|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
18-243 |
1.84e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.79 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 18 KSDERLLQAVENNDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYG 97
Cdd:COG0666 52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 98 HPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAA 177
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312930 178 ANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEAAQR 243
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
9-264 |
1.34e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.39 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 9 KKTESQDWGKSDERLLQAVENNDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYN 88
Cdd:COG0666 10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 89 ALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLC 168
Cdd:COG0666 90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 169 RLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEAAQRPSPPS 248
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
250
....*....|....*.
gi 1988312930 249 ALTEDDSGEASSQNSM 264
Cdd:COG0666 250 KDGLTALLLAAAAGAA 265
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
23-222 |
3.27e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.90 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 23 LLQAVENNDAPRVAALIArKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCL 102
Cdd:COG0666 91 LHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 103 KQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQD 182
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988312930 183 LQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAA 222
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
35-240 |
3.62e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.04 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 35 VAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDV 114
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 115 VDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACE 194
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1988312930 195 GASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEA 240
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-1071 |
2.08e-21 |
|
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: 101.29 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 295 EEIVRLRQERGRLLQKIRGLEQHKERRQQespeasSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERE 374
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRE------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 375 NTSYDVTTLQDEEGELPDLPGAevllSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENfEKDETQMEVEALAEV 454
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED-RRERLQQEIEELLKK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 455 IPLALYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATAtkngpthmELNGSVApetKVNGAETID 534
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER--------ELAQLQA---RLDSLERLQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 535 EEAAGDETMEARTMEAEATGAEATGAEATGAKVTEtkptgaevremettEEEANMETkptgaqatdtettgVEAMGVEAT 614
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE--------------GYEAAIEA--------------ALGGRLQAV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 615 KTKAEEAEMQAYgvgAGQAEPPVTGTTNMEATGSRATGMESTGVSATGVENPGVEATVPGISAGPILHPGAAEASEKLQV 694
Cdd:TIGR02168 551 VVENLNAAKKAI---AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 695 eletrIRGLEEALRQREREAAAELE-----AALGKC-----EAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQ 764
Cdd:TIGR02168 628 -----VDDLDNALELAKKLRPGYRIvtldgDLVRPGgvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 765 AREDLRDRDSRLRELEAAsacLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAE 844
Cdd:TIGR02168 703 LRKELEELEEELEQLRKE---LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 845 LGRARDAAEARVAELPAACEEARQGLAELREasealrqsvvpasEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAE 924
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRA-------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 925 LERERvcsvalsehERIVGtLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE 1004
Cdd:TIGR02168 847 IEELS---------EDIES-LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312930 1005 AERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQE 1071
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
90-182 |
2.47e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.71 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 90 LHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSfKAHLNPQDrSGATPLIIAAQMCHTDLCR 169
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1988312930 170 LLLQQGAAANDQD 182
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
764-1101 |
1.88e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 764 QAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAA 843
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 844 ELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVvpASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRA 923
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 924 ELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRT 1003
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1004 EAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARDHSSVVALY 1083
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330
....*....|....*...
gi 1988312930 1084 RSHLLYAIQGQMDEDVQR 1101
Cdd:COG1196 537 EAALEAALAAALQNIVVE 554
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
57-149 |
3.79e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 57 FHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLQaSCVVDVVDsSGWTALHHAAAGGCLSCSE 136
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1988312930 137 VLCSFKAHLNPQD 149
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
798-1090 |
1.64e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 798 EEARGLRAELAQREeaRLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREAS 877
Cdd:COG1196 213 ERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 878 EALRQSVV-PASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERVcsvALSEHERIVGTLQANVAQLEGQL 956
Cdd:COG1196 291 YELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE---ELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 957 EELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEV 1036
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1037 FNLKEALKEQPAALATPEVEALR------DQVKDLQQQLQEAARDHSSVVALYRSHLLYA 1090
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEeaalleAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
808-1072 |
4.90e-16 |
|
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: 83.57 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 808 AQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQsvvpa 887
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA----- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 888 sEHRRLQEealelrgRAASLEQEVVATGKEAARLRAELERERVcsvALSEHERIVGTLQANVAQLEGQLEELGRRHEKTS 967
Cdd:TIGR02168 741 -EVEQLEE-------RIAQLSKELTELEAEIEELEERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 968 AEVFQVQREAL-------FMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLK 1040
Cdd:TIGR02168 810 AELTLLNEEAAnlrerleSLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270
....*....|....*....|....*....|..
gi 1988312930 1041 EALKEQPAALATpEVEALRDQVKDLQQQLQEA 1072
Cdd:TIGR02168 890 ALLRSELEELSE-ELRELESKRSELRRELEEL 920
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
729-1068 |
9.58e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 729 EAEAGRLRERVREAEGSGASGGGGGDTTQL----RAALEQAREDLRDRDSRLRELeaasacLDEARASRLLAEEEARGLR 804
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLddadAEAVEARREELEDRDEELRDR------LEECRVAAQAHNEEAESLR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 805 AELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSV 884
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 885 VPASEHRRLQEEALElrgraasleqevvatgkEAARLRAE----------LERERVCsvALSEHERIVGTLQANVAQLEG 954
Cdd:PRK02224 429 AELEATLRTARERVE-----------------EAEALLEAgkcpecgqpvEGSPHVE--TIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 955 QLEELGRRHEKTSAEVfQVQREALFMKSERHAAEAQLATAE-------QQLRGLRTEA-----------ERARQAQSRAQ 1016
Cdd:PRK02224 490 EVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRetieekrERAEELRERAaeleaeaeekrEAAAEAEEEAE 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1988312930 1017 EALDKAKEKDKKITELSKEVFNLkEALKEQPAALA--TPEVEALRDQVKDLQQQ 1068
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESL-ERIRTLLAAIAdaEDEIERLREKREALAEL 621
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
38-213 |
1.36e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 38 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGS---NVMSADGAgyNALHLAAKYGHPQCLKQLLQASCVVDV 114
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 115 VDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
|
170 180
....*....|....*....|
gi 1988312930 194 EGASPETVEVLLQGGAQPGI 213
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNI 230
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
754-1079 |
4.19e-13 |
|
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: 73.95 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 754 DTTQLRAALEQAREDL----RDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLA 829
Cdd:TIGR02169 668 FSRSEPAELQRLRERLeglkRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 830 taratgeqqrtaaaELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPA------SEHRRLQEEALELRGR 903
Cdd:TIGR02169 748 --------------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 904 AASLEQEVVATGKEAARLRAELERERVCSVALSEHERivgTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSE 983
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 984 RHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEkdkkitelskevfNLKEALKEQPAALATPEVEALRDQVK 1063
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE-------------ELSEIEDPKGEDEEIPEEELSLEDVQ 957
|
330
....*....|....*.
gi 1988312930 1064 DLQQQLQEAARDHSSV 1079
Cdd:TIGR02169 958 AELQRVEEEIRALEPV 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
293-880 |
1.17e-12 |
|
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: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 293 AYEEIVRLRQERGRLLQKIRGLEQHKERRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENE 372
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 373 RENTSYDVTTLQDEEGELPDlpgAEVLLSRQLSpSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVEALA 452
Cdd:COG1196 297 LARLEQDIARLEERRRELEE---RLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 453 EVIP-LALYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATATKNgpthmELNGSVAPETKVNGAE 531
Cdd:COG1196 373 ELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-----ELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 532 TIDEEAAGDETMEARTMEAEATGAEATGAEATGAKVTETkpTGAEVREMETTEEEANMETKPTGAQATDTETTGVEAMGV 611
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 612 EATKTKAEEAEMQAYGVGAGQAEPPVTGTTNMEATGSRATGMESTGVSATgvenpgveatvpgISAGPILHPGAAEASEK 691
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-------------FLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 692 LQVELETRIRGLEEALRQREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRD 771
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 772 RDSRLRELEAASAclDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDA 851
Cdd:COG1196 673 ALLEAEAELEELA--ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580
....*....|....*....|....*....
gi 1988312930 852 AEARVAELPAACEEARQGLAELREASEAL 880
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
23-116 |
2.50e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 23 LLQAVENNDAPRVAALIaRKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSnvMSADGAGYNALHLAAKYGHPQCL 102
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1988312930 103 KQLLQASCVVDVVD 116
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
50-209 |
3.00e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.05 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 50 DPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAG 129
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 130 GCLSCSEVLCSFKAHLNPQdrSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGA 209
Cdd:PLN03192 602 KHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
33-192 |
5.07e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.67 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 33 PRVAALIARKGLVPTKLDPEGKSAFHlAAMRGAASCLEV---MIAHGSNVMSADGAGYNALHLAAKYGHP--QCLKQLLQ 107
Cdd:PHA03095 132 PKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELlrlLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 108 ASCVVDVVDSSGWTALHHAAAGGclSCSEVLCSF----KAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDL 183
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
|
....*....
gi 1988312930 184 QGRTALMLA 192
Cdd:PHA03095 289 DGNTPLSLM 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
728-1071 |
5.61e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 728 AEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRdRDSRLRELEAASACLDEARASRLLAEEEARglRAEL 807
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIARKAEDAR--KAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 808 AQR-EEAR-LEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVV 885
Cdd:PTZ00121 1169 ARKaEDAKkAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 886 PASEHRRLQEEAlelrgRAASLEQEVVATGKEAARLRAEL----ERERVCSVALSEHERivgtlqaNVAQLEGQLEELGR 961
Cdd:PTZ00121 1249 RNNEEIRKFEEA-----RMAHFARRQAAIKAEEARKADELkkaeEKKKADEAKKAEEKK-------KADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 962 RHE-KTSAEVFQVQREALFMKSE--RHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFN 1038
Cdd:PTZ00121 1317 ADEaKKKAEEAKKKADAAKKKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
330 340 350
....*....|....*....|....*....|...
gi 1988312930 1039 LKEALKEQPAALATPEVEALRDQVKDLQQQLQE 1071
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
685-1098 |
8.98e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 685 AAEASEKLQVELETRIRGLEEALRQREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQ 764
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 765 AREDLRDRDSRLRELEAASACLDEARASRLLAEEEArgLRAELAQREEARLEQSRELEVLREQLAT-ARATGEQQRTAAA 843
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--EEALLELLAELLEEAALLEAALAELLEElAEAAARLLLLLEA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 844 ELGRARDAAEARVAELPAACEEARQGLAELREASEALRQsVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRA 923
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA-ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 924 ELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREAL----FMKSERHAAEAQLATAEQQLR 999
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEaalrRAVTLAGRLREVTLEGEGGSA 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1000 GLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARDHSSV 1079
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
410
....*....|....*....
