|
Name |
Accession |
Description |
Interval |
E-value |
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
827-946 |
2.50e-37 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 136.26 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 827 AFYASFSEGTAAL--QTVKFNTTYINIGSSYFPEHGYFRAPERGVYLFAVSVEFGPGPGTG-QLVFGGHHRTPVCTTGQ- 902
Cdd:pfam00386 1 AFSAGRTTGLTAPneQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYvSLVKNGQEVVSFYDQPQk 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 296437373 903 GSGSTATVFAMAELQKGERVWFELT--QGSITKRSLSGTAFGGFLM 946
Cdd:pfam00386 81 GSLDVASGSVVLELQRGDEVWLQLTgyNGLYYDGSDTDSTFSGFLL 126
|
|
| EMI |
pfam07546 |
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
55-127 |
2.50e-17 |
|
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.
Pssm-ID: 462204 Cd Length: 69 Bit Score: 77.08 E-value: 2.50e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296437373 55 RNWCPYpmsKLVTLLALCKTEKFLIHSQQPCP---QGAPDCQkvkvMYRMAHKPVYQVKQKVLTSLAWRCCPGYTG 127
Cdd:pfam07546 1 RNVCAY---KVVSCVVVTGTESYVQPVYKPYLtwcAGHRRCS----TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
|
|
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
826-947 |
3.20e-09 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 56.16 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 826 VAFYASFSEGT-AALQTVKFNTTYINIGSSYFPEHGYFRAPERGVYLFAVSVEfgpgpgtgqlVFGGH-------HRTPV 897
Cdd:smart00110 8 SAFSVIRSNRPpPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVE----------SKGRNvkvslmkNGIQV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296437373 898 CTT---------GQGSGStatvfAMAELQKGERVWFELT--QGSITKRSLSGTAFGGFLMF 947
Cdd:smart00110 78 MSTydeyqkglyDVASGG-----ALLQLRQGDQVWLELPdeKNGLYAGEYVDSTFSGFLLF 133
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-675 |
1.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 258 AIRNLSLDVEANRQAISRVQ-DSAVARADFQELgakfEAKVQENTQRVGQLRQDVEdRLHAQHFTLHRSISELQADVDTK 336
Cdd:COG1196 233 KLRELEAELEELEAELEELEaELEELEAELAEL----EAELEELRLELEELELELE-EAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 337 LKRLHKAQEApgtngslvlatpGAGARPEPDSLQARLGQLQRNLSELhmttARREEELQYTLEDMRATLTRHVDEIKELY 416
Cdd:COG1196 308 EERRRELEER------------LEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 417 SESDETFDQISKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQgghadlikyvkdcncQK 496
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---------------EE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 497 LYLDLDVIREGQRDATRALEEtQVSLDERRQLDGSSLQALQNAVDAvslavdahkAEGERARAATSRLRSQVQALDDEVG 576
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEE-EEALLELLAELLEEAALLEAALAE---------LLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 577 ALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLAALFGEEVLEEMSEQTpgplplsyeqirVALQDAASGLQEQALGwd 656
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD------------EVAAAAIEYLKAAKAG-- 572
|
410
....*....|....*....
gi 296437373 657 elaaRVTALEQASEPPRPA 675
Cdd:COG1196 573 ----RATFLPLDKIRARAA 587
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
249-575 |
1.23e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 249 NQSLHSLTQAIRNLSLDVEANRQAISRVQDSAVARADFQElgaKFEAKVQENTQRVGQLRQDVEdRLHAQHFTLHRSISE 328
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIE-QLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 329 LQADVDTKLKRLHKAQEapgtngslvlatpgagarpepdslqaRLGQLQRNLSElhmtTARREEELQYTLEDMRATLTRH 408
Cdd:TIGR02168 808 LRAELTLLNEEAANLRE--------------------------RLESLERRIAA----TERRLEDLEEQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 409 VDEIKELYSESDETFDQISKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQgghadliky 488
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE--------- 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 489 vkdCNCQKLYLDLDVIREGQRDATRALEETQVSLDERRQLDGSSLQA----LQNAVDA---VSL-AVDAHKAEGER---- 556
Cdd:TIGR02168 929 ---LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRrlkrLENKIKElgpVNLaAIEEYEELKERydfl 1005
|
330 340
....*....|....*....|....*
gi 296437373 557 ------ARAATSRLRSQVQALDDEV 575
Cdd:TIGR02168 1006 taqkedLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
373-667 |
3.93e-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: 54.29 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 373 LGQLQRNLSELHM--TTARREEELQYTLEDMRATLTrhVDEIKELYSESDETFDQISKVERQVEELQVN----HTALREL 446
Cdd:TIGR02168 195 LNELERQLKSLERqaEKAERYKELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAElqelEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 447 RVILMEKS------------------------LIMEENKEEVERQLLELNLTLQHLQgghADLIKYVKDCN-CQKLYLDL 501
Cdd:TIGR02168 273 RLEVSELEeeieelqkelyalaneisrleqqkQILRERLANLERQLEELEAQLEELE---SKLDELAEELAeLEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 502 DVIREGQRDATRALEETQVSLDERrqldgssLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVG----- 576
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESR-------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqe 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 577 ALKAAAAEARHEVRQLHSAFAALleDALRHEAVLAALFGEEVLEEMSEQtpgplplsYEQIRVALQDAASGLQeqalgwd 656
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREE--------LEEAEQALDAAERELA------- 485
|
330
....*....|.
