|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
7.58e-107 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 325.41 E-value: 7.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 81 ITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273 81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 1370513639 161 ILSMIEEAAGTR 172
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-724 |
6.73e-88 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 299.58 E-value: 6.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463 80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 562 KLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAF 641
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKIEFFAICDTE 721
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
...
gi 1370513639 722 VKE 724
Cdd:pfam02463 715 LKL 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-713 |
5.15e-81 |
|
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: 280.40 E-value: 5.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKASV 79
Cdd:TIGR02168 2 LKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 80 SITFDNSDKkqsPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPP 159
Cdd:TIGR02168 80 ELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQF 239
Cdd:TIGR02168 156 ERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 240 LLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI--------------------LRSL 299
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqkqilrerLANL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 300 EDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQH 379
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 380 FNAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEvkkmdsgyrKDQEALEAVKRLKE 459
Cdd:TIGR02168 395 IASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEALE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 460 KLEAEMKKlnyeenKEESLLEKRRQLSRDIGRLKETyEALLARFPNLRFAYKDPEKN-WNRNCVKGLVASLISVkDTSAT 538
Cdd:TIGR02168 465 ELREELEE------AEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNqSGLSGILGVLSELISV-DEGYE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 539 TALELVAGERLYNVVVDTEVTGKK---LLERGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVEYKPE 615
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPK 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 616 LQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENEL 695
Cdd:TIGR02168 614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
730
....*....|....*...
gi 1370513639 696 RALEEELAGLKNTAEKIE 713
Cdd:TIGR02168 694 AELEKALAELRKELEELE 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-713 |
7.89e-76 |
|
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: 265.78 E-value: 7.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK-NGQAGITKASVS 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 81 ITFDNSDKKqsplgfeVHDEITVTRQVVIGGRNK---YLINGVNANNTRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMK 157
Cdd:TIGR02169 80 VTFKNDDGK-------FPDELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 318 DLKKKNL-------ACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSN 390
Cdd:TIGR02169 311 AEKERELedaeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 391 EDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMK 466
Cdd:TIGR02169 391 REKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewkLEQLAADLSKYEQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 467 KLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKdpEKNWNRNCVKGLVASLISVKDTSAtTALELVAG 546
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE--VLKASIQGVHGTVAQLGSVGERYA-TAIEVAAG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 547 ERLYNVVVDTEVTGKKLLERgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPDNVHVALSLVEYKPELQKAMEF 622
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAFKY 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 623 VFGTTFVCDNMDNAkkvafdKRIM--TRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELkdvqDELRIKENELRALEE 700
Cdd:TIGR02169 619 VFGDTLVVEDIEAA------RRLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEP----AELQRLRERLEGLKR 688
|
730
....*....|...
gi 1370513639 701 ELAGLKNTAEKIE 713
Cdd:TIGR02169 689 ELSSLQSELRRIE 701
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-713 |
5.97e-72 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 252.55 E-value: 5.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 78 SVSITFDNSDKKqSPLGFevhDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196 79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:COG1196 154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGE-LERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 318 DLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEAT 397
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN----YEEN 473
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 474 KEESLLEKRRQLSRDIGRLKETYEALL---ARFPNLRFAYKDPEKNWNRNCVKGLVASLISVkDTSATTALELVAGERLY 550
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 551 NVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTF 628
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 629 VCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQ-AASILTKFQELKDVQDELRIKENELRALEEELAGLKN 707
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRElLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
....*.
gi 1370513639 708 TAEKIE 713
Cdd:COG1196 708 ELAEAE 713
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
522-639 |
3.89e-33 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 123.50 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 522 VKGLVASLISVKDtSATTALELVAGERLYNVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 599
Cdd:smart00968 3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1370513639 600 PDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKV 639
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-164 |
4.42e-29 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 116.21 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVYKNGQAGITKASVSIT 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 83 FDNSDKKqsplgFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIL 162
Cdd:cd03272 80 FDNSDNR-----FPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154
|
..
gi 1370513639 163 SM 164
Cdd:cd03272 155 EM 156
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-86 |
3.75e-26 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 105.85 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQdLVYKNGQAGITKASVSIT 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78
|
....