gi 1988312930 1080 VALYRSHLLYAIQGQMDED 1098
Cdd:COG1196 739 EELLEEEELLEEEALEELP 757
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
336-929 |
1.48e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 336 RQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSYDVTTLQDEEGELpdlpGAEVLLSRQLSPSAQEHLASL 415
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 416 QEQVAVLTRQNQELMEKVQILENFEKDETQMEVEALAEViplalyDSLRAEFDQLRRQHAEALQALRQQETREVPREEGA 495
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEEL------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 496 ACGESEVAGATATkngpthmelngsvapETKVNGAETIDEEAAGDETMEARTMEAEATGAEATGAEATGAKVTETKPTGA 575
Cdd:COG1196 382 EELAEELLEALRA---------------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 576 EVREMETTEEEANMETKP---TGAQATDTETTGVEAMGVEATKTKAEEAEMQAYGVGAGQAEppvtgttnmeATGSRATG 652
Cdd:COG1196 447 AAEEEAELEEEEEALLELlaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----------GVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 653 MESTGVSATGVENPGVEATVPgisagPILHPGAAEASEKLQVELETRIRGLEEALRQREREAAAELEAalgkceAAEAEA 732
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYE-----AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL------DKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 733 GRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREE 812
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 813 ARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAElpaaceEARQGLAELREASEALRQSVVPASEHRR 892
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE------AEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988312930 893 LQEEALELRGRAASLEQEVVATGKEAARLRAELERER 929
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
761-994 |
5.18e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 761 ALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQsrELEVLREQLATARAtgeqqrt 840
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEA------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 841 AAAELGRARDAAEARVAELPAACEEA-RQGLAELREASEALRQsvvpasEHRRLQEEALELRGRAASLEQEVVATGKEAA 919
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLER------ELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 920 RLRAELERervcsvALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATA 994
Cdd:COG4913 384 ALRAEAAA------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
726-1072 |
1.06e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 726 EAAEAEAGRLRERVREAEgsgasgggggdttQLRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRA 805
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAE-------------ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 806 ELAQREEAR-LEQSRELEVLREQLATAR--ATGEQQRTAAAELGRA---RDAAEARVAELPAACEEARQGLAELREASEA 879
Cdd:PTZ00121 1241 EAKKAEEERnNEEIRKFEEARMAHFARRqaAIKAEEARKADELKKAeekKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 880 LRQS---------VVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERVCSV-ALSEHERIVGTLQANV 949
Cdd:PTZ00121 1321 KKKAeeakkkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkKKAEEKKKADEAKKKA 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 950 AQLEGQLEELGRRHE--------KTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRG--LRTEAERARQAQS------ 1013
Cdd:PTZ00121 1401 EEDKKKADELKKAAAakkkadeaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAeeAKKKAEEAKKADEakkkae 1480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 1014 ---RAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEA 1072
Cdd:PTZ00121 1481 eakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
805-1115 |
1.09e-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: 66.23 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 805 AELAQREEARLEQSRELE--VLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALrq 882
Cdd:TIGR02168 209 AEKAERYKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 883 svvpasehrrlQEEALELRGRAASLEQEVVATGKEAARLRAELERervCSVALSEHERIVGTLQANVAQLEGQLEELGRR 962
Cdd:TIGR02168 287 -----------QKELYALANEISRLEQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 963 HEKTSAEVfqvqrealfmkserHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEK----DKKITELSKEVFN 1038
Cdd:TIGR02168 353 LESLEAEL--------------EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRER 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312930 1039 LKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARDHSSVVAlyrshLLYAIQGQMDEDVQRILSQILQMQRLQAQ 1115
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE-----ALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1064 |
1.16e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 684 GAAEASEKLQVELETRIRGLEEALRQREREAAAEleaalgkcEAAEAEAGRLRERVREAEGSGASGGGggdttqlRAALE 763
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE--------EARKAEDARKAEEARKAEDAKRVEIA-------RKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 764 QAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARglRAELAQR--EEARLEQSRELEVLREQLATARAtgEQQRta 841
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR--KAEAARKaeEERKAEEARKAEDAKKAEAVKKA--EEAK-- 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 842 aaelgraRDAAEARVAELPAACEEARQgLAELREASEALRQSVVPASEHRRLQE--EALELRgRAASLEQEVVATGKEAA 919
Cdd:PTZ00121 1237 -------KDAEEAKKAEEERNNEEIRK-FEEARMAHFARRQAAIKAEEARKADElkKAEEKK-KADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 920 RLRAELERERvcsvalSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLR 999
Cdd:PTZ00121 1308 KKKAEEAKKA------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 1000 GLRTEAERARqaqsRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKD 1064
Cdd:PTZ00121 1382 AAKKKAEEKK----KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
156-237 |
1.62e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 156 LIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDalGQDAAHYGALAGDKLILH 235
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
..
gi 1988312930 236 LL 237
Cdd:pfam12796 79 LL 80
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-1080 |
4.39e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 472 RQHAEALQALRQQETREVPREEGAACGESEVAGATATKNGPTHMELNGSVAPETKVNGAETIDEEAAGDEtmEARTMEAE 551
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--ELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 552 ATGAEATGAEATgAKVTETKPTGAEVREMETTEEEANMETKPTGAQATDTETTGVEAmgvEATKTKAEEAEMQAygvgAG 631
Cdd:PTZ00121 1290 KKADEAKKAEEK-KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEA----EA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 632 QAEPPVTGTTNMEATGSRATGMESTGVSATGVENPGVEATVPGISAGPIlhpGAAEASEKLQVELETR---IRGLEEALR 708
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL---KKAAAAKKKADEAKKKaeeKKKADEAKK 1438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 709 QREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAR---EDLRDRDSRLRELEAASAC 785
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 786 LDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLRE-----QLATARATGEQQRTAAAELGRARDAAEARVAELP 860
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 861 AACEEARQGLAE-LREASEALrqsvVPASEHRRLQEEALELRGRAASLEQEVvatgKEAARLRAELERERVCSVAL---S 936
Cdd:PTZ00121 1599 KLYEEEKKMKAEeAKKAEEAK----IKAEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEakkA 1670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 937 EHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREAlfmKSERHAAEaQLATAEQQLRGLRTEAERARQAQSRAQ 1016
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE---AEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312930 1017 EALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARDHSSVV 1080
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
301-1072 |
6.92e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 301 RQERGRLLQKIRGLEQHKERRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENtsydv 380
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN----- 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 381 ttlqdEEGELPDLPGAEVLLSRQLSPSAQEhlaslqeqvavlTRQNQEL--MEKVQILENFEKDETQMEVEAL---AEVI 455
Cdd:PTZ00121 1252 -----EEIRKFEEARMAHFARRQAAIKAEE------------ARKADELkkAEEKKKADEAKKAEEKKKADEAkkkAEEA 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 456 PLAlyDSLRAEFDQLRRQhAEALQalRQQETREVPREEGAACGESEVAGATATKNGPTHMELNGSVApETKVNGAETIDE 535
Cdd:PTZ00121 1315 KKA--DEAKKKAEEAKKK-ADAAK--KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAE 1388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 536 EAAGDETMEARTMEAEATGAEATGAEATGAKVTETKPTGAEVREMETTEEEANMETKptgaqATDTETTGVEAMGVEATK 615
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKAEEAK 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 616 TKAEEAEmqaygvgagQAEppvtgttNMEATGSRATGMESTGVSATGVENPGVEATvpgisagpilhpGAAEASEKLQve 695
Cdd:PTZ00121 1464 KKAEEAK---------KAD-------EAKKKAEEAKKADEAKKKAEEAKKKADEAK------------KAAEAKKKAD-- 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 696 letRIRGLEEALRQREREAAAeleaalgkcEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAalEQAREDLRDRDSR 775
Cdd:PTZ00121 1514 ---EAKKAEEAKKADEAKKAE---------EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMA 1579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 776 LRELEAASAcLDEARASRL--LAEEEARGLRAELAQREEARL--EQSRELEVLREQLATARATGEQQRTAAAELGRARDA 851
Cdd:PTZ00121 1580 LRKAEEAKK-AEEARIEEVmkLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 852 AEARVAELPAACEEARQGLAELREASEALRQSvvpASEHRRLQEEALELRGRAASLEQEVvatgKEAARLRAELERERVc 931
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAEEAKKAEELKKKEAEEK----KKAEELKKAEEENKI- 1730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 932 svalseherivgtlqaNVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLR-GLRTEAERARQ 1010
Cdd:PTZ00121 1731 ----------------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEeELDEEDEKRRM 1794
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 1011 aqsraqealdkakEKDKKITELSKEVFNLKEALKEQPAALATP---EVEALRDQVKDLQQQLQEA 1072
Cdd:PTZ00121 1795 -------------EVDKKIKDIFDNFANIIEGGKEGNLVINDSkemEDSAIKEVADSKNMQLEEA 1846
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
8-206 |
9.35e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 8 FKKTESQDWGKSDERLLQAVENNDAPRVAALIaRKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGY 87
Cdd:PLN03192 514 GDNGGEHDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 88 NALHLAAKYGHPQCLKQLLQASCVVDvvDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDL 167
Cdd:PLN03192 593 TALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988312930 168 CRLLLQQGAAANDQDLQgrtalmlacEGASPETVEVLLQ 206
Cdd:PLN03192 671 VRLLIMNGADVDKANTD---------DDFSPTELRELLQ 700
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
693-1115 |
2.66e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 693 QVELETRIRGLEEALRQREREAaaeleaalGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRDR 772
Cdd:COG4913 250 QIELLEPIRELAERYAAARERL--------AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 773 DSRLRELEAASACLDEARASRLlaEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAE----LGRA 848
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAlleaLEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 849 RDAAEARVAELPAACEEARQGLAELREASEAL--RQSVVPASEHRRLQ-----------------------------EEA 897
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLerRKSNIPARLLALRDalaealgldeaelpfvgelievrpeeerwRGA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 898 LE--LRGRAASLeqeVVATGKEAA------------RLRAELERERVCSVALS--EHERIVGTLQ--------------- 946
Cdd:COG4913 480 IErvLGGFALTL---LVPPEHYAAalrwvnrlhlrgRLVYERVRTGLPDPERPrlDPDSLAGKLDfkphpfrawleaelg 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 947 --------ANVAQL---------EGQLEELGRRHEK------TSAEVF----QVQREALfmKSERHAAEAQLATAEQQLR 999
Cdd:COG4913 557 rrfdyvcvDSPEELrrhpraitrAGQVKGNGTRHEKddrrriRSRYVLgfdnRAKLAAL--EAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1000 GLRTEaERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEqpAALATPEVEALRDQVKDLQQQLQEAARdhssv 1079
Cdd:COG4913 635 ALEAE-LDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER--LDASSDDLAALEEQLEELEAELEELEE----- 706
|
490 500 510
....*....|....*....|....*....|....*.
gi 1988312930 1080 valyRSHLLYAIQGQMDEDVQRILSQILQMQRLQAQ 1115
Cdd:COG4913 707 ----ELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
796-1052 |
9.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 796 AEEEARGLRAELAQREEARleqsRELEVLREQ---LATARATGEQQRTAAAELGRARDAAEARVAElpaaceEARQGLAE 872
Cdd:COG4913 223 TFEAADALVEHFDDLERAH----EALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLW------FAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 873 LREASEALRQsvvpasEHRRLQEEALELRGRAASLEQEVVATgkEAARLRAELERERVCSVALSEHERIVGTLQANVAQL 952
Cdd:COG4913 293 LEAELEELRA------ELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 953 EGQLEELGRRHEkTSAEVFQVQREalfmkserhAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDkakEKDKKITEL 1032
Cdd:COG4913 365 EALLAALGLPLP-ASAEEFAALRA---------EAAALLEALEEELEALEEALAEAEAALRDLRRELR---ELEAEIASL 431
|
250 260
....*....|....*....|
gi 1988312930 1033 SKEVFNLKEALKEQPAALAT 1052
Cdd:COG4913 432 ERRKSNIPARLLALRDALAE 451
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
50-220 |
1.15e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 50 DPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAG 129
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 130 GCLSCSEVLCSFKAHLNPQDRSGATPLIIAaqMCHTDLCRLLLQQGAAANDQDLQGRTALMLACE-GASPETVEVLLQGG 208
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHK 278
|
170
....*....|..