gi 296437373 657 ELAARVTALEQ 667
Cdd:TIGR02168 486 QLQARLDSLER 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-756 |
1.04e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 246 RSFNQSLHSLTQAIRNLSLDVEANRQAISRVQDSaVARADFQELGAKFEAKVQENTQRVGQLRQ---DVEDRLHAQHFTL 322
Cdd:pfam15921 176 RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDS-MSTMHFRSLGSAISKILRELDTEISYLKGrifPVEDQLEALKSES 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 323 HRSISELQADVDTKLKRLHKAQEAPGTNgslvLATPGAGARPEPDSLQARLGQLQ-----------RNLSELHMTTAR-- 389
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEITG----LTEKASSARSQANSIQSQLEIIQeqarnqnsmymRQLSDLESTVSQlr 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 390 ---RE---------EELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVerqveeLQVNHTALRELrvilmekSLIM 457
Cdd:pfam15921 331 selREakrmyedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL------LADLHKREKEL-------SLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 458 EENK-------------EEVERQLLELNLTLQHLQGghadLIKYVKDcNCQ-KLYLDLDVIR------EGQRDATRALEE 517
Cdd:pfam15921 398 EQNKrlwdrdtgnsitiDHLRRELDDRNMEVQRLEA----LLKAMKS-ECQgQMERQMAAIQgkneslEKVSSLTAQLES 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 518 TQVSLDERRQLDGSSLQALQNAVDAVSlAVDAHKAEGERARAAT----SRLRSQVqalDDEVGALKAAAAEARHeVRQLH 593
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVS-DLTASLQEKERAIEATnaeiTKLRSRV---DLKLQELQHLKNEGDH-LRNVQ 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 594 SAFAALLEDALRHEAVLAALfgEEVLEEMSE------QTPGPLPLSYEQIRVALQDAASGLQEQALGWD-------ELAA 660
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEIL--RQQIENMTQlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirELEA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 661 RVT--ALEQASEPPRPAEHLEPSHDAGREEAATTALAGLAR-ELQSLSNDVKNVGRCCEAEAGAGAASLNAslhgLHNAL 737
Cdd:pfam15921 626 RVSdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRnELNSLSEDYEVLKRNFRNKSEEMETTTNK----LKMQL 701
|
570
....*....|....*....
gi 296437373 738 FATQRSLEQHQRLFHSLFG 756
Cdd:pfam15921 702 KSAQSELEQTRNTLKSMEG 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
362-676 |
2.29e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 362 ARPEPDSLQARLGQLQRNLSEL--HMTTARREEE-------LQYTLEDMRATLtrHVDEIKELYSESDETFDQISKVERQ 432
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKrqQLERLRREREkaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 433 VEELQVNHTALR----ELRVILMEKSL-IMEENKEE---VERQLLELNLTLQHLQGGHADLIKYVKDCN--CQKLYLDLD 502
Cdd:TIGR02169 253 LEKLTEEISELEkrleEIEQLLEELNKkIKDLGEEEqlrVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 503 VIREGQRDATRALEETQVsldERRQLdGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAA 582
Cdd:TIGR02169 333 KLLAEIEELEREIEEERK---RRDKL-TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 583 AEARHEVRQLHSAFAALLEDALRHEAVLAALFG--EEVLEEMSEQTP---------GPLPLSYEQIRVALQDAASGLQEQ 651
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEekEDKALEIKKQEWkleqlaadlSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340
....*....|....*....|....*
gi 296437373 652 ALGWDELAARVTALEQASEPPRPAE 676
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVE 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-670 |
2.86e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 402 RATLTRHVDEIKELYSESDETFDQISKVERQVEELQvnhTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLqgg 481
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELE---EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 482 hADLIKYVKDCNCQKLYLDLDviREGQRDATRALEETQVSLDERRQLDGSSLQALQNAVDAVSlavDAHKAEGERARAAT 561
Cdd:TIGR02168 750 -AQLSKELTELEAEIEELEER--LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 562 SRLRSQVQALDDEvgalkaaaaeaRHEVRQLHSAFAALLEDALRHEAVLAALfgEEVLEEMSEQTPGPLPLsYEQIRVAL 641
Cdd:TIGR02168 824 ERLESLERRIAAT-----------ERRLEDLEEQIEELSEDIESLAAEIEEL--EELIEELESELEALLNE-RASLEEAL 889
|
250 260
....*....|....*....|....*....
