSDLSQK------LKETQSKY 484
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERQETSAELNQ---LLRTLDDQWKEKRDEL----NGELSAADAAVAKDrseleaLEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 485 EEAMKEVLSvQKQMKLGLVSPEsMDNYSHFHELRVT-----EEEINVLKQDLqnaleeSERNKEKVRELEEKLVEREKGT 559
Cdd:pfam12128 335 LDADIETAA-ADQEQLPSWQSE-LENLEERLKALTGkhqdvTAKYNRRRSKI------KEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 560 VIKPPVEE--YEEMKSSYCSVIENMNKEkaflfekYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNrmIDELNKQV 637
Cdd:pfam12128 407 DRQLAVAEddLQALESELREQLEAGKLE-------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--DERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 638 SELSQLYKE---AQAELEDYRKRKSLEDVTAEYIHKAEHE---KLMQLTNVSRAKAEDALSEMKSQ-------YSKVLN- 703
Cdd:pfam12128 478 EEQEAANAEverLQSELRQARKRRDQASEALRQASRRLEErqsALDELELQLFPQAGTLLHFLRKEapdweqsIGKVISp 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 704 EL---TQLKQLVD----AQKENSVSITEHLQVI---------TTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEE 767
Cdd:pfam12128 558 ELlhrTDLDPEVWdgsvGGELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 768 KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKE-KEKVHSEVVQIRSEVSQVKREkenIQTLLKSKEQEVNELLQ 846
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREART 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1370488827 847 KFQQAQEElaemkryaessskLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam12128 715 EKQAYWQV-------------VEGALDAQLALLKAAIAARRSGA 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
458-690 |
5.49e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 458 LVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNyshfhELRVTEEEINVLKQDLQNALEE 537
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 538 SERNKEKVRELEEKLVEReKGTVIKPPVEEYEEMKSSYCSVI---ENMNK--EKAFLFEKYQEA-QEEIMKLKDTLKSQM 611
Cdd:COG4942 85 LAELEKEIAELRAELEAQ-KEELAELLRALYRLGRQPPLALLlspEDFLDavRRLQYLKYLAPArREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 612 TQEAsdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDA 690
Cdd:COG4942 164 ALRA--ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
423-696 |
5.73e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 423 IQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN----------------TEISENSSDLSQKLKETQSKYEE 486
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkelreeaqelrekrDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 487 AMKEVLSVQKQMKLGLVSPESMDNyshfhelrvTEEEINVLKQDLQNA---LEESERNKEKVRELEEKLVEREKGTVIKp 563
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDK---------LRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 564 pvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLksqmtQEASDEAEDMKE---AMNRMIDELNKQVSEL 640
Cdd:COG1340 160 --EKLKELRAELKELRKEAEE----IHKKIKELAEEAQELHEEM-----IELYKEADELRKeadELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 641 SQLYKEAQAELEDYRKrksledVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKS 696
Cdd:COG1340 229 HEEIIELQKELRELRK------ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
422-717 |
6.89e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVclnNTEISENS-----SDLSQKLKETQSK---YEEAMKEVLS 493
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE---AAEEEVDSlksqlADYQQALDVQQTRaiqYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 494 VQKQMKLGLVSPESMDNYshFHELRVTEEEIN----VLKQDLQNAlEESERNKEKVRELEEKL---VEREK-GTVIKPPV 565
Cdd:COG3096 425 ARALCGLPDLTPENAEDY--LAAFRAKEQQATeevlELEQKLSVA-DAARRQFEKAYELVCKIageVERSQaWQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 566 EEYeemkSSYCSVIENMNKEKAFLFEKYQ--EAQEEIMKLKDTLKSQMTQE--ASDEAEDMKEAMNRMIDELNKQVSELS 641
Cdd:COG3096 502 RRY----RSQQALAQRLQQLRAQLAELEQrlRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAV 577
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370488827 642 QLYKEAQAELEDYR-KRKSLEDVTAEYIHKAEH-EKLMQLTNVSRAKAEDALSEMKSQYSKvLNELTQLKQLVDAQKE 717
Cdd:COG3096 578 EQRSELRQQLEQLRaRIKELAARAPAWLAAQDAlERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQ 654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
605-854 |
7.42e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 605 DTLKSQMTQEASDEAEDMKEAMNRmIDELNKQVSELSQLYKEAQAELEDyrKRKSLEDVTAEyIHKAEHEklmqltnvsR 684
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEA--LQAEIDKLQAE-IAEAEAE---------I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 685 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQkensvSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQL 764
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 765 LEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL 844
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 1370488827 845 LQKFQQAQEE 854
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
512-890 |
7.54e-05 |
|
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: 46.66 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 512 SHFHELRVTEEEINVLKQDLQnalEESERNKE---KVRELEEKLVEREKGtvikppveeyeemkssycsvienmNKEKAF 588
Cdd:pfam05557 24 EHKRARIELEKKASALKRQLD---RESDRNQElqkRIRLLEKREAEAEEA------------------------LREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 589 LFEKYQEAQEEIMKLKDTLKSQMTqeasdEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYI 668
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLA-----DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HK--AEHEKLMQLTNVSRAKAEDALSEMKSQyskvlnelTQLKQLVDAQKENSVSITEHLQVITTLRtaakEMEEKISNL 746
Cdd:pfam05557 152 EQlrQNLEKQQSSLAEAEQRIKELEFEIQSQ--------EQDSEIVKNSKSELARIPELEKELERLR----EHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 747 KEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKeKEKVHSEVVQIRSEVSQVKRE 826
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS-PEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 827 KENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
633-891 |
8.44e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 633 LNKQVSE-LSQLYKEAQAELEDYRKRKSledvtAEYIHKAEHEklmqltnvsRAKAEDALSEMKSqYSKVLNELTQLKQL 711
Cdd:PRK05771 14 LKSYKDEvLEALHELGVVHIEDLKEELS-----NERLRKLRSL---------LTKLSEALDKLRS-YLPKLNPLREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 712 VDAQKENSV--SITEHLQVIttlRTAAKEMEEKISNLKEHLASKEVEVAKLE---------KQLLEEK-AAMTDAMVPRS 779
Cdd:PRK05771 79 VSVKSLEELikDVEEELEKI---EKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlSLLLGFKyVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 SYEKLQSSLESEVSVLASKLKESV-------KEKEKVHSEVV---------------------QIRSEVSQVKREKENIQ 831
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELkklgferleleeegtpselirEIKEELEEIEKERESLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 832 TLLKSKEQEVNELLqkfQQAQEELAEMKRYAESSSKLEEDKDKKINE---MSKEVTKLKEALN 891
Cdd:PRK05771 236 EELKELAKKYLEEL---LALYEYLEIELERAEALSKFLKTDKTFAIEgwvPEDRVKKLKELID 295
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
177-204 |
8.80e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.32 E-value: 8.80e-05
10 20
....*....|....*....|....*...