gi 1988312930 209 AQPGITDALGQD 220
Cdd:PHA02874 279 ADISIKDNKGEN 290
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1075 |
1.88e-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: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 870 LAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEvvatgkeaaRLRAELERERVcsvALSEHERIVGTLQANV 949
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLE---------ELREELEELQE---ELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 950 AQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERA----RQAQSRAQEALDKAKEK 1025
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqlEELESKLDELAEELAEL 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1026 DKKITELSKEVFNLKEALKEQPAalatpEVEALRDQVKDLQQQLQEAARD 1075
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEA-----ELEELESRLEELEEQLETLRSK 387
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
705-1074 |
3.27e-08 |
|
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: 58.04 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 705 EALRQREREAAAELeaalgkcEAAEAEAGRLRERVReaegsgasgggggdttqLRAALEQAREDLRDRDSRLRE----LE 780
Cdd:COG3096 316 EELSARESDLEQDY-------QAASDHLNLVQTALR-----------------QQEKIERYQEDLEELTERLEEqeevVE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 781 AASACLDEARASRLLAEEEARGLRAELAQREEA-RLEQSRELEVLREQLATARAtgeQQRTAAAELgrARDAAEARVAEL 859
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAlDVQQTRAIQYQQAVQALEKA---RALCGLPDL--TPENAEDYLAAF 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 860 PAACEEARQGLAElreaseaLRQSVVPASEHRRLQEEALEL---------RGRAASLEQEVVatgKEAARLRAELERERV 930
Cdd:COG3096 447 RAKEQQATEEVLE-------LEQKLSVADAARRQFEKAYELvckiageveRSQAWQTARELL---RRYRSQQALAQRLQQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 931 CSVALSEHERivgtLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAE--RA 1008
Cdd:COG3096 517 LRAQLAELEQ----RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEqlRA 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312930 1009 RQAQSRAQE-ALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEA--LRDQVKDLQQQLQEAAR 1074
Cdd:COG3096 593 RIKELAARApAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAtvERDELAARKQALESQIE 661
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
69-237 |
3.34e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.37 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 69 LEVMIAHGSNVMSADGAGYNALHLAA--KYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGC--LSCSEVLCSFKAH 144
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 145 LNPQDRsgatpliiaaqmchtdlCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHY 224
Cdd:PHA03100 169 INAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
|
170
....*....|...
gi 1988312930 225 GALAGDKLILHLL 237
Cdd:PHA03100 232 AILNNNKEIFKLL 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
769-1111 |
3.50e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 769 LRDRDSRLRELEAASAC---LDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLA---TARATGEQQRTAA 842
Cdd:PRK04863 275 MRHANERRVHLEEALELrreLYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 843 AELgrarDAAEARVAELPAACEEARQGLAELREASEALRQSV-------------VPASEHRRLQ--------EEALELR 901
Cdd:PRK04863 355 ADL----EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVdelksqladyqqaLDVQQTRAIQyqqavqalERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 902 GRAA-------SLEQEVVATGKEAARLRAELERE-RVCSVALSEHE-------RIVGTLQANVAQLEGQleELGRRHEKT 966
Cdd:PRK04863 431 GLPDltadnaeDWLEEFQAKEQEATEELLSLEQKlSVAQAAHSQFEqayqlvrKIAGEVSRSEAWDVAR--ELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 967 SAEVFQVQrealfmkserhAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQ 1046
Cdd:PRK04863 509 RHLAEQLQ-----------QLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312930 1047 PAalatpEVEALRDQVKDLQQQLQEAARD----HSSVVALYRshlLYAIQGQMDEDVQRILSQILQMQR 1111
Cdd:PRK04863 578 RE-----RRMALRQQLEQLQARIQRLAARapawLAAQDALAR---LREQSGEEFEDSQDVTEYMQQLLE 638
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
72-126 |
3.74e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 3.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312930 72 MIAHGS-NVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHA 126
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
686-1068 |
3.90e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 686 AEASEKLQVELETRIRGLEEALRQREREAaaeleaalgkcEAAEAEAGRLRERVREAEGSGASGGGGGDTtqLRAALEQA 765
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAA-----------QAHNEEAESLREDADDLEERAEELREEAAE--LESELEEA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 766 REDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQ-------- 837
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcp 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 838 ---QRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALEL-------RGRAASL 907
Cdd:PRK02224 456 ecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLeeliaerRETIEEK 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 908 EQEVVATGKEAARLRAELERERvcSVALSEHERIVGTLQAnVAQLEGQLEELGRRhektsaevfqvqREALFMKSERHAA 987
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKR--EAAAEAEEEAEEAREE-VAELNSKLAELKER------------IESLERIRTLLAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 988 EAQLATAEQQLRglrteaERARQAQSRAQEALDKAKEKDKKITELSKEV-FNLKEALKEQPA------ALATPEVEALRD 1060
Cdd:PRK02224 601 IADAEDEIERLR------EKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKEraeeylEQVEEKLDELRE 674
|
....*...
gi 1988312930 1061 QVKDLQQQ 1068
Cdd:PRK02224 675 ERDDLQAE 682
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
86-138 |
4.37e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 86 GYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVL 138
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
796-1072 |
5.00e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 796 AEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEqqrtaaaelgrARDAAEARVAELPAACEEARQgLAELRE 875
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE-----------ARKAEDARKAEEARKAEDAKR-VEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 876 ASEALRQSVVPASEHRRLQEE---ALELRgRAASLEQEVVATGKEAARlRAELEReRVCSVALSEHERIVGTL------- 945
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAarkAEEVR-KAEELRKAEDARKAEAAR-KAEEER-KAEEARKAEDAKKAEAVkkaeeak 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 946 ----QANVAQLEGQLEELgRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRT--EAERARQAQSRAQEAl 1019
Cdd:PTZ00121 1237 kdaeEAKKAEEERNNEEI-RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAEEA- 1314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 1020 DKAKEKDKKITELSKEVFNLKEALKE--QPAALATPEVEALRDQVKDLQQQLQEA 1072
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
758-1073 |
8.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 758 LRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEeARGLRAELAQREEARLEQ-SRELEVLREQLATARAtge 836
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKkAEEYEKLKEKLIKLKG--- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 837 QQRTAAAELGRARDAaEARVAELPAACEEARQGLAELreasealrqsvvpaseHRRLQEEAL----ELRGRAASLE---Q 909
Cdd:PRK03918 540 EIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAEL----------------LKELEELGFesveELEERLKELEpfyN 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 910 EVVATGKEAARLRAELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRHektSAEVFQVQREALFMKSERHAaea 989
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY---SEEEYEELREEYLELSRELA--- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 990 qlataeqqlrGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALkeqpaalatPEVEALRDQVKDLQQQL 1069
Cdd:PRK03918 677 ----------GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL---------ERVEELREKVKKYKALL 737
|
....
gi 1988312930 1070 QEAA 1073
Cdd:PRK03918 738 KERA 741
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
154-205 |
9.29e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 9.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 154 TPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLL 205
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-929 |
1.29e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 688 ASEKLQvELETRIRGLEEALRQREREAaaeleaalgkcEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQARE 767
Cdd:COG4913 608 NRAKLA-ALEAELAELEEELAEAEERL-----------EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 768 DLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGR 847
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 848 ARDAAEARVAELPAACEEARQGL-AELREASEALRQ----------------SVVPAS------EHRRLQEEAL-ELRGR 903
Cdd:COG4913 756 AAALGDAVERELRENLEERIDALrARLNRAEEELERamrafnrewpaetadlDADLESlpeylaLLDRLEEDGLpEYEER 835
|
250 260
....*....|....*....|....*.
gi 1988312930 904 AASLEQEvvATGKEAARLRAELERER 929
Cdd:COG4913 836 FKELLNE--NSIEFVADLLSKLRRAI 859
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
119-172 |
1.44e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1988312930 119 GWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLL 172
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
290-1036 |
1.88e-07 |
|
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: 55.61 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 290 DRDAYEEIVRLRQErgrllqkIRGLEQHKERRQQESPEASSLHI----LERQVQELQQLLVERQEEKESLGRE------- 358
Cdd:pfam12128 229 DIQAIAGIMKIRPE-------FTKLQQEFNTLESAELRLSHLHFgyksDETLIASRQEERQETSAELNQLLRTlddqwke 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 359 -VESLQSRLSLLENERENTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILE 437
Cdd:pfam12128 302 kRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 438 NFEKDETQMEVEALaeviplalYDSLRAEFDQLRRQHAEALQALRQQETREVPREEGAACGESEVAGATATKNGPTHMEL 517
Cdd:pfam12128 382 SKIKEQNNRDIAGI--------KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 518 NGSVA-PETKVNGAETIDEEAAGDETMEARTMEAEATGAEATGAEATGAKVTEtKPTGAEVREMETTEEEANMETKPTGA 596
Cdd:pfam12128 454 NQATAtPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASE-ALRQASRRLEERQSALDELELQLFPQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 597 QATDTETTGVEAMGVEATKTKAEEAEMqaygVGAGQAEPPVTGttnmeatgsratgmestgvsatgvENPGVEATVPGIS 676
Cdd:pfam12128 533 AGTLLHFLRKEAPDWEQSIGKVISPEL----LHRTDLDPEVWD------------------------GSVGGELNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 677 agpiLHPGAAEASEKLQveletrirgLEEALRQREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGasgggggdtT 756
Cdd:pfam12128 585 ----LDLKRIDVPEWAA---------SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE---------T 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 757 QLRAALEQAREDLRDRDSRLRELEAAsacLDEARASRL-LAEEEARGLRAELAQREearLEQSRELEVLREQLATARATG 835
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDK---KNKALAERKdSANERLNSLEAQLKQLD---KKHQAWLEEQKEQKREARTEK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 836 EQQRTAAAElgrARDAAEARVAELPAACEEARqglaelreasealrqsvvpASEHRRLQEE-ALELRGRAASlEQEVVAT 914
Cdd:pfam12128 717 QAYWQVVEG---ALDAQLALLKAAIAARRSGA-------------------KAELKALETWyKRDLASLGVD-PDVIAKL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 915 GKEAARLRAELERERVCSVALSEHERIVGT--------LQANVAQLEGQLEELGRRHEKTSAEVfQVQREALFMksERHA 986
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprLATQLSNIERAISELQQQLARLIADT-KLRRAKLEM--ERKA 850
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312930 987 AEAQLATAEQQLRGLRTEAER---------ARQAQSRAQEALDKAKEKDKKITELSKEV 1036
Cdd:pfam12128 851 SEKQQVRLSENLRGLRCEMSKlatlkedanSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-180 |
2.94e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 54.29 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 30 NDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMR--GAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQC------ 101
Cdd:PHA03100 83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkll 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 102 ------------LKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCR 169
Cdd:PHA03100 163 idkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242
|
170
....*....|.
gi 1988312930 170 LLLQQGAAAND 180
Cdd:PHA03100 243 LLLNNGPSIKT 253
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-1079 |
6.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 685 AAEASEKLQVELETRIRGLE---EALRQREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLR-- 759
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKel 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 760 ----AALEQAREDLRDRDSRLRE-LEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLAtarat 834
Cdd:TIGR02168 439 qaelEELEEELEELQEELERLEEaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK----- 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 835 geQQRTAAAELGRARDAAEARV---AELPAACEEARQ-----GLAELREASEALRQS--------VVPASEHRRLQEEAL 898
Cdd:TIGR02168 514 --NQSGLSGILGVLSELISVDEgyeAAIEAALGGRLQavvveNLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 899 ELR-------GRAASLEQE----------------VVATGKEAARLRAELERE------------RVCSVALSEHERIVG 943
Cdd:TIGR02168 592 EILkniegflGVAKDLVKFdpklrkalsyllggvlVVDDLDNALELAKKLRPGyrivtldgdlvrPGGVITGGSAKTNSS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 944 TL--QANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDK 1021
Cdd:TIGR02168 672 ILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 1022 A----KEKDKKITELSKEVFNLKEALKEQPAalatpEVEALRDQVKDLQQQLQEAARDHSSV 1079
Cdd:TIGR02168 752 LskelTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDEL 808
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
28-224 |
7.48e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.10 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 28 ENNDAPRVAALIARKGLVPTKlDPEGKSAFHLAAMRGAASCLEV---MIAHGSNVMSADGAGYNALHLaakyghpqclkq 104
Cdd:PHA03095 23 SNVTVEEVRRLLAAGADVNFR-GEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 105 LLQASCVVDVVDssgwtalhhaaaggclscseVLCSFKAHLNPQDRSGATPL-IIAAQMC-HTDLCRLLLQQGAAANDQD 182
Cdd:PHA03095 90 YLYNATTLDVIK--------------------LLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988312930 183 LQGRTAL--MLACEGASPETVEVLLQGGAQPGITDALGQDAAHY 224
Cdd:PHA03095 150 LYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH 193
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
761-1074 |
4.22e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 761 ALEQAREDLRDRDSRLRELEAASA----CLDEARASRLLAEEEARGLRAELAQREEA-RLEQSRELEVLREQLATARAtg 835
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEeadeQQEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQYQQAVQALERA-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 836 eQQRTAAAELgrARDAAEARVAELPAACEEARQglaELREASEALRQsvvpASEHRRLQEEALELrgraasleqevvatg 915
Cdd:PRK04863 427 -KQLCGLPDL--TADNAEDWLEEFQAKEQEATE---ELLSLEQKLSV----AQAAHSQFEQAYQL--------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 916 keAARLRAELERERVCSVA---LSEHERIVgTLQANVAQLEGQLEELGRRHEKtSAEVFQVQREALfMKSERH-----AA 987
Cdd:PRK04863 482 --VRKIAGEVSRSEAWDVArelLRRLREQR-HLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFC-KRLGKNlddedEL 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 988 EAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEA---LKEQ-PAALATPEvealrdQVK 1063
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDAlarLREQsGEEFEDSQ------DVT 630
|
330
....*....|.