gi 296437373 642 QDAASGLQEQALGWDELAARVTALEQASE 670
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-670 |
9.22e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 388 ARREE-ELQytLEDMRATLTRHVDEIKEL-------------------YSESDETFD------QISKVERQVEELQVNHT 441
Cdd:COG1196 172 ERKEEaERK--LEATEENLERLEDILGELerqleplerqaekaeryreLKEELKELEaellllKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 442 ALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKYVkdcncQKLYLDLDVIREGQRDATRALEETQVS 521
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-----ARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 522 LDE----------RRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAAAEARHEVRQ 591
Cdd:COG1196 325 LAEleeeleeleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296437373 592 LHSAFAALLEDALRHEAVLAALFGEEVLEEMSEqtpgplplsyEQIRVALQDAASGLQEQALGWDELAARVTALEQASE 670
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEE----------EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-576 |
3.09e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 262 LSLDVEANRQAISRVQDSavaRADFQELGAKFEAKVQENTQRVGQLRQDVEDrlhaqhftLHRSISEL----QADVDTKL 337
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQ---LASLEEELEKLTEEISELEKRLEEIEQLLEE--------LNKKIKDLgeeeQLRVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 338 KRLHKAQEapgtngslvlatpgagarpepdSLQARLGQLQRNLSELHMTTARREEELQYTLEDMR------ATLTRHVDE 411
Cdd:TIGR02169 297 GELEAEIA----------------------SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereiEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 412 IKELYSESDETFDqisKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKYVKD 491
Cdd:TIGR02169 355 LTEEYAELKEELE---DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 492 CNCQKLYLD--LDVIREGQRDATRALEETQVSL-DERRQL--DGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRS 566
Cdd:TIGR02169 432 IEAKINELEeeKEDKALEIKKQEWKLEQLAADLsKYEQELydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
330
....*....|
gi 296437373 567 QVQALDDEVG 576
Cdd:TIGR02169 512 VEEVLKASIQ 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
254-670 |
3.84e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 254 SLTQAIRNLSLD-VEANRQAISRVQDSAvARADFQELgAKFEAKVQENTQRVGQLRQDVE--DRLHAQHFTLHRSISELQ 330
Cdd:COG4717 38 TLLAFIRAMLLErLEKEADELFKPQGRK-PELNLKEL-KELEEELKEAEEKEEEYAELQEelEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 331 ADVDtKLKRLHKAQEAPGTNGSLvlatpgagaRPEPDSLQARLGQLQRNLSELHmTTARREEELQYTLEDMRATLTRHVD 410
Cdd:COG4717 116 EELE-KLEKLLQLLPLYQELEAL---------EAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 411 --------EIKELYSESDETFDQISKVERQVEELQVNHTALRElRVILMEKSLIMEENKEEVERQLLELN-----LTLQH 477
Cdd:COG4717 185 qlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLiaaalLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 478 LQGGHADLIKYVKD---------------CNCQKLYLDLDVIREGQRDATRALEETQVS--LDERRQLDGSSLQALQNAV 540
Cdd:COG4717 264 LGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 541 DAVSLAVDAH-KAEGERARAATSRLRSQVQALDDEVG-------ALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLAA 612
Cdd:COG4717 344 DRIEELQELLrEAEELEEELQLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 613 LFGEEVLEEMSEQTPGPLPLSYEQIRVALQDAAS--GLQEQALGWDELAARVTALEQASE 670
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAEleAELEQLEEDGELAELLQELEELKA 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-555 |
1.25e-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: 46.21 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 295 AKVQENTQRVGQLRQDVEdRLHAQHFTLhrsiSELQADVDTKLKRLHKAQEApgtngslvlatpgagARPEPDSLQARLG 374
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIE-QLEQEEEKL----KERLEELEEDLSSLEQEIEN---------------VKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 375 QLQRNLSELhmttarrEEELqytlEDMRATLTRH-VDEIKELYSESDETFDQISK----VERQVEELQVNHTALRELRVI 449