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLN 204
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
53-133 |
1.05e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 53 AAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCE 132
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
.
gi 1370488827 133 H 133
Cdd:PTZ00322 170 H 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
468-860 |
1.07e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 468 ENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSH-FHELRVTEEEINVLKQDLQNALEESERNKEKVR 546
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 547 ELEEKLVEREKGTVIKPP--VEEYEEMKSS---YCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQM------TQEA 615
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDaiKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgEEKS 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 616 SDEAEDMKEAMNRMIDELNKQVSELSQLYKEA--QAELEDYRKRKSLEDVTAEY--IHKAEHEKLMQLTNVSRAK-AEDA 690
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYnkIESARADLEDIKIKINELKdKHDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 691 LSEMKSQY---------SKVLNELTQLKQLVDAQKENSVSITEhlQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLE 761
Cdd:PRK01156 548 YEEIKNRYkslkledldSKRTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 762 KQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLAsKLKESVKEKEKVHSEVVQIRSEVSQVKREKENI-------QTLL 834
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTI 704
|
410 420
....*....|....*....|....*.
gi 1370488827 835 KSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMKK 730
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
177-207 |
1.38e-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: 1.38e-04
10 20 30
....*....|....*....|....*....|..
gi 1370488827 177 GRTALMLACEI-GSSNAVEALIKKGADLNLVD 207
Cdd:pfam00023 2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
46-188 |
1.67e-04 |
|
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: 45.46 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 46 KHCFHlAAAKGHV----ECLRVMITHGVD------VTAQDTT----GHSALHLAAKNSHHECIRKLLQSK-------CPA 104
Cdd:TIGR00870 83 DTLLH-AISLEYVdaveAILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGasvparaCGD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 105 ESVDSSGKTALHY-------AAAQGCLQAVQILCEHKSPINLKDLDGNIPL-LLAVQNGHSE-----ICH---FLLDHGA 168
Cdd:TIGR00870 162 FFVKSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADSLGNTLLhLLVMENEFKAeyeelSCQmynFALSLLD 241
|
170 180
....*....|....*....|....*..
gi 1370488827 169 DVNS-------RNKSGRTALMLACEIG 188
Cdd:TIGR00870 242 KLRDskeleviLNHQGLTPLKLAAKEG 268
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
471-699 |
1.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 471 SDLSQKLKETQSKYEEAMKEVLSVQKQMKlglvspesmdnyshfhelrVTEEEINVLKQDLQNALEESERNKEKVRELEE 550
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELE-------------------ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 551 KLVEREkgtvikppvEEYEE-MKSSY------------------------CSVIENMNKEKAFLFEKYQEAQEEIMKLKD 605
Cdd:COG3883 80 EIEERR---------EELGErARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 606 TLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRA 685
Cdd:COG3883 151 ELEAKL-----AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|....
gi 1370488827 686 KAEDALSEMKSQYS 699
Cdd:COG3883 226 AAAAAAAAAAAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-858 |
2.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 613 QEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSledVTAEYIHKAEH-----EKLMQLTNVSRAKA 687
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQelaalEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 688 EDALSEMKSQYSKVLNELTQLKQLVDAQ-KENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLAskevEVAKLEKQLLE 766
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKaamtdamvprssyeklqsslesevsvlasklkesvKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:COG4942 172 ER-----------------------------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250
....*....|..
gi 1370488827 847 KFQQAQEELAEM 858
Cdd:COG4942 217 ELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
418-674 |
2.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNteiSENSSDLSQKLKETQSKYEEAMKEVLSVQKq 497
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR---LAEYSWDEIDVASAEREIAELEAELERLDA- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 498 mklglvspeSMDnyshfhELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppvEEYEEMKSSYCS 577
Cdd:COG4913 683 ---------SSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE---------EELDELQDRLEA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 578 VIENMNKEKAFLFEKYQEAQeeimkLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAEL------ 651
Cdd:COG4913 739 AEDLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLdadles 813
|
250 260
....*....|....*....|....
gi 1370488827 652 -EDYRKRksLEDVTAEYIHKAEHE 674
Cdd:COG4913 814 lPEYLAL--LDRLEEDGLPEYEER 835
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
122-206 |
2.58e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.57 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 122 GCLQAVQILCEHKSP-INLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKG 200
Cdd:PHA02874 12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
....*.
gi 1370488827 201 ADLNLV 206
Cdd:PHA02874 92 VDTSIL 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-891 |
2.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNtEISENSSD----LSQKLKETQSKYEEAMKEVLSVQKQ 497
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDrleqLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 498 MK-LGLVSPESMDNY-SHFHELRVTEEEINVLKQDLQNALEESERNKEKVR-ELEEKLVERE----KGTVIkPPveEYEE 570
Cdd:COG4913 368 LAaLGLPLPASAEEFaALRAEAAALLEALEEELEALEEALAEAEAALRDLRrELRELEAEIAslerRKSNI-PA--RLLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 571 MKSSYCSVIENMNKEKAFL----------------FEK---------------YQEAQEEI-----------MKLKDTLK 608
Cdd:COG4913 445 LRDALAEALGLDEAELPFVgelievrpeeerwrgaIERvlggfaltllvppehYAAALRWVnrlhlrgrlvyERVRTGLP 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 609 SQMTQEASDE--AEDMKEAMNRMIDELNKQVSELSQLYK-EAQAELEDYRKRksledVTAE---YIHKAEHEKLMQLTNV 682
Cdd:COG4913 525 DPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRA-----ITRAgqvKGNGTRHEKDDRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 683 SR----AKAEDALSEMKSQYSKVLNELTQLKQLVDAqkensvsITEHLQVITTLRTAAKEMEEKISNLKEhLASKEVEVA 758
Cdd:COG4913 600 SRyvlgFDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEID-VASAEREIA 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 759 KLEKQLleekaamtdamvprssyEKLQSSlESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 838
Cdd:COG4913 672 ELEAEL-----------------ERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 839 QEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKInemSKEVTKLKEALN 891
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLN 783
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
424-909 |
3.23e-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: 44.71 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisenSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLV 503
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-----------HFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 504 spesmdnyshfhelRVTEEEINVlkQDLQNALEESernKEKVRELEEK--LVEREKGTVIKPPVEEYEEMKSSYCSVIEN 581
Cdd:pfam05483 248 --------------QITEKENKM--KDLTFLLEES---RDKANQLEEKtkLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAfLFEKYQEAQEEIMKLKDTLKSQMtqeasDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyRKRKSLE 661
Cdd:pfam05483 309 MSTQKA-LEEDLQIATKTICQLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE--KNEDQLK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 662 DVTAEYIHKA-EHEKLMQLTNVSRAKAEDaLSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV-----------I 729
Cdd:pfam05483 381 IITMELQKKSsELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekeihdleiqL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 730 TTLRTAAKEMEEKISNLKEHLASKEVEVAKL----------EKQLLEEKAAMTDAMVPRS----SYEKLQSSLESEVSVL 795
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 796 ASKLKESVKEKEKVHSEVVQIRSEVS-QVKREKENIQTL----------LKSKEQEVNELLQK-------FQQAQEELAE 857
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIeyevlkkekqMKILENKCNNLKKQienknknIEELHQENKA 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 858 MKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
411-655 |
3.28e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQvelqsRRAELVCLNNTE--ISENSSDLSQKLKETQSKYEEAM 488
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAklLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 489 KEVLSVQKQMKLGLVSPESMDNYSHFHELRvteEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgtvikppveey 568
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 569 EEMKSSYCSVIENMNKEKAFLfekyQEAQEEIMKLKDTLKSQMTQEASDEAEdmkeamnrmIDELNKQVSELSQLYKEAQ 648
Cdd:COG3206 305 AQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAE---------LRRLEREVEVARELYESLL 371
|
....*..