gi 1988312930 1064 DLQQQLQEAAR 1074
Cdd:PRK04863 631 EYMQQLLERER 641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
771-977 |
4.35e-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: 50.15 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 771 DRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARD 850
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 851 AAEARVAE-LPAACEEARQGLAEL----REASEALRQSVVPASEHRRLQEEALELRGRAASLE---QEVVATGKEAARLR 922
Cdd:COG4942 101 AQKEELAElLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalrAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312930 923 AELERERV-CSVALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREA 977
Cdd:COG4942 181 AELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
836-1072 |
5.41e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 836 EQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASealrQSVVPASEHRRLQEEALELRGRAASLEQEVVATG 915
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKN----GLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 916 KEAARLRAELERERVCSVALSEHERIvGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREalfmkseRHAAEAQLATAE 995
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVI-QQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312930 996 QQ-LRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEalkeqpaalatpEVEALRDQVKDLQQQLQEA 1072
Cdd:COG3206 312 QRiLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLER------------EVEVARELYESLLQRLEEA 377
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
38-159 |
6.45e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.96 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 38 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGhpQCLKQLLQASCVVDVVDS 117
Cdd:PHA02874 175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDI 252
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988312930 118 SGWTALHHAAAGGC-LSCSEVLCSFKAHLNPQDRSGATPLIIA 159
Cdd:PHA02874 253 DGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
55-106 |
6.69e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 6.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 55 SAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLL 106
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
760-1076 |
7.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 760 AALEQAREDLRDRDSRLRELEAASACLDEARAsRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQR 839
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 840 TAAAELGRAR-------------------------DAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQ 894
Cdd:COG4717 167 ELEAELAELQeeleelleqlslateeelqdlaeelEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 895 EEALELRGRAASLEQEVVATGKEAARLR--------------AELERERVCSVALSEHERIVGTLQANVAQLEGQLEELG 960
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 961 RRHEKTSAEVFQVqREALFMKSERHAAEAQLATAEQQLRGLRTEAERAR---QAQSRAQEALDKAKEKDKKITELSKEVF 1037
Cdd:COG4717 327 ALGLPPDLSPEEL-LELLDRIEELQELLREAEELEEELQLEELEQEIAAllaEAGVEDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1988312930 1038 NLKEALKEQP----AALATPEVEALRDQVKDLQQQLQEAARDH 1076
Cdd:COG4717 406 ELEEQLEELLgeleELLEALDEEELEEELEELEEELEELEEEL 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-489 |
1.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 291 RDAYEEIVRLRQERGRLLQKIRGLEQHKERRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLE 370
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 371 NERENTSYDVTTLQDEEGELPDLPGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEK-VQILENF------EKDE 443
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaETAD 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1988312930 444 TQMEVEALAEVipLALYDSLRAefDQLRRQHAEALQALRQQETREV 489
Cdd:COG4913 807 LDADLESLPEY--LALLDRLEE--DGLPEYEERFKELLNENSIEFV 848
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-217 |
1.29e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 49.29 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 9 KKTESQDWGKS-DERLLQavennDAPRVAALIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGY 87
Cdd:PHA02876 138 KINESIEYMKLiKERIQQ-----DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 88 NALHLAAKYGHPQCLKQLLQASCVVDVVDSSgwtaLHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMchTDL 167
Cdd:PHA02876 213 SVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA--PSL 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988312930 168 CRL---LLQQGAAANDQDLQGRTAL-MLACEGASPETVEVLLQGGAQPGITDAL 217
Cdd:PHA02876 287 SRLvpkLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRL 340
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
102-208 |
1.30e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 102 LKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQ 181
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
|
90 100
....*....|....*....|....*..
gi 1988312930 182 DLQGRTALMLACEGASPETVEVLLQGG 208
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHG 213
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
53-226 |
1.57e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.87 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 53 GKSAFHLAAMRGA-ASCLEVMIAHGSNVMSADGAGYNALH--LAAKYGHPQCLKQLLQASCVVDVVDSSGWTALH----- 124
Cdd:PHA03095 83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllks 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 125 HAAaggCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLC--RLLLQQGAAANDQDLQGRTALMLACEGASPETVE 202
Cdd:PHA03095 163 RNA---NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL 239
|
170 180
....*....|....*....|....*.
gi 1988312930 203 V--LLQGGAQPGITDALGQDAAHYGA 226
Cdd:PHA03095 240 VlpLLIAGISINARNRYGQTPLHYAA 265
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
939-1115 |
2.30e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 939 ERIVGTLQANVAQLEGQLEELGRRHEKTSAEV--FQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQ 1016
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1017 EALDKAKEKDKKITElSKEVFNLKEALKEQPAALAT---------PEVEALRDQVKDLQQQL-QEAARDHSSVVALYRSh 1086
Cdd:COG3206 247 AQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAElsarytpnhPDVIALRAQIAALRAQLqQEAQRILASLEAELEA- 324
|
170 180
....*....|....*....|....*....
gi 1988312930 1087 lLYAIQGQMDEDVQRILSQILQMQRLQAQ 1115
Cdd:COG3206 325 -LQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
726-893 |
2.45e-05 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 48.43 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 726 EAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAR---EDLRDRDSRLRELEAasacldeaRASRLLAEeeARG 802
Cdd:pfam04632 167 DALRLAAAALAGAPGAEAFEAARLRLAADILALEALRSHAAfesPRGRARARALRRLLA--------RMLALLPR--LRS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 803 LRAELAQREEARLEQSRELEVLREQLATARATGEQQ---------RTAAAELGRARDAAEARVAELPAACEEARQGLAEL 873
Cdd:pfam04632 237 LARLLARLRTEGAGTVPELAALLDELAAWEAALAAEalqaalaalRARLRALRPALPLDFDTAAELLARLADLLAELAEA 316
|
170 180
....*....|....*....|
gi 1988312930 874 REASEALRQSVVPASEHRRL 893
Cdd:pfam04632 317 LASCRALRHPIAQGARPARL 336
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
772-1104 |
2.62e-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: 48.68 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 772 RDSRLRELEAASACLdEARASRLLAEEEARGLRAelaqREEARLEQSReLEVLREQLATARATGE---QQRTAAAELGRA 848
Cdd:pfam12128 403 REARDRQLAVAEDDL-QALESELREQLEAGKLEF----NEEEYRLKSR-LGELKLRLNQATATPElllQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 849 RDAAEARVAELPAACEEARQGLAELREASEALRQsvvpasEHRRLQeealELRGRAASLEQEVVA---TGKEAARLRAEL 925
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQ------ASRRLE----ERQSALDELELQLFPqagTLLHFLRKEAPD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 926 ERERVCSVALSE-------HERIVGTLQANVAQLEGQLEELGR-RHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQ 997
Cdd:pfam12128 547 WEQSIGKVISPEllhrtdlDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 998 LRGLRTEAERARQAQSRAQEALDKAKEkdkKITELSKEVFNLKEALKEQPAALATPEVEALRD----------QVKDLQQ 1067
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARL---DLRRLFDEKQSEKDKKNKALAERKDSANERLNSleaqlkqldkKHQAWLE 703
|
330 340 350
....*....|....*....|....*....|....*..
gi 1988312930 1068 QLQEAARDHSSVVALYRSHLLYAIQGQMDEDVQRILS 1104
Cdd:pfam12128 704 EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAA 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
805-1034 |
2.98e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 805 AELAQREEARLEQ-SRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQS 883
Cdd:COG4942 19 ADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 884 VVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERErvcsvALSEHERIVGTLQANVAQLEGQLEELGRRH 963
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-----LAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312930 964 EKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSK 1034
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
758-1071 |
3.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 758 LRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQlataratgeq 837
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 838 qrtaAAELGRARDAAEARVaELPAACEEARQGLAELREASEALRQSvvpASEHRRLQEEALELRGRAASLEQEVVATGKE 917
Cdd:PRK03918 282 ----VKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEE---INGIEERIKELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 918 AARLRA---ELERERVCSVALSEHERIVGTLqaNVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERhaaeAQLATA 994
Cdd:PRK03918 354 LEELEErheLYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 995 EQQLRGLR----------TEAERARQAQSRAQEALDKAKEK---DKKITELSKEVFNLKEALKEQPAALAtpeVEALRDQ 1061
Cdd:PRK03918 428 IEELKKAKgkcpvcgrelTEEHRKELLEEYTAELKRIEKELkeiEEKERKLRKELRELEKVLKKESELIK---LKELAEQ 504
|
330
....*....|
gi 1988312930 1062 VKDLQQQLQE 1071
Cdd:PRK03918 505 LKELEEKLKK 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1075 |
3.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 864 EEARQGLAELREASEALRQSVvpasehRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERVcsvALSEHERIVG 943
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 944 TLQANVAQLEGQLEELGRRHEKT-----------SAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQ 1012
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 1013 SRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATpEVEALRDQVKDLQQQLQEAARD 1075
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAE 235
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
53-215 |
3.36e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.95 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 53 GKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHaAAGGCL 132
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI-SVGYCK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 133 ScsevlcsfkahlnpqdrsgatpliiaaqmchTDLCRLLLQQGAAANDQD-LQGRTALMLACEgaSPETVEVLLQGGAQP 211
Cdd:PHA02878 247 D-------------------------------YDILKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYGADI 293
|
....