Cdd:TIGR02169 769 ELEEDLHKL-------EEAL----NDLEARLSHSrIPEIQAELSKLEEEVSRIEArlreIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 450 LMEKSLIMEENK--------------EEVERQLLELNLTLQHLQGGHADLIKyvkdcncqklylDLDVIREGQRDATRAL 515
Cdd:TIGR02169 838 LQEQRIDLKEQIksiekeienlngkkEELEEELEELEAALRDLESRLGDLKK------------ERDELEAQLRELERKI 905
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 296437373 516 EETQVSLDERRQLDGSSLQALQNAVDAVSlAVDAHKAEGE 555
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELS-EIEDPKGEDE 944
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
250-574 |
1.66e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 250 QSLHSLTQAIRNLSLDVEANRQAisrvqdsavaRADFQElgakfeaKVQENTQRVGQLRQDVEDRLHAQHF------TLH 323
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----------REELAE-------EVRDLRERLEELEEERDDLLAEAGLddadaeAVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 324 RSISELQADVDTKLKRLHKAQEAPGTngslvlatpgagARPEPDSLQARLGQLQRNLSELHMTTARREEELQYT---LED 400
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQA------------HNEEAESLREDADDLEERAEELREEAAELESELEEAreaVED 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 401 MRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTALRElRVILMEKSLIMEENKEEVERQLLELNLTL---QH 477
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE-REAELEATLRTARERVEEAEALLEAGKCPecgQP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 478 LQG-GHADLIKyvkDCNCQKLYLDLDviREGQRDATRALEETQVSLDERRQLDgSSLQALQNAVDAVSLAVDAHKAEGER 556
Cdd:PRK02224 461 VEGsPHVETIE---EDRERVEELEAE--LEDLEEEVEEVEERLERAEDLVEAE-DRIERLEERREDLEELIAERRETIEE 534
|
330
....*....|....*...
gi 296437373 557 ARAATSRLRSQVQALDDE 574
Cdd:PRK02224 535 KRERAEELRERAAELEAE 552
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
390-527 |
1.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 390 REEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTALRELRVIL--MEKSL-IMEENKEEVER 466
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELesLEGSKrKLEEKIRELEE 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296437373 467 QLLELNLTLQHLQGGHADLIKYVKDcncQKLYLDLDVIREGQRDATRALEETQVSLDERRQ 527
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEK---AEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
364-567 |
2.58e-04 |
|
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: 44.50 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 364 PEPDSLQARLGQLQRNLSELH----MTTARREEELQYT------LEDMRATLTRHVDEIKELYSESDEtfdQISKVERQV 433
Cdd:pfam07888 27 PRAELLQNRLEECLQERAELLqaqeAANRQREKEKERYkrdreqWERQRRELESRVAELKEELRQSRE---KHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 434 EELQVNHTALRELRVILMEKslimeenKEEVERQLLELNLTLQHLqgGHADLIKYVkdcncqklylDLDVIREGQRDATR 513
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQ-------RAAHEARIRELEEDIKTL--TQRVLERET----------ELERMKERAKKAGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296437373 514 ALEETQvslDERRQLDGSSLQALQnavDAVSLAVDAHKAEGERARAATSRLRSQ 567
Cdd:pfam07888 165 QRKEEE---AERKQLQAKLQQTEE---ELRSLSKEFQELRNSLAQRDTQVLQLQ 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-628 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 352 SLVLATPGAGARPEPDSLQARLGQLQRNLselhmttarreEELQYTLEDMRAtltrhvdEIKELYSESDETFDQISKVER 431
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEI-----------AELEKELAALKK-------EEKALLKQLAALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 432 QVEELQvnhtalRELRVIlmekslimEENKEEVERQLLELNLTLQHLQGGHADLIKYVkdcncQKL----YLDLDVIREG 507
Cdd:COG4942 70 RIRALE------QELAAL--------EAELAELEKEIAELRAELEAQKEELAELLRAL-----YRLgrqpPLALLLSPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 508 QRDATRALEETQVSLDERRQLdGSSLQALQNAVDAVSLAVDAHKAEGERARAatsRLRSQVQALDDEVGALKAAAAEARH 587
Cdd:COG4942 131 FLDAVRRLQYLKYLAPARREQ-AEELRADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 296437373 588 EVRQLHSAFAALLEDALRHEAVLAALfgEEVLEEMSEQTPG 628
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARL--EAEAAAAAERTPA 245
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
272-617 |
4.59e-04 |
|