gi 1370513639 83 FDNS 86
Cdd:cd03239 79 FDKS 82
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-89 |
3.84e-25 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 103.31 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK--NGQAGITKASVS 80
Cdd:cd03278 1 LKKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVT 79
|
....*....
gi 1370513639 81 ITFDNSDKK 89
Cdd:cd03278 80 LTFDNSDGR 88
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
522-640 |
6.51e-23 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 94.25 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 522 VKGLVASLISVKDTsATTALELVAGERLYNVVVDTEVTGKKLLE--RGELKRRYTIIPLNKISARCIAPETLRVAqnlvg 599
Cdd:pfam06470 4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIEflKKNKLGRATFLPLDRLKPRPRRPGADLKG----- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370513639 600 pdNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVA 640
Cdd:pfam06470 78 --GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-159 |
1.78e-21 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 94.18 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVY--KNGQAGITKASVS 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513639 81 ITFDNSDKkqsplgfevhdEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:cd03275 79 AVYEDDDG-----------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-156 |
4.13e-16 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 77.72 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASNLQDLVYK-NGQAGITKASVSI 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSVEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370513639 82 TFDnsdkkqsplgfEVHDEitvtrqvviggrnkylingvnanntrvqDLFCSVGLNVNNPHFLIMQGRITKVLNM 156
Cdd:cd03274 82 HFQ-----------EIIDK----------------------------PLLKSKGIDLDHNRFLILQGEVEQIAQM 117
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-83 |
1.70e-14 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 71.62 E-value: 1.70e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513639 5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasnlqdlvYKNGQAGITKASVSITF 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-203 |
5.98e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 68.50 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSqvRASNLQDLVYKngqaGITKASVSI 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINV----GSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 82 TFDNSDKkqsplgfevhdEITVTRQvviggrnkylingvnanntrvqdlfcsvglnvnnphflimQGRITKVLNMKPPEI 161
Cdd:COG0419 74 EFEHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSER 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1370513639 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI--LEEEI 203
Cdd:COG0419 103 KEALKRLLGLEIYEELKERLKELEEALESALEELAELqkLKQEI 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-509 |
1.02e-11 |
|
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: 67.10 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 257 QDKVIKLQEELSENDKKIKALNHEIEELEKRKdKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLAceeskrkELEK 336
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 337 NMVEDSKTLAAKEKEVKKItdgLHALQEASNKDAEALaaaqqhfnavsagLSSNEDGAEATLAGQMMACKNDISKAQTEA 416
Cdd:COG4942 91 EIAELRAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 417 -KQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEM-KKLNYEENKEESLLEKRRQLSRDIGRLKE 494
Cdd:COG4942 155 lRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*
gi 1370513639 495 TYEALLARFPNLRFA 509
Cdd:COG4942 235 EAAAAAERTPAAGFA 249
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-196 |
1.28e-11 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 64.05 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:pfam13476 1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 84 DNSDKKQSplgFEVHDEITVTRQVVIGGRNKYL-INGVNANNTRVQDLFCSvgLNVNNPHFLIM-QGRITKVLNMKPPEI 161
Cdd:pfam13476 79 ENNDGRYT---YAIERSRELSKKKGKTKKKEILeILEIDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1370513639 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK 196
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-468 |
1.58e-11 |
|
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: 68.07 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLLgisnLSQVRASNlQDLVYKNGQAGITKAS 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRS-EVIRSLNSLYAAPSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 79 VSITFDNSDKKQSplgFEVHDEITVTR---------QVVI---GGRNKYLINGVNANNTRVQDLfcsvgLNVNNPHF--- 143
Cdd:TIGR00618 75 AFAELEFSLGTKI---YRVHRTLRCTRshrkteqpeQLYLeqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 144 -LIMQGRITKVLNMKPPEILSMIEEAAGTRMYE---------YKKIAAQKTIEKKEAKL------------KEIKTILEE 201
Cdd:TIGR00618 147 vLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTqlalmefakKKSLHGKAELLTLRSQLltlctpcmpdtyHERKQVLEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 202 EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHeI 281
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ-I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 282 EELEKRKDKETGGILRSLEDALAEAQRVnTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEvKKITDGLHA 361
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 362 LQEASNKDAEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK 439
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
490 500
....*....|....*....|....*....