gi 1988312930 212 GITD 215
Cdd:PHA02878 294 NSLN 297
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
321-459 |
4.24e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 321 RQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSYDVTTLQDEEGELP---DLPGAE 397
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEgraGELAQE 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 398 VLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKdETQMEVEALAEVIPLAL 459
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAKIADLGRRLNVAL 185
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
759-1061 |
5.85e-05 |
|
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: 47.20 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 759 RAALEQAR--EDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAEL---AQREEARLEQSRE-LEVLREQLATAR 832
Cdd:pfam07888 28 RAELLQNRleECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREkHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 833 ATGEQQRTAAAELGRARDAAEARV------------------AELPAACEEARQGLAELREASEALRQS----VVPASEH 890
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIreleediktltqrvlereTELERMKERAKKAGAQRKEEEAERKQLqaklQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 891 RRLQEEALELRGRAASLEQEVVA--------TGKEAARLRAELERERVCSVALSEHERIVGTLQAnVAQLEGQLEELGRR 962
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQlqdtittlTQKLTTAHRKEAENEALLEELRSLQERLNASERK-VEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 963 HEKTSAEVFQVQREALFMKserhaaeAQLATAEQQLRglrteAERARQAQSRaqEALDKAKEKDK-KITELSKEVFNLKE 1041
Cdd:pfam07888 267 RDRTQAELHQARLQAAQLT-------LQLADASLALR-----EGRARWAQER--ETLQQSAEADKdRIEKLSAELQRLEE 332
|
330 340
....*....|....*....|
gi 1988312930 1042 ALKEQPAALATPEVEALRDQ 1061
Cdd:pfam07888 333 RLQEERMEREKLEVELGREK 352
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
707-1019 |
5.91e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 47.32 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 707 LRQREREAAAEleaalgkCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRDRDSRLRELEAASACL 786
Cdd:COG3903 557 LRGLLREGRRW-------LERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAAL 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 787 DEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEA 866
Cdd:COG3903 630 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 867 RQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERVCSVALSEHERIVGTLQ 946
Cdd:COG3903 710 ALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAA 789
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 947 ANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEAL 1019
Cdd:COG3903 790 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAA 862
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
754-897 |
6.50e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 46.26 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 754 DTTQLRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARA 833
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312930 834 TGEQ---QRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEA 897
Cdd:pfam00529 132 LAPIggiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
756-1071 |
8.75e-05 |
|
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: 47.04 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 756 TQLRAALEQAREDLRDRDSRL-RELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARAT 834
Cdd:pfam15921 327 SQLRSELREAKRMYEDKIEELeKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 835 GEQQRTAAAELGRARDAAEARVAELPAACEEARqglaelreaSEALRQsvvpasehrrLQEEALELRGRAASLEQEVVAT 914
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAMK---------SECQGQ----------MERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 915 gkeaARLRAELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVqrealfmkseRHAAEAQLata 994
Cdd:pfam15921 468 ----AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL----------RSRVDLKL--- 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312930 995 eQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEA--LRDQVKDLQQQLQE 1071
Cdd:pfam15921 531 -QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKaqLEKEINDRRLELQE 608
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-487 |
8.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 291 RDAYEEIVRLRQERGRLLQkirgLEQHKERRQQESPEASSLHIL---------ERQVQELQQLLVERQEEKESLGREVES 361
Cdd:COG4913 238 ERAHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLraalrlwfaQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 362 LQSRLSLLENERENtsydvttlqdeegelpdlpgaevlLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILenfek 441
Cdd:COG4913 314 LEARLDALREELDE------------------------LEAQIRGNGGDRLEQLEREIERLERELEERERRRARL----- 364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1988312930 442 detqmevEALAEVIPLALYDSlRAEFDQLRRQHAEALQALRQQETR 487
Cdd:COG4913 365 -------EALLAALGLPLPAS-AEEFAALRAEAAALLEALEEELEA 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
687-1012 |
9.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 687 EASEKLQVELETRIRGLeealrqrereaaaeleaalgkceaAEAEAGRLRERVReaegsgasgggggdttQLRAALEQAR 766
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDL------------------------GEEEQLRVKEKIG----------------ELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 767 EDLRDRDSRLRELEaasacldearasrllaeeearglrAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELG 846
Cdd:TIGR02169 308 RSIAEKERELEDAE------------------------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 847 RARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPA-SEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAEL 925
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 926 ErervcsvalseherivgTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEA 1005
Cdd:TIGR02169 444 E-----------------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
....*..
gi 1988312930 1006 ERARQAQ 1012
Cdd:TIGR02169 507 RGGRAVE 513
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
757-1078 |
1.02e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 757 QLRAALEQAREDLRDRDSRLRELeaaSACLDEARASRLLAEEEARGLRAELAQREEArLEQSRELEVLREQLATARATGE 836
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEM---ARELEELSARESDLEQDYQAASDHLNLVQTA-LRQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 837 QQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEAL-------RQSVVPASEHRRLQEEALELRGRAASLEQ 909
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQALEKARALCGLPDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 910 EVVATGKEAARLRAELE-RERVCSVALSEHERIVGTLQANVAQLEgqleelgrrhektSAEVFQVQREALFMKSERHAAE 988
Cdd:COG3096 445 AFRAKEQQATEEVLELEqKLSVADAARRQFEKAYELVCKIAGEVE-------------RSQAWQTARELLRRYRSQQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 989 AQLATAEQQLRglrtEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATpEVEALRDQVKDLQQQ 1068
Cdd:COG3096 512 QRLQQLRAQLA----ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE-QAAEAVEQRSELRQQ 586
|
330
....*....|
gi 1988312930 1069 LQEAARDHSS 1078
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
774-884 |
1.27e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 774 SRLR-ELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSR-ELEVLREQLATARATGEQQRTAAAELGRARDA 851
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRdELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|...
gi 1988312930 852 AEARVAELPAACEEARQGLAELREASEALRQSV 884
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
757-1117 |
1.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 757 QLRAALEQAREDLRDRDS---RLRELEAASA--CLDEARASRLLAEEEAR--GLRAELAQREEARLEQSRELEVLREQLA 829
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQRaerLLAEFCKRLGknLDDEDELEQLQEELEARleSLSESVSEARERRMALRQQLEQLQARIQ 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 830 TARATGEQQRTAAAELGRARDAAEARVAElPAACEEARQGLAE-LREASEALRQSvvpASEHRRLQEEALELRGRAASLE 908
Cdd:PRK04863 597 RLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQQLLErERELTVERDEL---AARKQALDEEIERLSQPGGSED 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 909 QE---------------------------------------VVATGKEAARLRAELE----------------RERVCSV 933
Cdd:PRK04863 673 PRlnalaerfggvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEdcpedlyliegdpdsfDDSVFSV 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 934 ALSEHERIVGTLQANV--------------------AQLEGQLEELGRRHEKTSAEVFQVQR--EALFMKSERHAA---- 987
Cdd:PRK04863 753 EELEKAVVVKIADRQWrysrfpevplfgraarekriEQLRAEREELAERYATLSFDVQKLQRlhQAFSRFIGSHLAvafe 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 988 ---EAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEK-------------------DKKITELSKEVFNLKEA--- 1042
Cdd:PRK04863 833 adpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetlADRVEEIREQLDEAEEAkrf 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1043 ----------LKEQPAALATP--EVEALRDQVKDLQQQLQEA---ARDHSSVVALyRSHLLYA----IQGQMDEDVQRIL 1103
Cdd:PRK04863 913 vqqhgnalaqLEPIVSVLQSDpeQFEQLKQDYQQAQQTQRDAkqqAFALTEVVQR-RAHFSYEdaaeMLAKNSDLNEKLR 991
|
490
....*....|....
gi 1988312930 1104 SQILQMQRLQAQGR 1117
Cdd:PRK04863 992 QRLEQAEQERTRAR 1005
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
385-618 |
1.45e-04 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 46.01 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 385 DEEGELPDLPgaEVLLSRQLSPSAQEHLASLQeqVAVLTrqnqelMEKVQILENfEKDETQMEVEALAEVIPLALY---- 460
Cdd:PLN03237 1090 DDAAEEEEEI--DVSSSSGVRGSDYDYLLSMA--IGTLT------LEKVQELCA-DRDKLNIEVEDLKKTTPKSLWlkdl 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 461 DSLRAEFDQLRRQHAEALQALRQQetrevprEEGAACGESEvAGATATKNGPThmelngsvAPETKVNGAETIDEEAAgD 540
Cdd:PLN03237 1159 DALEKELDKLDKEDAKAEEAREKL-------QRAAARGESG-AAKKVSRQAPK--------KPAPKKTTKKASESETT-E 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 541 ETMEARTMEAEATGAEA-----TGAEATGAKVTETKPTGAEVREMETTEEEANMETKPTGAQATDTETTGVEAMGVEATK 615
Cdd:PLN03237 1222 ETYGSSAMETENVAEVVkpkgrAGAKKKAPAAAKEKEEEDEILDLKDRLAAYNLDSAPAQSAKMEETVKAVPARRAAARK 1301
|
...
gi 1988312930 616 TKA 618
Cdd:PLN03237 1302 KPL 1304
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
690-1082 |
1.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 690 EKLQVELETRIRGLEEALRQREREAAAELeaalgKCEAAEAEAGRLRERVReaegsgasGGGGGDTTQLRAALEQAREDL 769
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELE--------ELLEQLSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 770 RDRDSRLRELEAAsacLDEARASRLLAEEEARGLRAELaqREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRAR 849
Cdd:COG4717 202 EELQQRLAELEEE---LEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 850 DAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELEREr 929
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 930 vcsvaLSEHERivgtlQANVAQLEGQLEELGRRHEKTSAEVFqvqREALFMKSERHAAEAQLATAEQQLRGLRTEAERAR 1009
Cdd:COG4717 356 -----AEELEE-----ELQLEELEQEIAALLAEAGVEDEEEL---RAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312930 1010 QA------QSRAQEALDKAKEKDKKITELSKEVFNLKEALKEqpaALATPEVEALRDQVKDLQQQLQEAARDHSSVVAL 1082
Cdd:COG4717 423 EAldeeelEEELEELEEELEELEEELEELREELAELEAELEQ---LEEDGELAELLQELEELKAELRELAEEWAALKLA 498
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
766-884 |
1.98e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 766 REDLRDRDSRLRELEAASACLDEARAsrlLAEEEARGLRAELAQreearleqsrelevLREQLATARATGEQQRTAAAEL 845
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLS---LERQGNQDLQDSVAN--------------LRASLSAAEAERSRLQALLAEL 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988312930 846 GRARDAAEARVAELPAACEEARQGLAELREASEALRQSV 884
Cdd:PRK09039 108 AGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-1046 |
2.27e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 690 EKLQVELE------TRIRGLEEALRQREREAAAELEAALGKCEAAEAEAGRLRERVreaegsgasGGGGGDTTQLRAALE 763
Cdd:TIGR02169 684 EGLKRELSslqselRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL---------EELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 764 QAREDLRDRDSRLRELEAASACLDEARAS--RLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTA 841
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 842 AAELGRARDAAEARVAELPAACEEARQGLAELreasealrqsvvpASEHRRLQEEALELRGRAASLEQEVvatGKEAARL 921
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------------EEELEELEAALRDLESRLGDLKKER---DELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 922 RAELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRH--------EKTSAEVFQVQREALfmkserhaaeaqlat 993
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeipeEELSLEDVQAELQRV--------------- 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 994 aEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQ 1046
Cdd:TIGR02169 964 -EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-484 |
2.41e-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: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 292 DAYEEIVRLRQERGRLLQKIRGLEQHKERRQQEspeassLHILERQVQELQQLLVERQEEK--ESLGREVESLQSRLSLL 369
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAE------LDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 370 enerENTSYDVTTLQDEEGELpdlpGAEVLLSRQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVE 449
Cdd:COG4913 681 ----DASSDDLAALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190
....*....|....*....|....*....|....*.
gi 1988312930 450 A-LAEVIPLALYDSLRAEFDQLRRQHAEALQALRQQ 484
Cdd:COG4913 753 ErFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
690-1010 |
2.60e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 690 EKLQVELETRIRGLEEalRQREREAAAELEAALGKCEAAEAEAGRL-----RERVREAEGSGASGGGGGDTTQLRAALEQ 764
Cdd:pfam17380 299 ERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERMamereRELERIRQEERKRELERIRQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 765 AREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRaelaqreearlEQSRELEVLREQLATARatgeQQRTAAAE 844
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ-----------QQKVEMEQIRAEQEEAR----QREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 845 LGRARDAAEARVAELpaaceEARQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAasLEQEVvatgkeAARLRAE 924
Cdd:pfam17380 442 EERAREMERVRLEEQ-----ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKEL------EERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 925 LERERVCSVALSEHERivgTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQlaTAEQQLRGLRTE 1004
Cdd:pfam17380 509 IEEERKRKLLEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM--EREREMMRQIVE 583
|
....*.