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: 43.79 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 272 AISRVQDSAVARADFQELGAKFEAKVQENTQ-RVGQLRQDVE--DRLHAQHFTLHRSISELQADVDTKLKRLHKAQEApg 348
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDlRLEKLGENAEssKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAT-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 349 TNGSLVLATPGAgarpepdslqarLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELY-----SESDETF 423
Cdd:COG5185 312 ESLEEQLAAAEA------------EQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVgevelSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 424 DQISK-VERQVEELQVNHTALRELRVILMEKsliMEENKEEVERQLLELNLTLqhlqgghadlikyvkdcncqklyldld 502
Cdd:COG5185 380 DSFKDtIESTKESLDEIPQNQRGYAQEILAT---LEDTLKAADRQIEELQRQI--------------------------- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 503 viregqRDATRALEETQVSLDE--------RRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARaatSRLRSQVQALDDE 574
Cdd:COG5185 430 ------EQATSSNEEVSKLLNEliselnkvMREADEESQSRLEEAYDEINRSVRSKKEDLNEEL---TQIESRVSTLKAT 500
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 296437373 575 VGALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLAALFGEE 617
Cdd:COG5185 501 LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
250-570 |
6.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 250 QSLHSLTQAIRNLSLDVEANRQAISRV--QDSAVARADFQELGAKFE---AKVQENTQRVGQLRQDVEDrlhaqhftLHR 324
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEelqQRLAELEEELEEAQEELEE--------LEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 325 SISELQAD--VDTKLKRLHKAQEAPGTNGSLVL-----ATPGAGARPEPDSLQARLG--------------QLQRNLSEL 383
Cdd:COG4717 228 ELEQLENEleAAALEERLKEARLLLLIAAALLAllglgGSLLSLILTIAGVLFLVLGllallflllarekaSLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 384 HMTTAR---REEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHtALRELRVILMEKSLIMEE- 459
Cdd:COG4717 308 QALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEe 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 460 --NKEEVERQLLELNLTLQHLQgghADLIKYVKDCNCQKLYLDLDVIREGQRDATRALEETQVSLDERRQldgsSLQALQ 537
Cdd:COG4717 387 lrAALEQAEEYQELKEELEELE---EQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE----ELAELE 459
|
330 340 350
....*....|....*....|....*....|...
gi 296437373 538 NAVDAVSLAVDAHKAEGERARAAtSRLRSQVQA 570
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELK-AELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
395-662 |
6.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 395 QYTLEDmRATLTRhVDEIKELYSESDETFDQISKVERQVEELQV---NHTALRELRVILMEKSLIMEE-NKEEVERQLLE 470
Cdd:COG4913 215 EYMLEE-PDTFEA-ADALVEHFDDLERAHEALEDAREQIELLEPireLAERYAAARERLAELEYLRAAlRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 471 LNLTLQHLQGghadlikyvkdcncqklylDLDVIREGQRDATRALEETQVSLDE----RRQLDGSSLQALQNAVDAVSLA 546
Cdd:COG4913 293 LEAELEELRA-------------------ELARLEAELERLEARLDALREELDEleaqIRGNGGDRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 547 VDAHKAEGERARAATSRL-------RSQVQALDDEVGALKAAAAEARHEVRQLHSAFAALLEDALRHEAVLaalfgEEVL 619
Cdd:COG4913 354 LEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL-----EAEI 428
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 296437373 620 EEMsEQTPGPLPLSYEQIRVALqdaasglqEQALGWDELAARV 662
Cdd:COG4913 429 ASL-ERRKSNIPARLLALRDAL--------AEALGLDEAELPF 462
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-596 |
9.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 412 IKELYSESDETFDQISKVERQVEELQVNHTALRELRVIL--MEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLikyv 489
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLDASSDDL---- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 490 kdcncQKLYLDLDVIREGQRDATRALEETQV---SLDERRQLDGSSLQALQNAVDAVSLAVDAH---KAEGERARAATSR 563
Cdd:COG4913 688 -----AALEEQLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRLEAAEDLARLElraLLEERFAAALGDA 762
|
170 180 190
....*....|....*....|....*....|....