gi 1370513639 440 MDSGYRKDQEALEAVKRLKEKlEAEMKKL 468
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ-ETRKKAV 491
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-126 |
5.00e-11 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 64.79 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 2 HIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVSI 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1370513639 82 TFDNSDKKqsplgFEVhdEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:COG1195 72 EVERDGRE-----VRL--GLGLSR----GGKKRVRINGKPVRRLS 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-499 |
1.00e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrasnLQDLVYKngqaGITKAS 78
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 79 VSITFdnsdkkqSPLGFEVH---------DEITVTRQVVIGGRNkyLINGVNANNTRVQDLfcsvgLNVNNPHFL----I 145
Cdd:PRK02224 70 IELWF-------EHAGGEYHierrvrlsgDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 146 MQGRITKVLNMKPPEILSMIEEAAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------L 192
Cdd:PRK02224 136 RQGEVNKLINATPSDRQDMIDDLLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 193 KEIKTILE--EEITPTIQKLKEERSSYLE-YQKVMREIEHLSRLYIAYQFLLAEDTKVRS--AEELKEMQDKVIKLQEEL 267
Cdd:PRK02224 216 AELDEEIEryEEQREQARETRDEADEVLEeHEERREELETLEAEIEDLRETIAETEREREelAEEVRDLRERLEELEEER 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 268 SE-------NDKKIKALNHEIEELEKRKDketgGILRSLEDALAEAQRVNTKSQS----AFDLKKKNLACEEsKRKELEK 336
Cdd:PRK02224 296 DDllaeaglDDADAEAVEARREELEDRDE----ELRDRLEECRVAAQAHNEEAESlredADDLEERAEELRE-EAAELES 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 337 NMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHfnavSAGLSSNEDGA---EATLAGQMMACKNDISKAq 413
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF----LEELREERDELrerEAELEATLRTARERVEEA- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 414 tEAKQAQMKLKHAQQELKnkqaevkkmDSGyrkDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLS---RDIG 490
Cdd:PRK02224 446 -EALLEAGKCPECGQPVE---------GSP---HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIE 512
|
....*....
gi 1370513639 491 RLKETYEAL 499
Cdd:PRK02224 513 RLEERREDL 521
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
23-130 |
2.77e-10 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 61.83 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 23 FDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASNlqDLVykngQAGITKASVSITFDNSDK-----KQSPLGFEV 97
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEeeakaLLLELGIED 86
|
90 100 110
....*....|....*....|....*....|...
gi 1370513639 98 HDEITVTRQVVIGGRNKYLINGVNANNTRVQDL 130
Cdd:cd03241 87 DDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
165-515 |
3.42e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 165 IEEAagTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaed 244
Cdd:PTZ00121 1214 AEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------------- 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 245 tKVRSAEELKEMQDKviKLQEELSENDKKIKAlnheiEELEKRKDKEtggilRSLEDALAEAQRVNTKSQSAfdlKKKnl 324
Cdd:PTZ00121 1276 -EARKADELKKAEEK--KKADEAKKAEEKKKA-----DEAKKKAEEA-----KKADEAKKKAEEAKKKADAA---KKK-- 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 325 aCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmma 404
Cdd:PTZ00121 1338 -AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-------- 1407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 405 ckNDISKAQTEAKQAQmklkhaqqELKNKQAEVKKMDSGYRKDQE---ALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:PTZ00121 1408 --DELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350
....*....|....*....|....*....|....