gi 1370488827 649 AELEDYR 655
Cdd:COG3206 372 QRLEEAR 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
465-887 |
3.43e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 465 EISENSSDLSQKLKETQSKYEEAM----KEVLSVQKQMKLGLVSPESMdnyshfHELRVTEEEInvlKQDLQNALEESER 540
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAM------ADIRRRESQS---QEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 541 NKEKVRELEEKLVEREKGTVikppvEEYEEMKSSYCSVIENMNKekafLFEKYQEAQEEIMKLKDTLKSQmtqeasdEAE 620
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQI-----EQLRKMMLSHEGVLQEIRS----ILVDFEEASGKKIYEHDSMSTM-------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 621 DMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYrkrKSLEDVTAEYIHKAEHEKLMQLtnVSRAKAE-DALSEMKSQYS 699
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEAL---KSESQNKIELLLQQHQDRIEQL--ISEHEVEiTGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 700 KVLNELTQLKQLVDAQKENSVSIteHLQVITTLRTAAKEMEekiSNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRS 779
Cdd:pfam15921 292 SQANSIQSQLEIIQEQARNQNSM--YMRQLSDLESTVSQLR---SELREAKRMYEDKIEELEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 SYEKLQSSLESEVSVLASKL----KESVKEKEKVHS----------EVVQIRSEVSQVKREKENIQTLLKSKEQEV---- 841
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECqgqm 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 842 ----------NELLQK--------------FQQAQEELAEMKRYAESSSKLEED-------KDKKINEMSKEVTKLK 887
Cdd:pfam15921 447 erqmaaiqgkNESLEKvssltaqlestkemLRKVVEELTAKKMTLESSERTVSDltaslqeKERAIEATNAEITKLR 523
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
409-789 |
3.59e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 469
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRELRKTLlanrfsygPAIDELEKQLA-EIEEEFSQFEELTESgdylearevleKLEEE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 470 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALEESERNK 542
Cdd:pfam06160 188 TDALEELmedipplYEELKTELPDQLEELKEGYREME--------EEGY-ALEHLNV-DKEIQQLEEQLEENLALLENLE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 543 -EKVRELEEKLVERekgtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLF---EKYQEAQEEIMKLKDT-LKSQMTQEASD 617
Cdd:pfam06160 258 lDEAEEALEEIEER-----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEhaeEQNKELKEELERVQQSyTLNENELERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 618 EAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyiHKAEHEKLMQLTNVSRaKAEDALSEMKsq 697
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ--LEEIEEE--QEEFKESLQSLRKDEL-EAREKLDEFK-- 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 698 yskvlNELTQLKQLVdaQKEN----SVSITEHL-QVITTLRTAAKEMEEKISNLKE-----HLASKEVEVAKLEKQLLEE 767
Cdd:pfam06160 406 -----LELREIKRLV--EKSNlpglPESYLDYFfDVSDEIEDLADELNEVPLNMDEvnrllDEAQDDVDTLYEKTEELID 478
|
410 420
....*....|....*....|....*..
gi 1370488827 768 KAAMTDAMVP-----RSSYEKLQSSLE 789
Cdd:pfam06160 479 NATLAEQLIQyanryRSSNPEVAEALT 505
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
177-205 |
3.68e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.68e-04
10 20
....*....|....*....|....*....
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLNL 205
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
424-647 |
4.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQvELQSRRAELvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK---- 499
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyn 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 500 --LGLVSPEsmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtviKPPVEEYEEMKSSYCS 577
Cdd:PRK03918 603 eyLELKDAE--------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLE 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370488827 578 VIENMNKEKAFLfEKYQEAQEEIMKLKDTLKSQMT--QEASDEAEDMKEAMNRMiDELNKQVSELSQLYKEA 647
Cdd:PRK03918 671 LSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEerEKAKKELEKLEKALERV-EELREKVKKYKALLKER 740
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
132-243 |
4.59e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.89 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 132 EHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSS-----NAVEALIKKGADLNLV 206
Cdd:PHA03100 23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370488827 207 DSLGYNALHY--SKLSENAGIQSLLLSKISqDADLKTPT 243
Cdd:PHA03100 103 DNNGITPLLYaiSKKSNSYSIVEYLLDNGA-NVNIKNSD 140
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-864 |
5.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 422 RIQQLQEILQDLQKRLESSEAERKQLQVELQSRraelvclnnTEISENSSDLSQKLKETQSKYEEAMKEVlsvqkqmklg 501
Cdd:pfam01576 20 RQQKAESELKELEKKHQQLCEEKNALQEQLQAE---------TELCAEAEEMRARLAARKQELEEILHEL---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 lvspesmdnyshfhELRVTEEEINVlkQDLQNaleESERNKEKVRELEEKLVEREKGTvikppveeyeemkssycsviEN 581
Cdd:pfam01576 81 --------------ESRLEEEEERS--QQLQN---EKKKMQQHIQDLEEQLDEEEAAR--------------------QK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAFLFEKYQEAQEEIMKLKDTlKSQMTQEASDEAEDMKEAMNRMIDELN--KQVSELSQLYKEAQAELEDYRKRKs 659
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEkaKSLSKLKNKHEAMISDLEERLKKE- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 660 ledvtaeyihkaehEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAA--- 736
Cdd:pfam01576 200 --------------EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkk 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 737 -KEMEEKISNLKEHLASKEVEVAKLEKQ---LLEE----KAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKE- 807
Cdd:pfam01576 266 iRELEAQISELQEDLESERAARNKAEKQrrdLGEElealKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEa 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 808 -------KVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEELAEMKRYAES 864
Cdd:pfam01576 346 qlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELqaeLRTLQQAKQDSEHKRKKLEG 412
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
535-911 |
5.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 535 LEESERNKEKVRELEEKLVEREKgtvikppVEEYEEMKSSYCSVIENMNKEKaflfEKYQEAQEEIMKLKDTLKSQMTQE 614
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEE-------TENLAELIIDLEELKLQELKLK----EQAKKALEYYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 615 ASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEdyrkrkSLEDVTAEYIhkaEHEKLMQLTNVSRAKAEDALSEM 694
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE------KLAQVLKENK---EEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 695 KSQYSKvlneLTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKIsnLKEHLASKEVEVAKLEKQLLEEKAAmtda 774
Cdd:pfam02463 299 KSELLK----LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE--LKELEIKREAEEEEEEELEKLQEKL---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 mvprssyEKLQSSLESEVSVLASKLKESVKEKEKVH---SEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 851
Cdd:pfam02463 369 -------EQLEEELLAKKKLESERLSSAAKLKEEELelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 852 QEELAEMKRYAESSSKLEEDKDKkinEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLE 911
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDE---LELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
591-865 |
5.89e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 591 EKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAM---NRMIDELN--KQVSEL--SQLYKEAQAELEDYRKRKSLEDV 663