gi 1988312930 1005 AERARQ 1010
Cdd:pfam17380 584 SEKARA 589
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
123-205 |
2.93e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 123 LHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVE 202
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1988312930 203 VLL 205
Cdd:PTZ00322 166 LLS 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-487 |
3.12e-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: 44.37 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 295 EEIVRLRQERGRLLQKIRGLEQH-KERRQQESPEASSLHILERQVQELQQLLVERQEEKESLGREVESLQSRLSLLENER 373
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKElAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 374 ENTSYDVTTLQDEEGELPDLPGAEVLLS--------------RQLSPSAQEHLASLQEQVAVLTRQNQELMEKVQILENF 439
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSpedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988312930 440 eKDETQMEVEALAEVIplALYDSLRAEFDQLRRQHAEALQALRQQETR 487
Cdd:COG4942 180 -LAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
767-1084 |
3.56e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 767 EDLRDRDSrLRELEAASACLDEARASRllAEEEA---RGLRAELAQREEARLE-QSRELEVLREQLATARatgEQQRTAA 842
Cdd:pfam07111 325 QDLEHRDS-VKQLRGQVAELQEQVTSQ--SQEQAilqRALQDKAAEVEVERMSaKGLQMELSRAQEARRR---QQQQTAS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 843 AE--LGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELrgraASLEQEVVATGKEAAR 920
Cdd:pfam07111 399 AEeqLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVAL----AQLRQESCPPPPPAPP 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 921 LRAELERErvCSVALSEHERIVGTLQANVAQLEgqlEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLrg 1000
Cdd:pfam07111 475 VDADLSLE--LEQLREERNRLDAELQLSAHLIQ---QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQL-- 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1001 lrteaERARQAQsraQEALDKAKEKDKKITElSKEVFNlkEALKEQPAALATpeveALRDQVKDLQQQLQEAARDHSSVV 1080
Cdd:pfam07111 548 -----EVARQGQ---QESTEEAASLRQELTQ-QQEIYG--QALQEKVAEVET----RLREQLSDTKRRLNEARREQAKAV 612
|
....
gi 1988312930 1081 ALYR 1084
Cdd:pfam07111 613 VSLR 616
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
946-1043 |
3.67e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 946 QANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAErarQAQSRAQEALDKAKEK 1025
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE---QLQEKAAETSQERKQK 217
|
90
....*....|....*...
gi 1988312930 1026 DKKITELSKEVFNLKEAL 1043
Cdd:PRK11448 218 RKEITDQAAKRLELSEEE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
935-1073 |
4.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 935 LSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTE---------- 1004
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkei 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 1005 ---AERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATpEVEALRDQVKDLQQQLQEAA 1073
Cdd:COG1579 99 eslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE-ELAELEAELEELEAEREELA 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
892-1045 |
4.78e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 892 RLQE---EALELRGRAASLEQEVVATGKEAARLRAELErervcsvalsEHERIVGTLQANVAQLEGQLEELGRRHEKTSA 968
Cdd:COG1579 11 DLQEldsELDRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 969 EVFQV--QREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEK-DKKITELSKEVFNLKEALKE 1045
Cdd:COG1579 81 QLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAELEAELEE 160
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
812-1071 |
4.89e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 812 EARLEQ-SRELEVLREQLATARA-TGEQQRTAA----------------------AELGRARDAAEARVAELPAACEEAR 867
Cdd:COG3096 784 EKRLEElRAERDELAEQYAKASFdVQKLQRLHQafsqfvgghlavafapdpeaelAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 868 QGLAELREASEALRQsVVPASEHrrLQEEALELRGRAAsleQEVVATGKEAARLRAElerervCSVALSEHERIVGTLQ- 946
Cdd:COG3096 864 QQLDQLKEQLQLLNK-LLPQANL--LADETLADRLEEL---REELDAAQEAQAFIQQ------HGKALAQLEPLVAVLQs 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 947 --ANVAQLEGQLEELGRRHEKTSAEVFQ----VQREALFMKSErhaAEAQLATAEQQLRGLRTEAERARQAQSRAQEALd 1020
Cdd:COG3096 932 dpEQFEQLQADYLQAKEQQRRLKQQIFAlsevVQRRPHFSYED---AVGLLGENSDLNEKLRARLEQAEEARREAREQL- 1007
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1988312930 1021 kaKEKDKKITELSKEVFNLKEALkeqpaalatpevEALRDQVKDLQQQLQE 1071
Cdd:COG3096 1008 --RQAQAQYSQYNQVLASLKSSR------------DAKQQTLQELEQELEE 1044
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
812-1071 |
5.18e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 812 EARLEQ-SRELEVLREQLATARA-TGEQQRT----------------------AAAELGRARDAAEARVAELPAACEEAR 867
Cdd:PRK04863 785 EKRIEQlRAEREELAERYATLSFdVQKLQRLhqafsrfigshlavafeadpeaELRQLNRRRVELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 868 QGLAELREASEALR----QSVVPASEHrrLQEEALELRGRAASLEqevvatgkEAARLRAELERervcsvALSEHERIVG 943
Cdd:PRK04863 865 SQLEQAKEGLSALNrllpRLNLLADET--LADRVEEIREQLDEAE--------EAKRFVQQHGN------ALAQLEPIVS 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 944 TLQA---NVAQLEGQLEELGRRHEKTSAEVFQ----VQREALFMKSErhaaEAQLATAEQQLR-GLRTEAERARQAQSRA 1015
Cdd:PRK04863 929 VLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFAltevVQRRAHFSYED----AAEMLAKNSDLNeKLRQRLEQAEQERTRA 1004
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312930 1016 QEALdkaKEKDKKITELSKEVFNLKEALkeqpaalatpevEALRDQVKDLQQQLQE 1071
Cdd:PRK04863 1005 REQL---RQAQAQLAQYNQVLASLKSSY------------DAKRQMLQELKQELQD 1045
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
755-977 |
5.51e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 755 TTQLRAALEQAREDLrdrdSRLRELEAASACLDEARAsrllaEEEARGLRAELAQREEARL---EQSRELEVLREQLATA 831
Cdd:COG3096 859 EQQLRQQLDQLKEQL----QLLNKLLPQANLLADETL-----ADRLEELREELDAAQEAQAfiqQHGKALAQLEPLVAVL 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 832 RATGEQQRTAAAELGRA---RDAAEAR-------VAELPA-ACEEARQGLAELREASEALRQSVVPASEHRRLQEEALE- 899
Cdd:COG3096 930 QSDPEQFEQLQADYLQAkeqQRRLKQQifalsevVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRq 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 900 --------------LRGRA-------ASLEQEVVATGKEA---ARLRAELERERVCSvALSEHERIVGTLQANVAQLEGQ 955
Cdd:COG3096 1010 aqaqysqynqvlasLKSSRdakqqtlQELEQELEELGVQAdaeAEERARIRRDELHE-ELSQNRSRRSQLEKQLTRCEAE 1088
|
250 260
....*....|....*....|..
gi 1988312930 956 LEELGRRHEKTSAEVFQVQREA 977
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQEREQV 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
687-882 |
6.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 687 EASEKLQVELETRIRGLEEALRQrereaaaeleaalgkceaAEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAR 766
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEE------------------AEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 767 EDLRDRDSRLRELEAASAcLDEARASRLLAEEEARGLRAELAQREEARLEQSR-------ELEVLREQLATARATGEQQ- 838
Cdd:COG3206 233 AELAEAEARLAALRAQLG-SGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEa 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988312930 839 RTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQ 882
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
185-237 |
6.92e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 6.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 185 GRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLL 237
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
756-1045 |
7.01e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 756 TQLRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARG---------------------LRAELAQREEAR 814
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKalvdelelaqlsannrqelarLRSELAKKRSQQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 815 LEQsrELEVLREQLATARatgeqQRTAAAELGRARDAAEaRVAELPAACEEArqgLAELREASEALRQSV----VPASEH 890
Cdd:PRK10929 220 LDA--YLQALRNQLNSQR-----QREAERALESTELLAE-QSGDLPKSIVAQ---FKINRELSQALNQQAqrmdLIASQQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 891 RRLQEEALELRgraasleqEVVATGKEAARLRAElerervcSVALSEherivgTLQANVA---------QLEGQLEELgr 961
Cdd:PRK10929 289 RQAASQTLQVR--------QALNTLREQSQWLGV-------SNALGE------ALRAQVArlpempkpqQLDTEMAQL-- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 962 rhektsaevfQVQR---EALFmksERHAAEAQLATAEQQlrGLRTEAERARQAQSRAQEALDKA--KEKDKKITELSK-E 1035
Cdd:PRK10929 346 ----------RVQRlryEDLL---NKQPQLRQIRQADGQ--PLTAEQNRILDAQLRTQRELLNSllSGGDTLILELTKlK 410
|
330
....*....|..
gi 1988312930 1036 VFN--LKEALKE 1045
Cdd:PRK10929 411 VANsqLEDALKE 422
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
728-1019 |
8.00e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.47 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 728 AEAEAGRLRERVREAEGSGASGGGGGDTTQLRAALEQAREDLRDRDSRLRELEAASACLDEARA------SRLLAEEEAR 801
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAlapfwfLRGLLREGRR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 802 GLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALR 881
Cdd:COG3903 567 WLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAA 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 882 QSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERVCSVALSEHERIVGTLQANVAQLEGQLEELGR 961
Cdd:COG3903 647 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAA 726
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312930 962 RHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEAL 1019
Cdd:COG3903 727 LLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAA 784
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
760-1036 |
1.00e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 760 AALEQAREDLRDRDSRLRELEAAsacLDEARASRLLAEEEARGLRAELAQREEARLEQS--RELEVLREQLATARATGEQ 837
Cdd:COG0497 151 AGLEELLEEYREAYRAWRALKKE---LEELRADEAERARELDLLRFQLEELEAAALQPGeeEELEEERRRLSNAEKLREA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 838 QRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVpasehrRLQEEALELRGRAASLEQevvatgkE 917
Cdd:COG0497 228 LQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALI------ELEEAASELRRYLDSLEF-------D 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 918 AARLrAELErervcsvalsehERIvgtlqanvaqleGQLEELGRRHEKTSAEVFQVQREAlfmkserhAAE-AQLATAEQ 996
Cdd:COG0497 295 PERL-EEVE------------ERL------------ALLRRLARKYGVTVEELLAYAEEL--------RAElAELENSDE 341
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1988312930 997 QLRGLRTEAERARQAQSRAQEALDKAKEkdKKITELSKEV 1036
Cdd:COG0497 342 RLEELEAELAEAEAELLEAAEKLSAARK--KAAKKLEKAV 379
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
38-93 |
1.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312930 38 LIARKGLVPTKLDPEGKSAFHLAAMRGAASCLEVMIAHGSNVMSADGAGYNALHLA 93
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
76-210 |
1.07e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 76 GSNVMSADGAGYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCS-EVLCSFKAHLNPQDRSGAT 154
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLST 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312930 155 PLIIAAQM-CHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASpeTVEVLLQGGAQ 210
Cdd:PHA02876 445 PLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAE 499
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1075 |
1.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 684 GAAEASEKLQVELETRIRGLEEALRQREREAAAELeaalgKCEAAEAEAGRLRE-RVREAEGSGASGGGGGDTTQLRAAL 762
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-----ELKEKAEEYIKLSEfYEEYLDELREIEKRLSRLEEEINGI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 763 EQAREDLRDRDSRLREL---------------------EAASACLDEARA-SRLLAEEEARGLRAELAQREEARLEQSRE 820
Cdd:PRK03918 327 EERIKELEEKEERLEELkkklkelekrleeleerhelyEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 821 LEVLREQLATARATGEQQRTAAAELGRA--------RDAAE-----------ARVAELPAACEEARQGLAELREASEALR 881
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgRELTEehrkelleeytAELKRIEKELKEIEEKERKLRKELRELE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 882 QSVVPASEHRRLQEEALELRGRAASLE------------------QEVVATGKEAARLRAELERERVCSVALSEHERIVG 943
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKkynleelekkaeeyeklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 944 TLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQaqsRAQEALDKAK 1023
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE---ELAETEKRLE 643
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 1024 EKDKKITELSKEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARD 1075
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-472 |
1.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 295 EEIVRLRQERGRLLQKIrgLEQHKERRQQESPEASSLHILERQVQELQQL---LVERQEEKESLGREVESLQSRLSLLEN 371
Cdd:PRK03918 189 ENIEELIKEKEKELEEV--LREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 372 ERENTSYDVTTLQDEEGELPDLPGAE---VLLSRQLSPSAQE------HLASLQEQVAVLTRQNQELMEKVQILENFEK- 441
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDElreiekRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190
....*....|....*....|....*....|..