gi 1370513639 482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEK 515
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-123 |
2.08e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 59.79 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVS 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370513639 81 ITFDNSdkkqsplGFEVHDEITVTRQvvigGRNKYLINGVNAN 123
Cdd:PRK00064 72 GRVEKG-------GRELPLGLEIDKK----GGRKVRINGEPQR 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-468 |
3.98e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 175 EYKKIAAQKTIEKKEAKLKEIK---TILEEEITPTIQKLKEERSsylEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSA- 250
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALDEl 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 251 -EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILrSLEDALAEAQRVNTKSQSAFDLKKKNLACEES 329
Cdd:TIGR02168 809 rAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 330 KRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDI 409
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370513639 410 SKAQTEAKQAQMKLKH-------AQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKL 468
Cdd:TIGR02168 968 EEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-499 |
4.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 252 ELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKR---KDKETGGILRSLEDALAEAQRVNTKSQSA---FDLKKKNLA 325
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQLeerIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 326 CEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEatlagqmmAC 405
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE--------SL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 406 KNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEenkEESLLEKRRQL 485
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE---LEELSEELREL 906
|
250
....*....|....
gi 1370513639 486 SRDIGRLKETYEAL 499
Cdd:TIGR02168 907 ESKRSELRRELEEL 920
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-95 |
5.15e-09 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 56.84 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03276 1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
|
90
....*....|...
gi 1370513639 83 FDNSDKKQSPLGF 95
Cdd:cd03276 75 LKNQGLDANPLCV 87
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-97 |
6.30e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL--LGISNLSQVRASN--LQDLVYKNGQAGITKAS 78
Cdd:COG4637 2 ITRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITEPIR 78
|
90
....*....|....*....
gi 1370513639 79 VSITFDNSDkkQSPLGFEV 97
Cdd:COG4637 79 LELEFAEED--ERDLRYEL 95
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-494 |
6.81e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 167 EAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEitptiQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTk 246
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA- 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 247 vRSAEELKEMQDKviKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDAlAEAQRVNTKSQSAFDLKKKNLAC 326
Cdd:PTZ00121 1534 -KKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKA 1609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 327 EESKRKELEKNMVEDSKtlaaKEKEVKKITDGLHALQEASNKDAEALAAAQQHfNAVSAGLSSNEDGAEATLAGQMMACK 406
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE-NKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 407 NDISKAQTEAKQAQMKLKHAQQeLKNKQAEVKKMDSGYRKDQEA-LEAVKRLKEKLEAEMKKLNyEENKEESLLEKRRQL 485
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHL 1762
|
....*....
gi 1370513639 486 SRDIGRLKE 494
Cdd:PTZ00121 1763 KKEEEKKAE 1771
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-109 |
1.59e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASNLQDLVYKngqaGITKASVSI 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
|
90 100
....*....|....*....|....*...
gi 1370513639 82 TFDNSDKKQsplgFEVHDEITVTRQVVI 109
Cdd:cd03240 76 AFENANGKK----YTITRSLAILENVIF 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-499 |
1.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGqagiTKASVS 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG----SGTEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 81 ITFDNSDKKqsplgfevhdeITVTRQVVIGgrNKYLINGVNANNTRVQDLFCS------VGLNVNNPHFLIMQGRITKVL 154
Cdd:PRK03918 75 LKFEKNGRK-----------YRIVRSFNRG--ESYLKYLDGSEVLEEGDSSVRewverlIPYHVFLNAIYIRQGEIDAIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 155 nmkppeilsmieEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEitptIQKLKEERSSYLEYQKVMREiehlsrly 234
Cdd:PRK03918 142 ------------ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKE-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 235 iayqfllAEDTKVRSAEELKEMQDKVIKLQEEL---SENDKKIKALNHEIEELEKRKDKETGGiLRSLEDALAEAQrvnt 311
Cdd:PRK03918 198 -------KEKELEEVLREINEISSELPELREELeklEKEVKELEELKEEIEELEKELESLEGS-KRKLEEKIRELE---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 312 ksqsafdlkkKNLACEESKRKELEKNmVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNE 391
Cdd:PRK03918 266 ----------ERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 392 DgaeatlagqMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDsGYRKDQEALEAVKRLKEKLEAEMKKLNYE 471
Cdd:PRK03918 335 E---------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
490 500
....*....|....*....|....*...
gi 1370513639 472 EnKEESLLEKRRQLSRDIGRLKETYEAL 499
Cdd:PRK03918 405 E-EISKITARIGELKKEIKELKKAIEEL 431
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-84 |
2.37e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 56.55 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLqdlvYKNGQAGITKASVS 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDF----YLGDDPDLPEIEIE 74
|
....