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQKFGRSLKakKRFSLLkkETIYLQSAQRVELAERQLQELKI 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 664 TAEyihKAEHEKLMQLTNVSRakaedaLSEMKSQYSKVLNELTQLKqlvdaqkensvsiTEHlqvITTLRTAAKEMEEKI 743
Cdd:COG5022 890 DVK---SISSLKLVNLELESE------IIELKKSLSSDLIENLEFK-------------TEL---IARLKKLLNNIDLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 744 SnlkehlASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLK-----------------ESVKEK 806
Cdd:COG5022 945 G------PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkkelaelskqygalqESTKQL 1018
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 807 EKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEvNELLQKFQQAQEELAEMKRYAESS 865
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLRRENS 1076
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
418-557 |
6.61e-04 |
|
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: 43.28 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN---TEISENSSDLSQKLK--ETQSKYEEamkEVL 492
Cdd:pfam15066 388 DINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNYVHLQEryiTEMQQKNKSVSQCLEmdKTLSKKEE---EVE 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 493 SVQkQMKLGL--VSPESMDNYSHFHELRvtEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK 557
Cdd:pfam15066 465 RLQ-QLKGELekATTSALDLLKREKETR--EQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
147-171 |
6.92e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.01 E-value: 6.92e-04
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
459-887 |
7.30e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 459 VCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMK--------------------LGLVSPESMDN--YSHFHE 516
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfdntlidkineldkafkdASLNDYEAKNNelIKYFND 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTeeeinvLKQDLQNALEESERNKEK-VRELEEKLVEREKG---------TVIKPPVEEYEE-----MKSSYCSVIEN 581
Cdd:TIGR01612 1005 LKAN------LGKNKENMLYHQFDEKEKaTNDIEQKIEDANKNipnieiaihTSIYNIIDEIEKeigknIELLNKEILEE 1078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MN---------KEKA-------FLFEKYQEAQEEIMKLKDTLKS--QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQ- 642
Cdd:TIGR01612 1079 AEinitnfneiKEKLkhynfddFGKEENIKYADEINKIKDDIKNldQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDv 1158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 643 ----LYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAedALSEMKS---QYSKVLNELtqLKQLVDAQ 715
Cdd:TIGR01612 1159 adkaISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKT--SLEEVKGinlSYGKNLGKL--FLEKIDEE 1234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 716 KENSvsitEHLqvittlrtaAKEMEEKISNLKEhLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQS--------- 786
Cdd:TIGR01612 1235 KKKS----EHM---------IKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIiskkhdeni 1300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 787 --------------SLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKR--EKENIQTLLKSKEQEVNELLQKFQQ 850
Cdd:TIGR01612 1301 sdirekslkiiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKN 1380
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1370488827 851 AQEELAE----MKRYAESSSkLEEDK--------DKKINEMSKEVTKLK 887
Cdd:TIGR01612 1381 IKDELDKseklIKKIKDDIN-LEECKskiestldDKDIDECIKKIKELK 1428
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
411-860 |
9.60e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 411 SLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclnnteisensSDLSQKLKETQSKYEEAMKE 490
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL------------ESVSSLLNEAEGKNIKLSKD 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 491 VLSVQKQMK--LGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNAlEESERNKEK-VRELEEKLVE-REKGTVIKPPVE 566
Cdd:pfam01576 463 VSSLESQLQdtQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE-EEAKRNVERqLSTLQAQLSDmKKKLEEDAGTLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 567 EYEEMKSSYCSVIENMN---KEKAFLFEKYQEA----QEEIMKLKDTLKSQMT--------------------------Q 613
Cdd:pfam01576 542 ALEEGKKRLQRELEALTqqlEEKAAAYDKLEKTknrlQQELDDLLVDLDHQRQlvsnlekkqkkfdqmlaeekaisaryA 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 614 EASDEAE-DMKE------AMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHeklmqltnvSRAK 686
Cdd:pfam01576 622 EERDRAEaEAREketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHELER---------SKRA 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKqlvDAQkensvsitehLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAK----LEK 762
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATE---DAK----------LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKqvreLEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 763 QLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVN 842
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836
|
490
....*....|....*...
gi 1370488827 843 ELLQKFQQAQEELAEMKR 860
Cdd:pfam01576 837 NLEAELLQLQEDLAASER 854
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
177-230 |
1.10e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 177 GRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLL 230
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
46-73 |
1.33e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 1.33e-03
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
409-653 |
1.44e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELV------CLNNTEISENS-----SDLSQKL 477
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLeltrvnELLKAKFSEDGtqkkmSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 478 KETQSKYEEAMKEVLSVQKQMKLGLvspesmdnyshfhelrvteeeinvlkQDLQNALEESernKEKVRELEEKLVEREK 557
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGKL--------------------------QVTQKNLEHS---KGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 558 GTVikppVEEYEEMKssycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQV 637
Cdd:pfam15905 213 EKI----EEKSETEK------LLEYITELSCVSEQVEKYKLDIAQLEELLK-----EKNDEIESLKQSLEEKEQELSKQI 277
|
250
....*....|....*.
gi 1370488827 638 SELSQLYKEAQAELED 653
Cdd:pfam15905 278 KDLNEKCKLLESEKEE 293
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
527-891 |
1.50e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 527 LKQDLQNALEESERNKEKVRELEEKlverekgtvIKPPVEEYEEmkssycSVIEnMNKEKAFLFEKYQEAQEEIM---KL 603
Cdd:TIGR01612 538 LYKEIEAGLKESYELAKNWKKLIHE---------IKKELEEENE------DSIH-LEKEIKDLFDKYLEIDDEIIyinKL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 604 KDTLKSQMtQEASDEAEDMKEAM---------NRMIDELNK----QVSE----LSQLYKEAQAELEDYRKrkslEDVTAE 666
Cdd:TIGR01612 602 KLELKEKI-KNISDKNEYIKKAIdlkkiiennNAYIDELAKispyQVPEhlknKDKIYSTIKSELSKIYE----DDIDAL 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 667 YIHKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSitEHLQVITTLRTAA-KEMEEKIS 744
Cdd:TIGR01612 677 YNELSSIVKENAIDNTEdKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKN--ELLDIIVEIKKHIhGEINKDLN 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 745 NLKEHLASKEVEVAKLEKQLLEEKAAMTdamVPRSSYEKLQSSLESEVSVLASKLKESVK--EKEKVHSEVVQIRS-EVS 821
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELN---KYKSKISEIKNHYNDQINIDNIKDEDAKQnyDKSKEYIKTISIKEdEIF 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 822 QVKREKENIQTLLKSKEQEV----NELLQKFQQAQEELAEM--KRYAESSSKLEEDKDKK-------INEMSKEVTKLKE 888
Cdd:TIGR01612 832 KIINEMKFMKDDFLNKVDKFinfeNNCKEKIDSEHEQFAELtnKIKAEISDDKLNDYEKKfndskslINEINKSIEEEYQ 911
|
...