gi 296437373 564 LRSQV-QALDDEVGALKAAAAEARHEVRQLHSAF 596
Cdd:COG4913 763 VERELrENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-444 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 264 LDVEANRQAISRVQDsavARADFQELGAKFEAKVQENTQRVGQLRQDvEDRLHAQHFTL-HRSISELQADVDTKLKRLhk 342
Cdd:COG4913 281 LRLWFAQRRLELLEA---ELEELRAELARLEAELERLEARLDALREE-LDELEAQIRGNgGDRLEQLEREIERLEREL-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 343 aqeapgtngslvlatpgagarpepDSLQARLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELYSESDET 422
Cdd:COG4913 355 ------------------------EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
170 180
....*....|....*....|..
gi 296437373 423 FDQISKVERQVEELQVNHTALR 444
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLE 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
368-667 |
1.02e-03 |
|
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: 42.90 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 368 SLQARLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELYSESD-ETFDQ---ISKVERQVEELQVNHTAL 443
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgELSAAdaaVAKDRSELEALEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 444 RELRVilmEKSLIMEENKEEVERQLLELNLTLQHLQGGHADL--------IKYVKDCN--CQKLYLDLDVIREGqRDATR 513
Cdd:pfam12128 335 LDADI---ETAAADQEQLPSWQSELENLEERLKALTGKHQDVtakynrrrSKIKEQNNrdIAGIKDKLAKIREA-RDRQL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 514 ALEETQVSLDE---RRQLDGSSLQAlqnAVDAVSLAVDAHKAEGERARA-ATSRLRSQVQALDDEVGALKAAAAEARHEV 589
Cdd:pfam12128 411 AVAEDDLQALEselREQLEAGKLEF---NEEEYRLKSRLGELKLRLNQAtATPELLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 590 RQLHSAFAALleDALRHEAVLAALFGEEVLEEMSEQTpgplplsyEQIRVALqDAASG-----LQEQALGWDELAARVTA 664
Cdd:pfam12128 488 ERLQSELRQA--RKRRDQASEALRQASRRLEERQSAL--------DELELQL-FPQAGtllhfLRKEAPDWEQSIGKVIS 556
|
...
gi 296437373 665 LEQ 667
Cdd:pfam12128 557 PEL 559
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
362-666 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 362 ARPEPDSLQARLGQLQRNLSELHMTTARREEELQY---TLEDMRATLTRH---VDEIKELYSESDETFDQISKVERQVEE 435
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQareTRDEADEVLEEHeerREELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 436 LQvnhTALRELRVILMEkslIMEENKEEVERQLLElnltlqhlqgghadlikyvkdcncqklylDLDViregqrdatRAL 515
Cdd:PRK02224 277 LA---EEVRDLRERLEE---LEEERDDLLAEAGLD-----------------------------DADA---------EAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 516 EETQVSLDERRQldgsslqALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAAAEARHEVRQLHSA 595
Cdd:PRK02224 313 EARREELEDRDE-------ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296437373 596 FAALledalrheavlaalfgEEVLEEMSEQtpgplplsYEQIRVALQDAASGLQEQALGWDELAARVTALE 666
Cdd:PRK02224 386 IEEL----------------EEEIEELRER--------FGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-479 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 250 QSLHSLTQAIRNLSLDVEANRQ---AISRVQ-------DSAVARADFQELGAKFEA------KVQENTQRVGQLRQDVED 313
Cdd:COG4913 624 EELAEAEERLEALEAELDALQErreALQRLAeyswdeiDVASAEREIAELEAELERldassdDLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 314 rLHAQHFTLHRSISELQ---ADVDTKLKRLHKAQEAPGTNGSLVLATPGAGARPEPDsLQARLGQLQRNLSELHMTTARR 390
Cdd:COG4913 704 -LEEELDELKGEIGRLEkelEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDAVERELRENLEERIDALRAR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 391 EEELQytlEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNH-----TALRELRVILMEKSLI-----MEEN 460
Cdd:COG4913 782 LNRAE---EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGlpeyeERFKELLNENSIEFVAdllskLRRA 858
|
250
....*....|....*....