gi 1370513639 81 ITFD 84
Cdd:COG3593 75 LTFG 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-497 |
4.30e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 156 MKPPEILSMIEEAagTRMYEYKKIAAQKTIEkkEAKLKEIKTILEEEITPTIQKlKEERSSYLEYQKVMREIEHLSRLYI 235
Cdd:PTZ00121 1121 KKKAEDARKAEEA--RKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEAR-KAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 236 AYQFLLAEDTK----VRSAEELKEMQD----KVIKLQEELSENDKKIKALNHE--IEELEKRKDKETGGILRSLEDALAE 305
Cdd:PTZ00121 1196 AEDARKAEAARkaeeERKAEEARKAEDakkaEAVKKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 306 AQRVNTKSQSAFDLKKKN-LACEESKRK--ELEKNMVEDSKTLAAKEK--EVKKITDGLHALQEASNKDAEALAAAQQhf 380
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADeAKKAEEKKKadEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAE-- 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 381 nAVSAGLSSNEDGAEAT-LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKdqeALEAVKRLKE 459
Cdd:PTZ00121 1354 -AAADEAEAAEEKAEAAeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK---ADEAKKKAEE 1429
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370513639 460 KLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYE 497
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
207-466 |
5.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 207 IQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK 286
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 287 RKDKETGGILRSLEDALAEAQRvntksqsafdlkkknlaceeskrkeleknmvedskTLAAKEKEVKKITDGLHALQEAS 366
Cdd:COG4913 331 QIRGNGGDRLEQLEREIERLER-----------------------------------ELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 367 NKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmmackndiskAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYrk 446
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLRRELRELEAEIASLERRKSNI-- 438
|
250 260
....*....|....*....|...
gi 1370513639 447 DQEALEAVKRLKEKL---EAEMK 466
Cdd:COG4913 439 PARLLALRDALAEALgldEAELP 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-497 |
1.58e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 188 KEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHlsrlyiayQFLLAEDTKVRSAEELKEMQDKVIKLQEEL 267
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK--------EIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 268 SENDKKIKALNHEIEELEKRKDKETGGiLRSLEDALAEaQRVNTKSQSAFDLKKKNLACEES--------KRKELEKNMV 339
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEA-LNDLEARLSH-SRIPEIQAELSKLEEEVSRIEARlreieqklNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 340 EDSKT--------LAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagQMMACKNDISK 411
Cdd:TIGR02169 832 EKEIQelqeqridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 412 AQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQE------ALEAVKRLKEKLEAEMKKL---------NYEENKE- 475
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALepvnmlaiqEYEEVLKr 987
|
330 340
....*....|....*....|...
gi 1370513639 476 -ESLLEKRRQLSRDIGRLKETYE 497
Cdd:TIGR02169 988 lDELKEKRAKLEEERKAILERIE 1010
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
183-534 |
1.60e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 183 KTIEKKEAKLKEIKTILEEeitpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAED--TKVRSAEELK-EMQDK 259
Cdd:PRK03918 331 KELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKleKELEELEKAKeEIEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 260 VIKLQEELSENDKKIKALNHEIEELEKRKdketgGILRSLEDALAEAQRVNTKSQSAFDLKK--KNLACEESKRKELEKN 337
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAK-----GKCPVCGRELTEEHRKELLEEYTAELKRieKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 338 MVEDSKTLaAKEKEV---KKITDGLHALQEASNK-DAEALAAAQQHFNAVSAGLssnedgaeATLAGQMMACKNDISKAQ 413
Cdd:PRK03918 482 LRELEKVL-KKESELiklKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKL--------IKLKGEIKSLKKELEKLE 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 414 tEAKQAQMKLKHAQQELKNKQAEVKK--MDSGYRKDQEALEAVKRLKE-------------KLEAEMKKLNYEENKEESL 478
Cdd:PRK03918 553 -ELKKKLAELEKKLDELEEELAELLKelEELGFESVEELEERLKELEPfyneylelkdaekELEREEKELKKLEEELDKA 631
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370513639 479 LEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKD 534
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
177-484 |
1.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 177 KKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEM 256
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 257 QDKVIKLQEELsendKKIKALNHEIEELEKRKDKETGGILRSLEDAL-AEAQRVNTKSQSAFDLKK-KNLACEESKRKEL 334
Cdd:PTZ00121 1492 AEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkADEAKKAEEKKKADELKKaEELKKAEEKKKAE 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 335 EKNMVEDSKTLA------AKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACK-- 406
Cdd:PTZ00121 1568 EAKKAEEDKNMAlrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkk 1647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 407 --NDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEaEMKKLNYEENKEESLLEKRRQ 484
Cdd:PTZ00121 1648 kaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEE 1726
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-90 |
3.18e-07 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 51.83 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASNLQDLVyKNGQagiTKASVS 80
Cdd:cd03277 3 IVRIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIE 74
|
90
....*....|.