gi 1370488827 889 ALN 891
Cdd:TIGR01612 912 NIN 914
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
582-860 |
1.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 582 MNKEKAF-LFEKYQEAQEeIMKLKDTLKSQMTqeasdEAEDMKEAmnrmIDELNKQVSELSQLYKEAqaeLEDYRKRKSL 660
Cdd:COG4913 188 IGSEKALrLLHKTQSFKP-IGDLDDFVREYML-----EEPDTFEA----ADALVEHFDDLERAHEAL---EDAREQIELL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 EDVTAEY-------IHKAEHEKLMQLTNVSRAKAEDALSEmksqyskvlNELTQLKQLVDAQKENsvsitehlqvITTLR 733
Cdd:COG4913 255 EPIRELAeryaaarERLAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAE----------LERLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 734 TAAKEMEEKISNLKEHLASKEVE-VAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKEsvkekekvhse 812
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA----------- 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370488827 813 vvqirsEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKR 860
Cdd:COG4913 385 ------LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
152-222 |
1.60e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.36 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370488827 152 VQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN 222
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
426-891 |
1.68e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 426 LQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLN-NTEISENSSDLSQKLKET---QSKYEEAMKEVLSVQKQMKLG 501
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETeEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVSPESMD------NYSHFHELRVT-EEEINVLKQDLQNAL-EESERNKEKVRELEEKL------VEREKGTVIKPPVEE 567
Cdd:COG5022 879 LAERQLQElkidvkSISSLKLVNLElESEIIELKKSLSSDLiENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNK 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 568 YEEMKSSY---CSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQ-EASDEAEDMKEAMNRMIDELNKqvseLSQL 643
Cdd:COG5022 959 LHEVESKLketSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQyGALQESTKQLKELPVEVAELQS----ASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 644 YKEAQAELedyRKRKSLEDVTAEYIhKAEHEKLMQLTNVS-RAKAEDALSEMKSQYSKVLNELTQLKQL-VDAQKENSVS 721
Cdd:COG5022 1035 ISSESTEL---SILKPLQKLKGLLL-LENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKdLEVTNRNLVK 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 722 ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEK-QLLEEKAAMTDAMVPRSSYEKLQSSLESEvSVLASKLK 800
Cdd:COG5022 1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVlQLELDGLFWEANLEALPSPPPFAALSEKR-LYQSALYD 1189
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 801 ESVKEKekvHSEVVQIRSEVSqvkrekeniqtLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMS 880
Cdd:COG5022 1190 EKSKLS---SSEVNDLKNELI-----------ALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS 1255
|
490
....*....|.
gi 1370488827 881 KEVTKLKEALN 891
Cdd:COG5022 1256 MSNEKLLSLLN 1266
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
583-909 |
1.84e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 583 NKEKAFLFEKYQEAQEEIMKLKDTLKsqmtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLED 662
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLR----LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 663 VTAEYIHKAEHEKLMqltnvsrAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEK 742
Cdd:COG5185 317 QLAAAEAEQELEESK-------RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 743 ISNLKEHLASkevevAKLEKQLLEEKAAMTDAMVPRSSyEKLQSSLESevsvLASKLKESVKEKEKVHSEVVQIRSEVSQ 822
Cdd:COG5185 390 KESLDEIPQN-----QRGYAQEILATLEDTLKAADRQI-EELQRQIEQ----ATSSNEEVSKLLNELISELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 823 VKREK--ENIQTLLKSKEQEVNELLQKFQQAQEELAEMKryaESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYST 900
Cdd:COG5185 460 ESQSRleEAYDEINRSVRSKKEDLNEELTQIESRVSTLK---ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYA 536
|
....*....
gi 1370488827 901 SSSKRQSQQ 909
Cdd:COG5185 537 HILALENLI 545
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
94-239 |
1.88e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.18 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 94 IRKLLQSKcPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLkdLDGNIPLLLAVQNGHSEICHFLLDHGADVNSR 173
Cdd:PHA02791 14 LKSFLSSK-DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 174 NKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGY-NALHYSKLSENAGIQSLLLSKISQDADL 239
Cdd:PHA02791 91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
516-657 |
2.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 516 ELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREK--GTVIKPpvEEYEEMKSSycsvIENMNKEKAFLFEKY 593
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNN--KEYEALQKE----IESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370488827 594 QEAQEEIMKLKDTLKsqmtqEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKR 657
Cdd:COG1579 113 LELMERIEELEEELA-----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
702-857 |
2.07e-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: 41.80 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 702 LNELTQLKQLVDAQKENSVSitEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQ----------LLEEKAAM 771
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKE--RYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelsasseeLSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 772 TDAmvpRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQA 851
Cdd:pfam07888 121 LAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
....*.
gi 1370488827 852 QEELAE 857
Cdd:pfam07888 198 RNSLAQ 203
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
627-806 |
2.36e-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: 40.68 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 627 NRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEyihKAEHEKLMQLTNVSRAKAEDALSEMKS--QYSKVLNE 704
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKE---IKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 705 LTQLKQLvdaqkensvsitehlqvITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvprSSYEKL 784
Cdd:COG1579 98 IESLKRR-----------------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAE 157
|
170 180
....*....|....*....|..
gi 1370488827 785 QSSLESEVSVLASKLKESVKEK 806
Cdd:COG1579 158 LEELEAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
424-912 |
2.37e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQVELQsrraelvclnNTEISENSSDLSQKLKETQSKYEEAMKEVLSvqkqmklglv 503
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQ----------QTQQSHAYLTQKREAQEEQLKKQQLLKQLRA---------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 504 spesmdnyshfhelrvTEEEINVLKQDLQNALEESERNKEKvreleEKLVEREKGtvikppVEEYEEMKSSYCSVIENMN 583
Cdd:TIGR00618 268 ----------------RIEELRAQEAVLEETQERINRARKA-----APLAAHIKA------VTQIEQQAQRIHTELQSKM 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 584 KEKAFLFEKYQEAQEEIMKLKDTLKS-QMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSL-- 660
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLck 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 661 -------EDVTAEYIHKAEHEKLMQLTnVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLR 733
Cdd:TIGR00618 401 eldilqrEQATIDTRTSAFRDLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 734 TAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQsSLESEVSVLAsklkesvKEKEKVHSEV 813
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-RGEQTYAQLE-------TSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 814 VQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEedkDKKINEMSKEVTKLKEALNSL 893
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DMLACEQHALLRKLQPEQDLQ 628
|
490
....*....|....*....
gi 1370488827 894 SQLSYSTSSSKRQSQQLEA 912
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTA 647
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
418-840 |
2.44e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 418 DNDVRIQQ---LQEILQDL-QKRLESSEaERKQLQVELQSRRAELvcLNNT-----EISENSSDLSQKLKetqskyeeam 488
Cdd:PTZ00108 967 DENGKIKKysdALDILKEFyLVRLDLYK-KRKEYLLGKLERELAR--LSNKvrfikHVINGELVITNAKK---------- 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 489 KEVLSVQKQMKLGLVSP-ESMDNYSHFHELRVTEEEINVLKQDLQNALEESERN-------------KEKVRELEEKLVE 554
Cdd:PTZ00108 1034 KDLVKELKKLGYVRFKDiIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAELEK 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 555 REKgtvikppveEYEEMKSsycSVIENMNKekaflfekyqeaqEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELN 634
Cdd:PTZ00108 1114 KEK---------ELEKLKN---TTPKDMWL-------------EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 635 KQVSELSQLyKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDalsemKSQYSKVLNELTQLKQLVDA 714
Cdd:PTZ00108 1169 LRKPKLKKK-EKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG-----SDQEDDEEQKTKPKKSSVKR 1242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 715 QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAamTDAMVPRSSYEKLQSSLESEVSV 794
Cdd:PTZ00108 1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVKKRLEGSLAA 1320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1370488827 795 LASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQE 840
Cdd:PTZ00108 1321 LKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
409-769 |
2.59e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRL--------ESSEAERKQLQvELQSRRAELVCLNNT-----------EISEN 469
Cdd:PRK04778 128 LQELLESEEKNREEVEQLKDLYRELRKSLlanrfsfgPALDELEKQLE-NLEEEFSQFVELTESgdyveareildQLEEE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 470 SSDLSQK-------LKETQSKYEEAMKEVLSVQKQMKlglvspesMDNYsHFHELRVtEEEINVLKQDLQNALE-----E 537
Cdd:PRK04778 207 LAALEQImeeipelLKELQTELPDQLQELKAGYRELV--------EEGY-HLDHLDI-EKEIQDLKEQIDENLAlleelD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 538 SERNKEKVRELEEK------LVEREKGTviKPPVEEYEEMKSSYCSVIENMNK----EKAFLFEKYQEAQEEIMKLKdTL 607
Cdd:PRK04778 277 LDEAEEKNEEIQERidqlydILEREVKA--RKYVEKNSDTLPDFLEHAKEQNKelkeEIDRVKQSYTLNESELESVR-QL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 608 KSQMtqeasdeaedmkEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRksLEDVTAEYIHKAEHekLMQLTNvSRAKA 687
Cdd:PRK04778 354 EKQL------------ESLEKQYDEITERIAEQEIAYSELQEELEEILKQ--LEEIEKEQEKLSEM--LQGLRK-DELEA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 688 EDALSEMKsqyskvlNELTQLKQLVdaQKEN----SVSITEHLQVITT-LRTAAKEMEEKISNLKEhlASKEVEVAKLEK 762
Cdd:PRK04778 417 REKLERYR-------NKLHEIKRYL--EKSNlpglPEDYLEMFFEVSDeIEALAEELEEKPINMEA--VNRLLEEATEDV 485
|
....*..