gi 296437373 461 KEEVERQLLELNLTLQHLQ 479
Cdd:COG4913 859 IREIKERIDPLNDSLKRIP 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
370-667 |
1.83e-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: 42.25 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 370 QARLGQLQRNLSELHMTTARREEELqytlEDMRATLTRHVDEIKELYSesdetfdQISKVERQVEELQVN----HTALRE 445
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEEVDSLKS-------QLADYQQALDVQQTRaiqyQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 446 LrvilmekslimeenkEEVERQLLELNLTLQHLQGGHADLikyvkdcncqklyldldVIREGQRDATRALEETQVSLDE- 524
Cdd:COG3096 422 L---------------EKARALCGLPDLTPENAEDYLAAF-----------------RAKEQQATEEVLELEQKLSVADa 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 525 -RRQLDgSSLQALQNAVDAVSLAvDAHkaegERARAATSRLRSQvQALDDEVGALKAAAAEARHEVRQLHSAFAALLEDA 603
Cdd:COG3096 470 aRRQFE-KAYELVCKIAGEVERS-QAW----QTARELLRRYRSQ-QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC 542
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296437373 604 LRHEAVLAALfgEEVLEEMSEQtpgplplsyEQIRVALQDAASGLQEQALGW----DELAARVTALEQ 667
Cdd:COG3096 543 QRIGQQLDAA--EELEELLAEL---------EAQLEELEEQAAEAVEQRSELrqqlEQLRARIKELAA 599
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
367-472 |
2.85e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.20 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 367 DSLQARLGQLQRNLSE--LHMTTARRE-EELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTAL 443
Cdd:pfam10473 27 ENLERELEMSEENQELaiLEAENSKAEvETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSL 106
|
90 100 110
....*....|....*....|....*....|...
gi 296437373 444 RELRVIL-MEKSLIMEENKEEVE---RQLLELN 472
Cdd:pfam10473 107 ENLLEEKeQEKVQMKEESKTAVEmlqTQLKELN 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-471 |
4.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 389 RREEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQVNHTALRELRVILME----KSLIMEENKEEV 464
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKL 389
|
....*..
gi 296437373 465 ERQLLEL 471
Cdd:PRK03918 390 EKELEEL 396
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
499-688 |
4.22e-03 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 41.00 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 499 LDLDVIREGQRDATRALEETQVSLDERRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGAL 578
Cdd:COG1020 56 ALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 579 KAAAAEARHEVRQLHSAFAALLEDALrHEAVLAALFGEEVLEEMSEQTPGPLPLSYEQIRVALQDAASGLQEQALGW-DE 657
Cdd:COG1020 136 LLLLLLLLLLLLALHHIISDGLSDGL-LLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWrQQ 214
|
170 180 190
....*....|....*....|....*....|.
gi 296437373 658 LAARVTALEQASEPPRPAehlEPSHDAGREE 688
Cdd:COG1020 215 LAGLPPLLELPTDRPRPA---VQSYRGARVS 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
250-527 |
4.50e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 250 QSLHSLTQAIRNLSLDVEANRQAISRVQD--SAVARADFQELGAKFEAKVQ----ENTQRVGQLRQDVEDRLHAQHFTLH 323
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKlqpeQDLQDVRLHLQQCSQELALKLTALH 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 324 RSISELQADVDTKLKRLHKAQEapgtngslvlATPGAGARPEPDSLQARLGQLQRNLSELHMTTARREEELQYTLEdmra 403
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLP----------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE---- 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 404 tLTRHVDEIkELYSESdetfdQISKVERQVEELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHA 483
Cdd:TIGR00618 716 -YDREFNEI-ENASSS-----LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQ 788
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 296437373 484 DLIKYVKDcNCQKLYLDLDVIREGQRDATRALEETQVSLDERRQ 527
Cdd:TIGR00618 789 FFNRLREE-DTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
362-644 |
5.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 362 ARPEPDSLQARLGQLQRNLSELHMTTARREEELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKVERQVEELQvnhT 441
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 442 ALRELRvilmEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKyvkdcNCQKLYLDLDVIREGQRDATRALEETQVS 521
Cdd:COG4372 88 QLQAAQ----AELAQAQEELESLQEEAEELQEELEELQKERQDLEQ-----QRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 522 LDERRQldgsSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQALDDEVGALKAAAAEARHEVRQLHSAFAALLE 601
Cdd:COG4372 159 LESLQE----ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 296437373 602 DALRHEAVLAALFGEEVLEEMSEQTPGPLPLSYEQIRVALQDA 644
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-527 |
6.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 369 LQARLGQLQRNLSELHMTTARREEELQY---------TLEDMR------ATLTRHVDEIKELYSESDETFDQISKVERQV 433
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDAlqerrealqRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 434 EELQVNHTALRELRVILMEKSLIMEENKEEVERQLLELNLTLQHLQGGHADLIKYvkdcNCQKLYLDLDvIREGQRDATR 513
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAAL-GDAVERELRE 769
|
170
....*....|....