gi 1370513639 81 IT-FDNSDKKQ 90
Cdd:cd03277 75 IElYGNPGNIQ 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
175-487 |
3.59e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 175 EYKKIAAQKTIEKKEAKLKEIKTIlEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELK 254
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAA-EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 255 EMQDKVIKLQEELSEND--KKIKALNHEIEELEKRKD--KETGGILRSLEDA--LAEAQRVNTKSQSAFDLKKKnlaCEE 328
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADeaKKKAEEAKKADEAKKKAEeaKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKK---AEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 329 SKRK--ELEKNMVEDSKTLAAKEKEVKKITDGLHALQEAsnKDAEALAAAQQHFNA----VSAGLSSNEDGAEATLAGQM 402
Cdd:PTZ00121 1495 AKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEKKKAdelkKAEELKKAEEKKKAEEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 403 MACKNDISKAQTEAKQAQMK-----LKHAQQELKNKQAEVKKMDSG------YRKDQEALEAVKRLKEKLEAEMKKLNYE 471
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEAKKAEEAkikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
330
....*....|....*.
gi 1370513639 472 ENKEESLLEKRRQLSR 487
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAK 1668
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
147-489 |
6.63e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 147 QGRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTIEKKEAKLKEIKTILE-EEITPTIQKLKEE-RSSYLEYQKVM 224
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSElREAKRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 225 REIEHlsrlyiayQFLLA--EDTKVRS-----AEELKEMQDKvikLQEELSENDKKIKALNHEIEELEKRKDKETGG--- 294
Cdd:pfam15921 345 EELEK--------QLVLAnsELTEARTerdqfSQESGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 295 ---ILRSLEDALAEAQRVNT-----KSQSAFDLKKKnLACEESKRKELEKnmvedSKTLAAKEKEVKKItdgLHALQEAS 366
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEAllkamKSECQGQMERQ-MAAIQGKNESLEK-----VSSLTAQLESTKEM---LRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 367 NKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMKLKHAQQE---LKNKQAEVKKMDSG 443
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNA--------EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370513639 444 YRKDQEALEAvkrLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDI 489
Cdd:pfam15921 557 MAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-368 |
7.70e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEErssyleyqkvMREIEHLSRLYIayQF 239
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER----------LKELEPFYNEYL--EL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 240 LLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETggilrsledaLAEAQRVNTKSQSAFDL 319
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE----------YEELREEYLELSRELAG 677
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370513639 320 KKKNLACEESKRKELEKN---MVEDSKTLAAKEKEVKKITDGLHALQEASNK 368
Cdd:PRK03918 678 LRAELEELEKRREEIKKTlekLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-63 |
1.03e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 50.77 E-value: 1.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370513639 1 MHIKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQ 63
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-126 |
1.35e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 50.37 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVykngQAGITKASVSIT 82
Cdd:cd03242 1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1370513639 83 FDNSdkkqsplGFEVHDEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:cd03242 72 LERQ-------GGELALELTIRS----GGGRKARLNGIKVRRLS 104
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-89 |
1.50e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 49.57 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:cd03279 8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82
|
....*.