gi 1370488827 763 QLLEEKA 769
Cdd:PRK04778 486 ETLEEET 492
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
517-874 |
2.63e-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: 41.42 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREkgTVIKPPVEEYEEMKSSYCSVI---ENMNKEKAFLFEKY 593
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK--EELRQSREKHEELEEKYKELSassEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 594 QEAQEEIMKLKDTLK--SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL-YKEAQAELEDYRKRKSLEdvtaeyihk 670
Cdd:pfam07888 125 AAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqAKLQQTEEELRSLSKEFQ--------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 671 aeheklmqltnvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHL 750
Cdd:pfam07888 196 ---------------ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 751 AS--------------KEVEVAKLEKQLLEEKAAMTDAmvpRSSY----EKLQSSLESEVSVLASKLKESVKEKEKVHSE 812
Cdd:pfam07888 261 SSmaaqrdrtqaelhqARLQAAQLTLQLADASLALREG---RARWaqerETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 813 VVQIRSEVSQVKREKENIQTLLKSKEQEVNEL---LQKFQQAQEEL-AEMKRYAESSSKLEEDKDK 874
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELkasLRVAQKEKEQLqAEKQELLEYIRQLEQRLET 403
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
529-807 |
2.70e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 529 QDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLK 608
Cdd:pfam09731 124 QEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 609 SQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAqAELEDYRKRKSLEDVtaeyIHKAEHEKLMqlTNVSRAKAE 688
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA-KLVDQYKELVASERI----VFQQELVSIF--PDIIPVLKE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 689 DALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVIttLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEK 768
Cdd:pfam09731 277 DNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERA--LEKQKEELDKLAEELSARL---EEVRAADEAQLRLEF 351
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370488827 769 AAMTDAMvpRSSYE-KLQSSLESEVSVLASKLKESVKEKE 807
Cdd:pfam09731 352 EREREEI--RESYEeKLRTELERQAEAHEEHLKDVLVEQE 389
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
566-887 |
2.88e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 566 EEYEEMKSSYCSVIENmnkekafLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYK 645
Cdd:PRK04778 64 EKFEEWRQKWDEIVTN-------SLPDIEEQLFEAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 646 EAQAE----LEDYRK-RKSLED------VTAEYIHK------AEHEKLMQLTN----------VSRAKAE-DALSEMKSQ 697
Cdd:PRK04778 137 KNREEveqlKDLYRElRKSLLAnrfsfgPALDELEKqlenleEEFSQFVELTEsgdyveareiLDQLEEElAALEQIMEE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 698 YSKVLNELT-----QLKQLVDAQKENSVS--ITEHLQVITTLrtaaKEMEEKISNLKEHLASKEVEVAKLEKQLLEEK-- 768
Cdd:PRK04778 217 IPELLKELQtelpdQLQELKAGYRELVEEgyHLDHLDIEKEI----QDLKEQIDENLALLEELDLDEAEEKNEEIQERid 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 769 ---AAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKV-------HSEVVQIRS---EVSQVKREKENIQTLLK 835
Cdd:PRK04778 293 qlyDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVkqsytlnESELESVRQlekQLESLEKQYDEITERIA 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370488827 836 SKEQEVNELLQKFQQAQEELAEMK----RYAESSSKLEEDKDK---KINEMSKEVTKLK 887
Cdd:PRK04778 373 EQEIAYSELQEELEEILKQLEEIEkeqeKLSEMLQGLRKDELEareKLERYRNKLHEIK 431
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
706-885 |
3.05e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 706 TQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDA----------- 774
Cdd:PHA02562 199 TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskieqfqkvi 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 ------------MVPRSSYEKLQSSLESEVSVLA---SKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQ 839
Cdd:PHA02562 279 kmyekggvcptcTQQISEGPDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370488827 840 EVNELLQKFQQAQeelAEMKRYAESSSKLEEDKDKKINEMSKEVTK 885
Cdd:PHA02562 359 KAKKVKAAIEELQ---AEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
517-887 |
3.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 517 LRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKyQEA 596
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE--IERLSIEYNNAMDDYNNLKSALNELSSLEDMK-NRY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 597 QEEIMKLKDTLksQMTQEASDEAEDMKEAMNRMIDE--------------LNKQVSELSQLYKEAQAELEDYRK-RKSLE 661
Cdd:PRK01156 255 ESEIKTAESDL--SMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAiIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 662 DVTAEYIHKAEHEKLMQLTNvsraKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENS------VSITEHLQVIT--TLR 733
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLN----NQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIermsafISEILKIQEIDpdAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 734 TAAKEMEEKISNLKEHLASKEVEVAKLEKQL--LEEKAAMTDAmvpRSSYEKLQSSLESEVSvlASKLKESVKEKEKVHS 811
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLdeLSRNMEMLNG---QSVCPVCGTTLGEEKS--NHIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 812 EVVQIRSEVSQVKREKENIQTLLKSKE-QEVNELLQKFQQAQEELAEMKRYAESSSKLeEDKDKKINEMSKEVTKLK 887
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLK 559
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
94-242 |
3.21e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.19 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 94 IRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPL--LLAVQNGHSEICHFLLDHGADVN 171
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 172 SRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSEN------AGIQSLLLSKISQDADLKTP 242
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTP 211
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
599-824 |
3.38e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 599 EIMKLKDTLKSQMTQEASDEAEDMKEAMN------RMIDELNKQVS----------ELSQLYKEAQAELEDYRKRK-SLE 661
Cdd:COG3096 882 QANLLADETLADRLEELREELDAAQEAQAfiqqhgKALAQLEPLVAvlqsdpeqfeQLQADYLQAKEQQRRLKQQIfALS 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 662 DVTAEYIHKAEHEKLMQLTNVS----------------RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKEnsvsiteh 725
Cdd:COG3096 962 EVVQRRPHFSYEDAVGLLGENSdlneklrarleqaeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 726 lqvitTLRTAAKEMEEkisnLKEHLASKEVEVAKLEKQLLEEKAAMTDAMvpRSSYEKLQSSLESEVSVLASKLKesvKE 805
Cdd:COG3096 1034 -----TLQELEQELEE----LGVQADAEAEERARIRRDELHEELSQNRSR--RSQLEKQLTRCEAEMDSLQKRLR---KA 1099
|
250
....*....|....*....