gi 1988312930 442 -DETQMEVEALAEviPLALYDSLRAEFDQLRR 472
Cdd:PRK03918 347 lKELEKRLEELEE--RHELYEEAKAKKEELER 376
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
160-265 |
1.40e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 160 AQMCHTDLC-----------RLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALA 228
Cdd:PTZ00322 79 AHMLTVELCqlaasgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988312930 229 GDKLILHLLQEAAQRP------SPPSALTEDDSGEASSQNSMS 265
Cdd:PTZ00322 159 GFREVVQLLSRHSQCHfelganAKPDSFTGKPPSLEDSPISSH 201
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
86-114 |
1.52e-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: 1.52e-03
10 20
....*....|....*....|....*....
gi 1988312930 86 GYNALHLAAKYGHPQCLKQLLQASCVVDV 114
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
102-241 |
1.60e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 102 LKQLLQASCVVDVVD-SSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAAND 180
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 181 QDLQGRTALMLACEGA-SPETVEVLLQGGAQPGITDA-LGQDAAHYGALAGDKLILhLLQEAA 241
Cdd:PHA02878 230 RDKCGNTPLHISVGYCkDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKL-LLEYGA 291
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
112-159 |
1.93e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988312930 112 VDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNPQDRSGATPLIIA 159
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
935-1075 |
2.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 935 LSEHERIVGTLQANVAQLEgQLEELGRRHEKTSAE------------VFQVQREALFMKSERHAAEAQLATAEQQLRGLR 1002
Cdd:COG4913 237 LERAHEALEDAREQIELLE-PIRELAERYAAARERlaeleylraalrLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1003 TEAERARQAQSRAQEALDKAkeKDKKITELSKEVFNLKEALKEQ----------------PAALATPEVEALRDQVKDLQ 1066
Cdd:COG4913 316 ARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERerrrarleallaalglPLPASAEEFAALRAEAAALL 393
|
....*....
gi 1988312930 1067 QQLQEAARD 1075
Cdd:COG4913 394 EALEEELEA 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
683-888 |
2.55e-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: 41.67 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 683 PGAAEASEKLQVELEtRIRGLEEALRQREREAAAELEAALGKCEAAEAEAGRLRERVREAEGSGASGGGGGDTTQ----- 757
Cdd:COG4942 16 AAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiae 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 758 LRAALEQAREDLRD---------RDSRLRELEAASACLDEARASRLLAE---------EEARGLRAELAQREEARLEQSR 819
Cdd:COG4942 95 LRAELEAQKEELAEllralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYlaparreqaEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 820 ELEVLREQLATARATGEQQR----TAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPAS 888
Cdd:COG4942 175 ELEALLAELEEERAALEALKaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
754-1060 |
2.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 754 DTTQLRAALEQAREDLrdrdSRLRELEAASACLDEARASRLLAEEEARGLRAELA----QREEARLEQ-SRELEVLR--- 825
Cdd:PRK04863 859 QEQQQRSQLEQAKEGL----SALNRLLPRLNLLADETLADRVEEIREQLDEAEEAkrfvQQHGNALAQlEPIVSVLQsdp 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 826 EQLATARATGEQ----QRTAAAelgRARDAAE--ARVAELpaACEEARQGLAELREASEALRQSVVPASEHRRLQEEalE 899
Cdd:PRK04863 935 EQFEQLKQDYQQaqqtQRDAKQ---QAFALTEvvQRRAHF--SYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRARE--Q 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 900 LRGRAASLEQevvatgkeAARLRAELErervcsvalSEHErivgTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALF 979
Cdd:PRK04863 1008 LRQAQAQLAQ--------YNQVLASLK---------SSYD----AKRQMLQELKQELQDLGVPADSGAEERARARRDELH 1066
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 980 M-----KSERHAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPE 1054
Cdd:PRK04863 1067 ArlsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLSADE 1146
|
....*.
gi 1988312930 1055 VEALRD 1060
Cdd:PRK04863 1147 LRSMSD 1152
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
86-244 |
2.67e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 41.52 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 86 GYNALHLAAKYGHPQCLKQLLQASCVVDVVDSSGWTALHHAAAGGCLSCSEVLCSFKAHLNpqD---RSGATPLIIAAQM 162
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DvfyKDGMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 163 CHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHYGALAGDKLILHLLQEAAQ 242
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
..
gi 1988312930 243 RP 244
Cdd:PHA02875 193 NI 194
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
86-116 |
3.13e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 36.11 E-value: 3.13e-03
10 20 30
....*....|....*....|....*....|..
gi 1988312930 86 GYNALHLAA-KYGHPQCLKQLLQASCVVDVVD 116
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
171-224 |
3.16e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 171 LLQQG-AAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDALGQDAAHY 224
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
886-999 |
3.55e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 886 PASEHRRLQEEALELRgraasleQEVVATGKEAARLRAELERERVCSVALsehERIVGTLQANVAQLEGQLEELGRRHEK 965
Cdd:PRK11448 140 PENLLHALQQEVLTLK-------QQLELQAREKAQSQALAEAQQQELVAL---EGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1988312930 966 TSAEVFQVQREAlfmkSERHAAEAQLATAE------QQLR 999
Cdd:PRK11448 210 TSQERKQKRKEI----TDQAAKRLELSEEEtrilidQQLR 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
762-937 |
3.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 762 LEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTA 841
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 842 AAELGRARD---AAEARVAEL----------PAACEEARQGLAE-LREASEALRQSvvpASEHRRLQEEALELRGRAASl 907
Cdd:PRK04863 595 IQRLAARAPawlAAQDALARLreqsgeefedSQDVTEYMQQLLErERELTVERDEL---AARKQALDEEIERLSQPGGS- 670
|
170 180 190
....*....|....*....|....*....|
gi 1988312930 908 eqevvatgkEAARLRAelERERVCSVALSE 937
Cdd:PRK04863 671 ---------EDPRLNA--LAERFGGVLLSE 689
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
985-1072 |
3.74e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 985 HAAEAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKekdKKITELSKEVfnlkEALKEQPAALATPEVEALRDQVKD 1064
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQ---AALATAQKEL----ANAQAQALQTAQNNLATAQAALAN 329
|
....*...
gi 1988312930 1065 LQQQLQEA 1072
Cdd:TIGR04320 330 AEARLAKA 337
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
760-1074 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 760 AALEQAREDLRDRDS---RLRELEAASACLDEARaSRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGE 836
Cdd:COG3096 492 QAWQTARELLRRYRSqqaLAQRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 837 QQ----RTAAAELGRARDAAEARVAELPA---ACEEARQGLAELREAS-EAL--RQSVVPASEH-----RRLQEEALELR 901
Cdd:COG3096 571 EQaaeaVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSgEALadSQEVTAAMQQllereREATVERDELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 902 GRAASLEQEV----VATGKEAARLRAEleRERVCSVALSE---------------------HERIVGTLQANVAQLEG-- 954
Cdd:COG3096 651 ARKQALESQIerlsQPGGAEDPRLLAL--AERLGGVLLSEiyddvtledapyfsalygparHAIVVPDLSAVKEQLAGle 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 955 ----------------------------------------------------------------QLEELGRRHEKTSAEV 970
Cdd:COG3096 729 dcpedlyliegdpdsfddsvfdaeeledavvvklsdrqwrysrfpevplfgraarekrleelraERDELAEQYAKASFDV 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 971 FQVQR--EAL--FMKSERHAA-----EAQLATAEQQLRGLRTEAERARQAQSRAQEALDKAKEKdkkitelskevFNLKE 1041
Cdd:COG3096 809 QKLQRlhQAFsqFVGGHLAVAfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ-----------LQLLN 877
|
410 420 430
....*....|....*....|....*....|...
gi 1988312930 1042 ALKEQPAALATPEVEALRDQVKDLQQQLQEAAR 1074
Cdd:COG3096 878 KLLPQANLLADETLADRLEELREELDAAQEAQA 910
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
61-237 |
4.78e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 40.72 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 61 AMR-GAASCLEVMIAHGSNVMSADGAGYNALHLAAKYGHPQCLKQLLqascvVDVVDSSGWTA--LHHAAAGGCLSCSev 137
Cdd:PHA02874 42 AIRsGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVDTSILPIpcIEKDMIKTILDCG-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 138 lcsfkAHLNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGASPETVEVLLQGGAQPGITDAL 217
Cdd:PHA02874 115 -----IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
|
170 180
....*....|....*....|
gi 1988312930 218 GQDAAHYGALAGDKLILHLL 237
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLL 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
805-959 |
5.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 805 AELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAEL---REASEALR 881
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312930 882 QSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAELERERvcsvalSEHERIVGTLQANVAQLEGQLEEL 959
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAEREEL 168
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
777-879 |
5.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.62 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 777 RELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATA-------RATGEQQRT------AAA 843
Cdd:PRK12472 197 REAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAktdeakaRAEERQQKAaqqaaeAAT 276
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988312930 844 ELGRARDAAEARVAELPAACEEARQGLAELREASEA 879
Cdd:PRK12472 277 QLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKA 312
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
786-943 |
5.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 786 LDEArASRL-----LAEEEARGLRAELAQreearleqsreLEVLREQLATARATGEQQRtaAAELGRARDAAEARVAELP 860
Cdd:COG0542 395 IDEA-AARVrmeidSKPEELDELERRLEQ-----------LEIEKEALKKEQDEASFER--LAELRDELAELEEELEALK 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 861 AACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVV-----------ATGKEAARLRAElERER 929
Cdd:COG0542 461 ARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVteediaevvsrWTGIPVGKLLEG-EREK 539
|
170
....*....|....*.
gi 1988312930 930 VcsVALSE--HERIVG 943
Cdd:COG0542 540 L--LNLEEelHERVIG 553
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
290-900 |
5.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 290 DRDAYEEIVRLRQERGRLLQKIRGLEQHKERRQQESPEASS-----------LHILERQVQELQQLLVERQEEKESLGRE 358
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheerreeLETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 359 VESLQSRLSLLENERENT--SYDVTTLQDE--EGELPDLPGAEVLLSRQLS---PSAQEHLA---SLQEQVAVLTRQNQE 428
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaEAGLDDADAEavEARREELEDRDEELRDRLEecrVAAQAHNEeaeSLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 429 LMEKVQILENfEKDETQMEVEALAEVIplalyDSLRAEFDQLRRQHAEALQAL-RQQETREVPREEGAACGESEVAGATA 507
Cdd:PRK02224 361 LREEAAELES-ELEEAREAVEDRREEI-----EELEEEIEELRERFGDAPVDLgNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 508 TKNGPTHMELNGSVAPETKVNGAETIDEEAAGDETMEARTMEAEATGAEATGAEATGAKVTETKPTGAEVREMETtEEEA 587
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 588 NMETKPTGAQATDTETTGVEAMGVEATKTKAEEAEMQAygvgagqaeppvtgttnmEATGSRATGMEstgvsatgvenpg 667
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEA------------------EAEEKREAAAE------------- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 668 veatvpgisagpiLHPGAAEASEKLQvELETRIRGLEEALRQREREAAAELEAalgkcEAAEAEAGRLRERVReaegsga 747
Cdd:PRK02224 563 -------------AEEEAEEAREEVA-ELNSKLAELKERIESLERIRTLLAAI-----ADAEDEIERLREKRE------- 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 748 sgggggdttQLRAALEQAREDLRDRDSRLRELEAAsacLDEARAsrllaeEEARGLRAELAQREEARLEQSRELEVLREQ 827
Cdd:PRK02224 617 ---------ALAELNDERRERLAEKRERKRELEAE---FDEARI------EEAREDKERAEEYLEQVEEKLDELREERDD 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312930 828 LATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEhrRLQEEALEL 900
Cdd:PRK02224 679 LQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE--RMLNETFDL 749
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
152-182 |
5.99e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 35.34 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|..