gi 1370513639 84 DNSDKK 89
Cdd:cd03279 83 QLGGKK 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
148-508 |
2.61e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 148 GRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTI----EKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKV 223
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEK-EVKELEELKEEieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 224 MREIEHLSRLYIAYQFLLAEDTKVRsaEELKEMQDKVIKLQEELSENDKKIKAL---NHEIEELEKRKdKETGGILRSLE 300
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYL--DELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKL-KELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 301 DALAEAQRVNTKSQSAFDLKKKnLACEESKRKELEKNMVEDSKTlaAKEKEVKKITDGLHALQEAS---NKDAEALAAAQ 377
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKR-LTGLTPEKLEKELEELEKAKE--EIEEEISKITARIGELKKEIkelKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 378 QHFNAVSAGLSSNEDG---AEATL-----AGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQA-----EVKKMDSGY 444
Cdd:PRK03918 436 GKCPVCGRELTEEHRKellEEYTAelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeqlkELEEKLKKY 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513639 445 -----RKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRF 508
Cdd:PRK03918 516 nleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
160-489 |
3.18e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK--TILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELlaDRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 238 QFLLAEDTKVRSAEELKEMQDKVIKLQEE-LSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSA 316
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEkLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 317 FDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEA 396
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 397 TLAGQMMAC-KNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKE 475
Cdd:pfam02463 926 EAEILLKYEeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
330
....*....|....
gi 1370513639 476 ESLLEKRRQLSRDI 489
Cdd:pfam02463 1006 KLIRAIIEETCQRL 1019
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-100 |
8.68e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 48.50 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 2 HIKSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITK 76
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEP 80
|
90 100
....*....|....*....|....
gi 1370513639 77 ASVSITFdNSDKKQSPLGFEVHDE 100
Cdd:COG1106 81 SEFEILF-LLDGVRYEYGFELDKE 103
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-472 |
1.28e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 48.58 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 3 IKSII-LEGFKSYAQRTEVNGFDPLfNAITGLNGSGK---SNILDSICfllgisnlsqvrasnlqdlvyKNGQAGITKAS 78
Cdd:COG4694 2 ITKIKkLKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE---------------------LGDTSSEVIAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 79 VSITFDNSDKKQSPLGF-------EVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLfcSVGLNVNNPHFLIMQGRIT 151
Cdd:COG4694 60 FEIEAGGSAPNPSVRVFnrdfveeNLRSGEEIKGIFTLGEENIELEEEIEELEKEIEDL--KKELDKLEKELKEAKKALE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 152 KVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEK-------------KEAKLKEIKTILEEEITPTIQKLKEERSSYL 218
Cdd:COG4694 138 KLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSAlksssedelkeklKLLKEEEPEPIAPITPLPDLKALLSEAETLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 219 EYQKVMREIEHLSRLyiayQFLLAEDTKVRSAEELKEMQDKVI------KLQEEL---------SENDKKIKALNHEIEE 283
Cdd:COG4694 218 EKSAVSSAIEELAAL----IQNPGNSDWVEQGLAYHKEEEDDTcpfcqqELAAERiealeayfdDEYEKLLAALKDLLEE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 284 LEKRKDKETGGILRSLEDALAEA-QRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAakeKEVKKITDGLHAL 362
Cdd:COG4694 294 LESAINALSALLLEILRTLLPSAkEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELL---DELNDLIAALNAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 363 QEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAGQmmacKNDISKAQTEAKQAQmKLKHAQQELKNKQAEVKKmds 442
Cdd:COG4694 371 IEEHNAKIANLKAEKE--EARKKLEAHELAELKEDLSRY----KAEVEELIEELKTIK-ALKKALEDLKTEISELEA--- 440
|
490 500 510
....*....|....*....|....*....|
gi 1370513639 443 gyrkdqeALEAVKRLKEKLEAEMKKLNYEE 472
Cdd:COG4694 441 -------ELSSVDEAADEINEELKALGFDE 463
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
23-376 |