gi 1370488827 806 KEKVHsevvQIRSEVSQVK 824
Cdd:COG3096 1100 ERDYK----QEREQVVQAK 1114
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
542-754 |
3.57e-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: 40.73 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 542 KEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIEnmnkekaflfekyqeaqeeimkLKDTLKSQMTQEASDEAED 621
Cdd:pfam17060 67 KESFSEMFNGLVGNNFKTVINKIFEDCDGIPASFISALE----------------------LKEDVKSSPRSEADSLGTP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 622 MKEAMNRMI--DELNKQVSELSQLYKEAQAELEDYRKRKSLEDvtaEYIHKAEHEkLMQLTNvsrakaedALSEMKSQYS 699
Cdd:pfam17060 125 IKVDLLRNLkpQESPETPRRINRKYKSLELRVESMKDELEFKD---ETIMEKDRE-LTELTS--------TISKLKDKYD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370488827 700 KVLNELTQLKQLVDAQKENSV-SITEHLQVITTLRTAAKEMEEKISNLKEHLASKE 754
Cdd:pfam17060 193 FLSREFEFYKQHHEHGGNNSIkTATKHEFIISELKRKLQEQNRLIRILQEQIQFDP 248
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
632-866 |
3.80e-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: 40.99 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 632 ELNKQVSELSQLYKEAQAELEDYRKRKsleDVTAEYIHKAEHEKLMQLTNVS----RAKAEdalSEMKSQYSKVLNELTQ 707
Cdd:pfam09726 420 ELRSQISSLTSLERSLKSELGQLRQEN---DLLQTKLHNAVSAKQKDKQTVQqlekRLKAE---QEARASAEKQLAEEKK 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 708 LKQLVDAQKENSVS--ITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaamtdamvpRSSYEKLQ 785
Cdd:pfam09726 494 RKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQE-----------LRKYKESE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 786 SSLESEVSVLaSKLKESVKEKEKVHSEVVQIR----SEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRY 861
Cdd:pfam09726 563 KDTEVLMSAL-SAMQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPSTSRI 641
|
....*
gi 1370488827 862 AESSS 866
Cdd:pfam09726 642 TPVTP 646
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
685-915 |
3.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 685 AKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQV----ITTLRTAAKEMEEKISNLKEHLASKEVEVAKL 760
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 761 EKQLLEEKAAMTDAMvpRSSYeklQSSLESEVSVL--ASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKE 838
Cdd:COG4942 96 RAELEAQKEELAELL--RALY---RLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370488827 839 QEVNELLQKFQQAQEELAEMkryaessSKLEEDKDKKINEMSKEvtklkealnslsqlsystssSKRQSQQLEALQQ 915
Cdd:COG4942 171 AERAELEALLAELEEERAAL-------EALKAERQKLLARLEKE--------------------LAELAAELAELQQ 220
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
409-676 |
5.09e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 409 IHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVcLNNTEISEnssdlsqkLKETQSKYEEAM 488
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKD--------LTNQDSVKELII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 489 KEVLSVQKQMKlglvspesmdnyshfHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKgtvikpPVEEY 568
Cdd:TIGR04523 457 KNLDNTRESLE---------------TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE------KVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 569 EEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQ 648
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
250 260 270
....*....|....*....|....*....|....
gi 1370488827 649 AELEDYRKRKSLEDVTAEYIH------KAEHEKL 676
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEkelekaKKENEKL 629
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
50-112 |
5.30e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 5.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370488827 50 HLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGK 112
Cdd:PTZ00322 120 HIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-757 |
5.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 506 ESMDNYSHFHE-LRVTEEEINVLKQ--DLQNALEESERNKEKVRELEEKLverekgtvikpPVEEYEEMKSSYCSVIENM 582
Cdd:COG4913 232 EHFDDLERAHEaLEDAREQIELLEPirELAERYAAARERLAELEYLRAAL-----------RLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 583 NKEKAFLFEKYQEAQEEIMKLK---DTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQA-ELEDYRKRK 658
Cdd:COG4913 301 RAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 659 SLEDVTAEYI-HKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQlvdaqkeNSVSITEHLQvitTLRTAak 737
Cdd:COG4913 381 EFAALRAEAAaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-------RKSNIPARLL---ALRDA-- 448
|
250 260
....*....|....*....|
gi 1370488827 738 emeekisnLKEHLASKEVEV 757
Cdd:COG4913 449 --------LAEALGLDEAEL 460
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
418-890 |
5.92e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 418 DNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELvclNNTEISENSSDLSQKLKETQSKYEEA-----MKEVL 492
Cdd:PTZ00440 592 EIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKF---YKGDLQELLDELSHFLDDHKYLYHEAkskedLQTLL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 493 --SVQKQMKLGLVSPESMDN--------YSHFHELR--VTEEEINVLKQDLQNALEESernkekvreleeklveREKGTV 560
Cdd:PTZ00440 669 ntSKNEYEKLEFMKSDNIDNiiknlkkeLQNLLSLKenIIKKQLNNIEQDISNSLNQY----------------TIKYND 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 561 IKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTlksqmtqeaSDEAEDMKEAMNRMIDELNKQVSEL 640
Cdd:PTZ00440 733 LKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNT---------YEEFLQYKDTILNKENKISNDINIL 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 641 SQLYKEAQAELEDYR-KRKSLEDVTAEyiHKAEHEKLMQ-----LTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDA 714
Cdd:PTZ00440 804 KENKKNNQDLLNSYNiLIQKLEAHTEK--NDEELKQLLQkfpteDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINI 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 715 QKENSVSITE---HLQVITTLRTAAKEMEEKISNLKEHLASKEV----EVAKLEKQLLEEKAAM-------------TDA 774
Cdd:PTZ00440 882 IKTLNIAINRsnsNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIiqknEKLNLLNNLNKEKEKIekqlsdtkinnlkMQI 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 775 MVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEV--------SQVKREKENIQTL----LKSKEQEVN 842
Cdd:PTZ00440 962 EKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYnilnkkidDLIKKQHDDIIELidklIKEKGKEIE 1041
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1370488827 843 ELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEAL 890
Cdd:PTZ00440 1042 EKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEAL 1089
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
124-242 |
6.19e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 39.94 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 124 LQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADL 203
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370488827 204 NLVDSLGYNALHYSKLSENAGIQSLLLSK----ISQDADLKTP 242
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAgadvNARDKDGETP 123
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
756-910 |
6.40e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 756 EVAKLEKQLLEEKAAmtdamVPRSSYEKLQSS-LESEVSVLASKLKESVKEKEKVHSEvvqirsEVSQVKREKENIQT-L 833
Cdd:COG5022 876 RVELAERQLQELKID-----VKSISSLKLVNLeLESEIIELKKSLSSDLIENLEFKTE------LIARLKKLLNNIDLeE 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 834 LKSKEQEVNELLQKFQQA----QEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQ 909
Cdd:COG5022 945 GPSIEYVKLPELNKLHEVesklKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE 1024
|
.