gi 1988312930 152 GATPLIIAAQMC-HTDLCRLLLQQGAAANDQD 182
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
757-1100 |
6.08e-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: 40.71 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 757 QLRAALEQAREDLRD-RDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARleqsRELEVLREQLATARATg 835
Cdd:COG5185 250 QTSDKLEKLVEQNTDlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIK----KATESLEEQLAAAEAE- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 836 eqqrtaaAELGRARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVVATG 915
Cdd:COG5185 325 -------QELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 916 KEAARLRAELERervcsvalseherivgTLQANVAQLEGQLEELGRRHEKTSAEVFQVQREALFMKSERHAAEaQLATAE 995
Cdd:COG5185 398 QNQRGYAQEILA----------------TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 996 QQLRGLRTEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQpaalatpeVEALRDQVKDLQQQLQEAARD 1075
Cdd:COG5185 461 SQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ--------LEGVRSKLDQVAESLKDFMRA 532
|
330 340
....*....|....*....|....*...
gi 1988312930 1076 HSSVVALYRS---HLLYAIQGQMDEDVQ 1100
Cdd:COG5185 533 RGYAHILALEnliPASELIQASNAKTDG 560
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
771-1026 |
6.20e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 40.35 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 771 DRDSRLRELEAASACLDEARAsRLLAEEEARGLRAELAQREEARLEQSRELEVLREQlatARATGEQQRTAAAELGRARD 850
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARK-RLVAKHGAEISKLEEENREKEKALPKNDDMTIEEA---KRRAAAAAKAKAAALAKQKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 851 AA------EARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEAARLRAE 924
Cdd:PRK07735 80 EGteevteEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 925 LERERVCSVALSEHERIVGTLQANVAQLEGQLEELGRRHEKTSAEVfqvqREALFMKSERHAAEAQLATAEQQLRGLRTE 1004
Cdd:PRK07735 160 TDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKA----KAAAAAKAKAAALAKQKASQGNGDSGDEDA 235
|
250 260
....*....|....*....|..
gi 1988312930 1005 AERARQAQSRAQEALDKAKEKD 1026
Cdd:PRK07735 236 KAKAIAAAKAKAAAAARAKTKG 257
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
759-867 |
6.52e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 40.24 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 759 RAALEQAREDLRDRDSrLRELEAASACLDE--ARASRLLA---EEEARglraelAQREEARLEQSRELEVLREQLATARA 833
Cdd:PRK12472 211 TAAAAAAREAAPLKAS-LRKLERAKARADAelKRADKALAaakTDEAK------ARAEERQQKAAQQAAEAATQLDTAKA 283
|
90 100 110
....*....|....*....|....*....|....
gi 1988312930 834 TGEQQRTAAAELGRARDAAEARVAELPAACEEAR 867
Cdd:PRK12472 284 DAEAKRAAAAATKEAAKAAAAKKAETAKAATDAK 317
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
916-1059 |
6.63e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 916 KEAARLRAELERERvcSVALSEHERivgtlQANVAQLEGQLEELGRRHEKTSAEVfQVQREALFMKSERHAAEAQLATAE 995
Cdd:COG2268 199 RDARIAEAEAERET--EIAIAQANR-----EAEEAELEQEREIETARIAEAEAEL-AKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312930 996 QQLRGLRtEAERARQAQSRAQEALDKAKEKDKKITELSKEVFNLKEALKEQPAALATPEVEALR 1059
Cdd:COG2268 271 AEANAER-EVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
299-488 |
6.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 299 RLRQERGRLLQKIRGLEQHKERRQQESPEASSLHILErQVQELQQLLVERQEEKESLGREVESLQSRLSLLENERENTSY 378
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 379 DvTTLQDEEGELPDLPGAEVLLSRQLSPSAQEhLASLQEQVAVLTRQNQELMEKVQILENFEKDETQMEVEALAEVIpla 458
Cdd:COG3206 262 S-PVIQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL--- 336
|
170 180 190
....*....|....*....|....*....|
gi 1988312930 459 lyDSLRAEFDQLRRQHAEALQALRQQETRE 488
Cdd:COG3206 337 --AQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
872-1045 |
7.05e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 872 ELREASEALRQSVVpasehrRLQEEALELRGRAASLEQEVVATGKEAARLRAELER-ERV------------CSVALSEH 938
Cdd:PHA02562 224 ELVEEAKTIKAEIE------ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfQKVikmyekggvcptCTQQISEG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 939 ERIVGTLQANVAQLEGQLEELGRRHEKTSA---EVFQVQREALFMKSerhaaeaQLATAEQQLRGLRTEAERARQAQSRA 1015
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELKN-------KISTNKQSLITLVDKAKKVKAAIEEL 370
|
170 180 190
....*....|....*....|....*....|.
gi 1988312930 1016 QEA-LDKAKEKDKKITELSKEVFNLKEALKE 1045
Cdd:PHA02562 371 QAEfVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
792-1115 |
7.48e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 792 SRLLAEEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAaceearqGLA 871
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA-------QIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 872 ELREASEALRQSVVPASEHRRLQEEALELRGRAASLEQEVVATGKEaarLRAELERErvcsvaLSEHERivgTLQANVAQ 951
Cdd:pfam01576 275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE---LRSKREQE------VTELKK---ALEEETRS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 952 LEGQLEELGRRH----EKTSAEVFQVQREALFMKSERHAAE---AQLATAEQQLRGLRTEAERARQA--------QSRAQ 1016
Cdd:pfam01576 343 HEAQLQEMRQKHtqalEELTEQLEQAKRNKANLEKAKQALEsenAELQAELRTLQQAKQDSEHKRKKlegqlqelQARLS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1017 EALDKAKEKDKKITELSKEVFNLKEALK--EQPAALATPEVEALRDQVKDLQQQLQEAARDHSSVVALYRS--HLLYAIQ 1092
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNeaEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQleDERNSLQ 502
|
330 340
....*....|....*....|...
gi 1988312930 1093 GQMDEDVQRILSQILQMQRLQAQ 1115
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQ 525
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
875-1112 |
7.83e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 875 EASEALrQSVVPASEHRRLQEEalelrgRAASLEQEVVATGKEAARLRAELERERVCSVALSEHERIvGTLQANVAQLEG 954
Cdd:PRK10929 45 EIVEAL-QSALNWLEERKGSLE------RAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMST-DALEQEILQVSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 955 QLEELGRRHEKTSAEVFQVQREALFMKSERHAAEAQLATAEQQLRGLRTEAERARQAQS---RAQEALDKAKEKDKKITE 1031
Cdd:PRK10929 117 QLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLtalQAESAALKALVDELELAQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 1032 LS----KEVFNLKEALKEQPAALATPEVEALRDQVKDLQQQLQEAARDHSSVVALYRSHLLYAIQGQMdeDVQRILSQIL 1107
Cdd:PRK10929 197 LSannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQF--KINRELSQAL 274
|
....*..
gi 1988312930 1108 --QMQRL 1112
Cdd:PRK10929 275 nqQAQRM 281
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
756-1037 |
8.66e-03 |
|
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: 40.11 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 756 TQLRAALEQAREDLRDRDSRLRELEAASACLDEARASRLLAEEEARGLRAELAQREEARLEQSRELEVLREQL--ATARA 833
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLdlLKAKA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 834 TGEQQRTAAAELG-RARDAAEARVAELPAACEEARQGLAELREASEALRQSVVPASEHRRLQEEALELRgraaSLEQEVV 912
Cdd:pfam05557 149 SEAEQLRQNLEKQqSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLN----ENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 913 ATGKEAARLRAELER-----ERVCSVALsEHERIVGTLQA--NVAQLEGQleELgRRHEKTSAEVFQVQREALFMKSERH 985
Cdd:pfam05557 225 LLKEEVEDLKRKLEReekyrEEAATLEL-EKEKLEQELQSwvKLAQDTGL--NL-RSPEDLSRRIEQLQQREIVLKEENS 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988312930 986 AAEAQLATAEQQLRGLRTEaerARQAQSRAQEALDKAKEKDKKITELSKEVF 1037
Cdd:pfam05557 301 SLTSSARQLEKARRELEQE---LAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
145-192 |
8.80e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 8.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988312930 145 LNPQDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLA 192
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
4-183 |
9.06e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 39.86 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 4 LRARFKKTESQDWGKSDERLLQAVEN-----NDAPRVAALIARKGLVPTKLDPE--------GKSAFHLAAMRGAASCLE 70
Cdd:cd21882 11 LRWYLTDSAYQRGATGKTCLHKAALNlndgvNEAIMLLLEAAPDSGNPKELVNApctdefyqGQTALHIAIENRNLNLVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 71 VMIAHGSNV-MSADGA------------GYNALHLAAKYGHPQCLKQLLQAS---CVVDVVDSSGWTALH-------HAA 127
Cdd:cd21882 91 LLVENGADVsARATGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvlqadNTP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312930 128 AGGCLSCS--EVLCSFKAHLNP-------QDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDL 183
Cdd:cd21882 171 ENSAFVCQmyNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQPL 235
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
777-1043 |
9.48e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 777 RELEAASACLDEARASRLLAEEEARGLRAELAQREE---ARLEQSRELEVLREQLATARATGEQQRTAAAELGRArdaAE 853
Cdd:pfam01576 812 RELEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaASERARRQAQQERDELADEIASGASGKSALQDEKRR---LE 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 854 ARVAELPAACEEArQGLAELreASEALRQSVVPASEhrrLQEEALELRGRAASLEQEVVATGKEAARLRAELERERvcSV 933
Cdd:pfam01576 889 ARIAQLEEELEEE-QSNTEL--LNDRLRKSTLQVEQ---LTTELAAERSTSQKSESARQQLERQNKELKAKLQEME--GT 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 934 ALSEHERIVGTLQANVAQLEGQLEE----------LGRRHEKTSAEVF-QVQ---REALFMKSERHAAEAQLATAEQQLR 999
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQesrerqaankLVRRTEKKLKEVLlQVEderRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1988312930 1000 GLRTEAERARQAQSRAQEALDKAKEKDKKiteLSKEVFNLKEAL 1043
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNES---MNREVSTLKSKL 1081
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
797-1070 |
9.97e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 797 EEEARGLRAELAQREEARLEQSRELEVLREQLATARATGEQQRTAAAELGRARDAAEARVAELPAACEEARQGLAELREA 876
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 877 sealrqsvvpASEHRRLQEEALELRGRAASLEQEVvatgkeaarlrAELERERVCSVALSEHERivgTLQANVAQLEGQL 956
Cdd:COG1340 94 ----------LDELRKELAELNKAGGSIDKLRKEI-----------ERLEWRQQTEVLSPEEEK---ELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312930 957 EELGRRHEK--------TSAEVFQVQREALFMKSERHAAEAQLATAE-QQLRGLRTE-AERARQAQSRAQEALDKAKEKD 1026
Cdd:COG1340 150 EKAKKALEKneklkelrAELKELRKEAEEIHKKIKELAEEAQELHEEmIELYKEADElRKEADELHKEIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988312930 1027 KKITELSKEVFNLKEALKE----QPAALATPEVEALRDQVKDLQQQLQ 1070
Cdd:COG1340 230 EEIIELQKELRELRKELKKlrkkQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| |