gi 296437373 514 ALEETQVSLDERRQ 527
Cdd:COG4913 770 NLEERIDALRARLN 783
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-667 |
7.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 386 TTARRE--------EELQYTLEDMRATLTRHVDEIKELYSESDETFDQISKV---ERQVEELQVNHTALRELRVILMEKS 454
Cdd:PRK04863 289 LELRRElytsrrqlAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtaLRQQEKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 455 LIME---ENKEEVERQLLELNLTLQHLQGGHADL-----------IKY---------VKDCnCQKLYLDLDVIREGQRDA 511
Cdd:PRK04863 369 EVVEeadEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraIQYqqavqalerAKQL-CGLPDLTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 512 TRALEE-TQVSLDERRQLDGSS---------LQALQNAVDAVSlAVDAHkaegERARAATSRLRSQvQALDDEVGALKAA 581
Cdd:PRK04863 448 QAKEQEaTEELLSLEQKLSVAQaahsqfeqaYQLVRKIAGEVS-RSEAW----DVARELLRRLREQ-RHLAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 582 AAEARHEVRQLHSAFAALLEDALRHEAVLAAlfgEEVLEEMSEQtpgplplsYEQIRVALQDAASGLQEQALG----WDE 657
Cdd:PRK04863 522 LSELEQRLRQQQRAERLLAEFCKRLGKNLDD---EDELEQLQEE--------LEARLESLSESVSEARERRMAlrqqLEQ 590
|
330
....*....|
gi 296437373 658 LAARVTALEQ 667
Cdd:PRK04863 591 LQARIQRLAA 600
|
|
| PHA01547 |
PHA01547 |
putative internal virion protein A |
256-362 |
7.63e-03 |
|
putative internal virion protein A
Pssm-ID: 177311 Cd Length: 206 Bit Score: 38.87 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 256 TQAIRNLsldVEANRQAISRVQDSAVARADFQELGAKFEAKVQENTQRVGQLRQDVEDRLHAQHFTLHRSISELQAdvDT 335
Cdd:PHA01547 62 KQAAKSL---QEAKRMAMLAGGSAAAQAAAAGVKGASVDAVALDIDREVGEALVQIDQNLDAQMYNLANQIRSIQA--QA 136
|
90 100
....*....|....*....|....*..
gi 296437373 336 KLKRLHKAQEAPGTNGSLVLATPGAGA 362
Cdd:PHA01547 137 KAGLLGQKSTTAGQRSPLLAGLMSAGS 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-601 |
9.53e-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: 39.77 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 287 QELGAKFEAKV---QENTQRVGQLRQDVED---RLHAQHFTLHRSISELQADVDTKLKRLHKAQEApgTNGSLVLATPGA 360
Cdd:pfam01576 179 SKLKNKHEAMIsdlEERLKKEEKGRQELEKakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE--LQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 361 GARPEP----DSLQARLGQLQRNLSELHMTTARRE----------EELQYTLED----------MRATLTRHVDEIKELY 416
Cdd:pfam01576 257 AQKNNAlkkiRELEAQISELQEDLESERAARNKAEkqrrdlgeelEALKTELEDtldttaaqqeLRSKREQEVTELKKAL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 417 SESDETFDQiskverQVEELQVNHT-ALRELRVILMEKS---LIMEENKEEVERQLLELNLTLQHLQGGHADlikyvkdc 492
Cdd:pfam01576 337 EEETRSHEA------QLQEMRQKHTqALEELTEQLEQAKrnkANLEKAKQALESENAELQAELRTLQQAKQD-------- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437373 493 ncqklyldldvIREGQRDATRALEETQVSLDE---RRQLDGSSLQALQNAVDAVSLAVDAHKAEGERARAATSRLRSQVQ 569
Cdd:pfam01576 403 -----------SEHKRKKLEGQLQELQARLSEserQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
330 340 350
....*....|....*....|....*....|..
gi 296437373 570 ALDDEVGALKAAAAEARHEVRQLHSAFAALLE 601
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
|
| |