gi 1370488827 910 L 910
Cdd:COG5022 1025 V 1025
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
424-870 |
6.88e-03 |
|
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: 40.42 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 424 QQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNN--TEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLG 501
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQekTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 502 LVS--PESMDNYSHFHELRVTEEE-----INVLKQDLQNALEESERNKEKVRELEEKLVE--REKGTVIKPPVEEYEEMK 572
Cdd:TIGR00606 381 GFErgPFSERQIKNFHTLVIERQEdeaktAAQLCADLQSKERLKQEQADEIRDEKKGLGRtiELKKEILEKKQEELKFVI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 573 SSycsvIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQL--YKEAQAE 650
Cdd:TIGR00606 461 KE----LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhHTTTRTQ 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 651 LEDYRKRKSLEDvtaEYIHKAEHEKLMQLTNVS-----RAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEH 725
Cdd:TIGR00606 537 MEMLTKDKMDKD---EQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 726 LQVITTLRTAAKE----------MEEKISNLKEhlaskEVEVAKLEKQLLEEKAAMTDAMVPRSSYE------------K 783
Cdd:TIGR00606 614 LESKEEQLSSYEDklfdvcgsqdEESDLERLKE-----EIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfQ 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 784 LQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAE 863
Cdd:TIGR00606 689 TEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
....*..
gi 1370488827 864 SSSKLEE 870
Cdd:TIGR00606 769 EQETLLG 775
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
468-876 |
7.04e-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: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 468 ENSSDLSQKLKETQSKyeeAMKEVLSVQKQMKLGLvSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRE 547
Cdd:pfam05483 105 ENKLQENRKIIEAQRK---AIQELQFENEKVSLKL-EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 548 LEEKLVEREKGtvIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMT------QEASDEAED 621
Cdd:pfam05483 181 TRQVYMDLNNN--IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSllliqiTEKENKMKD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 622 MKEAMNRMIDELNkQVSELSQLYKEAQAELEDYRKR--KSLEDVTAEyihkaehekLMQLTNVSRAKAEDALSEMKSQYS 699
Cdd:pfam05483 259 LTFLLEESRDKAN-QLEEKTKLQDENLKELIEKKDHltKELEDIKMS---------LQRSMSTQKALEEDLQIATKTICQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 700 KVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEekaaMTdamvprs 779
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE----MT------- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 780 syeKLQSSLESEVsvlaSKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNEL-LQKFQQAQEELAEM 858
Cdd:pfam05483 398 ---KFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeIQLTAIKTSEEHYL 470
|
410
....*....|....*...
gi 1370488827 859 KRYAESSSKLEEDKDKKI 876
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNI 488
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
512-774 |
7.67e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 512 SHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEklverekgtvIKPPVEEYEEMKSSYcSVIENMNKekafLFE 591
Cdd:COG0497 162 EAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA----------AALQPGEEEELEEER-RRLSNAEK----LRE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 592 KYQEAQEEImklkdtlksqmtQEASDEAEDM-KEAMNRM--IDELNKQVSELSQLYKEAQAELEDyrkrksLEDVTAEYI 668
Cdd:COG0497 227 ALQEALEAL------------SGGEGGALDLlGQALRALerLAEYDPSLAELAERLESALIELEE------AASELRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 669 HKAEHEklmqltnvsrakaEDALSEMKSQyskvLNELTQLKqlvdaQKENsVSITEhlqVITTLRTAAKEMEEkISNLKE 748
Cdd:COG0497 289 DSLEFD-------------PERLEEVEER----LALLRRLA-----RKYG-VTVEE---LLAYAEELRAELAE-LENSDE 341
|
250 260
....*....|....*....|....*.
gi 1370488827 749 HLASKEVEVAKLEKQLLEEKAAMTDA 774
Cdd:COG0497 342 RLEELEAELAEAEAELLEAAEKLSAA 367
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
420-646 |
7.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 420 DVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCL---NNTEISENSSDLSqKLKETQSKYEEAMKEVLSVQK 496
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEaktIKAEIEELTDELL-NLVMDIEDPSAALNKLNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 497 QMKlglvspESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLverekgTVIKPPVEEYEEMKSSYC 576
Cdd:PHA02562 266 KIK------SKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSL------EKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 577 SVIENMNKEKAFLFEKYQEAQEEIMKLKDtLKSQMtQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKE 646
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVDKAKK-VKAAI-EELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
581-874 |
8.98e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.84 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 581 NMNKEKAfLFEKYQEAQEEIMKLKDtlksQMTQEASDEAEDMKEAMNRMIDELNKqvsELSQLYKEA------QAELEDY 654
Cdd:PLN03229 420 NMKKREA-VKTPVRELEGEVEKLKE----QILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAviamglQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 655 RKRKS--------LEDVTAEYIHKAEHE----------------KLMQLTNVSRAKaedALSEMKSQYSKVLNELTQ-LK 709
Cdd:PLN03229 492 REEFSkansqdqlMHPVLMEKIEKLKDEfnkrlsrapnylslkyKLDMLNEFSRAK---ALSEKKSKAEKLKAEINKkFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 710 QLVDA----QKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLaskEVEVAKLEKQLLEEKAAMTDAMVPRSSY---E 782
Cdd:PLN03229 569 EVMDRpeikEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEI---ELELAGVLKSMGLEVIGVTKKNKDTAEQtppP 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 783 KLQSSLESEVSVLASKLKESVKEKEkVHSEVVQIRSEVSQVKR-----EKENIQTLLKSKEQEV------NELLQKFQQA 851
Cdd:PLN03229 646 NLQEKIESLNEEINKKIERVIRSSD-LKSKIELLKLEVAKASKtpdvtEKEKIEALEQQIKQKIaealnsSELKEKFEEL 724
|
330 340
....*....|....*....|....
gi 1370488827 852 QEELAEMKR-YAESSSKLEEDKDK 874
Cdd:PLN03229 725 EAELAAAREtAAESNGSLKNDDDK 748
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
607-857 |
8.99e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 39.71 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 607 LKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAK 686
Cdd:COG2770 255 LDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 687 AEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLE 766
Cdd:COG2770 335 LLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 767 EKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQ 846
Cdd:COG2770 415 ALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEE 494
|
250
....*....|.
gi 1370488827 847 KFQQAQEELAE 857
Cdd:COG2770 495 EEEAGAAAEEL 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
623-891 |
9.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 623 KEAMNRMIDELNKQVSELSQLYKEAQAELEDY-RKRKSLEDVTAEYIHKA---EHEKLMQLTNVSRAKAEDALSEMKSQY 698
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLqRLHQAFSRFIGSHLAVAfeaDPEAELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 699 SKVLNELTQLKQLVDA--QKENSVSI--TEHLQ-VITTLRTAAKEMEEKISNLKEH-------------LASKEVEVAKL 760
Cdd:PRK04863 861 QQQRSQLEQAKEGLSAlnRLLPRLNLlaDETLAdRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQL 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488827 761 EKQLLEEKA----------AMTDAMVPRS--SYEKLQSSLESEvSVLASKLKESVKEKEKVHSEV-VQIRSEVSQVkREK 827
Cdd:PRK04863 941 KQDYQQAQQtqrdakqqafALTEVVQRRAhfSYEDAAEMLAKN-SDLNEKLRQRLEQAEQERTRArEQLRQAQAQL-AQY 1018
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370488827 828 ENIQTLLKS----KEQEVNELLQKFQ----QAQEELAEmkRYAESSSKLEE---DKDKKINEMSKEVTKLKEALN 891
Cdd:PRK04863 1019 NQVLASLKSsydaKRQMLQELKQELQdlgvPADSGAEE--RARARRDELHArlsANRSRRNQLEKQLTFCEAEMD 1091
|
|
|