2.13e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 23 FDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASnlQDLVyKNGQAgitKASVSITFDNSDKKQ-----SPLGFEV 97
Cdd:COG0497 20 FGPGLTVLTGETGAGKSILLDALGLLLG------GRAD--ASLV-RHGAD---KAEVEAVFDLSDDPPlaawlEENGLDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 98 HD-EITVTRQVVIGGRNKYLINGVNANNTRVQDLFcsvglnvnnpHFLI-MQG-----RItkvlnMKPPEILSMIEEAAG 170
Cdd:COG0497 88 DDgELILRREISADGRSRAFINGRPVTLSQLRELG----------ELLVdIHGqhehqSL-----LDPDAQRELLDAFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 171 TR--MYEYKkiAAQKTIEKKEAKLKEIKTILEEeitptiqklKEERSSYLEYQkvMREIEHLSRLYIAYQFLLAEDTKVR 248
Cdd:COG0497 153 LEelLEEYR--EAYRAWRALKKELEELRADEAE---------RARELDLLRFQ--LEELEAAALQPGEEEELEEERRRLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 249 SAEELKEmqdKVIKLQEELSEND----KKIKALNHEIEELEkRKDKETGGILRSLEDALAEAQ----------------- 307
Cdd:COG0497 220 NAEKLRE---ALQEALEALSGGEggalDLLGQALRALERLA-EYDPSLAELAERLESALIELEeaaselrryldslefdp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 308 ----RVNTKSQSAFDLKKKN-------LACEESKRKELEK--NMVEDSKTLAAKEKEVKKITDGL-HALQEASNKDAEAL 373
Cdd:COG0497 296 erleEVEERLALLRRLARKYgvtveelLAYAEELRAELAEleNSDERLEELEAELAEAEAELLEAaEKLSAARKKAAKKL 375
|
...
gi 1370513639 374 AAA 376
Cdd:COG0497 376 EKA 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-446 |
2.13e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 180 AAQKTIEKKEAKLKEIKtileEEITPTIQKLKEERSSyleyqkvmreiehlsrlyiayqfllaedtKVRSAEELKEMQDK 259
Cdd:COG4942 17 AQADAAAEAEAELEQLQ----QEIAELEKELAALKKE-----------------------------EKALLKQLAALERR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 260 VIKLQEELSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAE----AQRVNTKSQSAFDLKKKNLACEESK----- 330
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIA-ELRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRlqylk 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 331 -----RKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmac 405
Cdd:COG4942 143 ylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA------ 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370513639 406 kndisKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK 446
Cdd:COG4942 217 -----ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-503 |
2.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 161 ILSMIEEAAGTRMYEY------KKIAAQKTIEKKEAKLKEIKTILEE--EITPTIQKLKEE----RSSYLEYQKVMREIE 228
Cdd:COG4717 43 IRAMLLERLEKEADELfkpqgrKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEEleelEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 229 HLSRLYIAYQFLLAEDTKVRS----AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA 304
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElperLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 305 EAQRVNTKSQSAFDLKKKNLaceESKRKELEKnmVEDSKTLAAKEKEVKKITDGLHALqeasnkdaeALAAAQQHFNAVS 384
Cdd:COG4717 203 ELQQRLAELEEELEEAQEEL---EELEEELEQ--LENELEAAALEERLKEARLLLLIA---------AALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 385 AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK-----MDSGYRKDQEALEAVKRLKE 459
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370513639 460 --KLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARF 503
Cdd:COG4717 349 lqELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-308 |
2.80e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 181 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKVMREIEH--------LSRLYIAYQFLLAEDTKV 247
Cdd:COG3206 187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQR 308
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-503 |
3.18e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 263 LQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRvntksqsafdlkKKNLACEESKRKELEKNMVEDS 342
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE--------LEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 343 KTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMK 422
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELA--------ELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 423 LKHAQQELKNK-QAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMKKLNyeenkeeSLLEKRRQLSRDIGRLKETYE 497
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEALQAreasLQAQLAQLEARLAELP-------ELEAELRRLEREVEVARELYE 368
|
....*.
gi 1370513639 498 ALLARF 503
Cdd:COG3206 369 SLLQRL 374
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-507 |
3.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 199 LEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE---DTKVRSAEELKEMQDKVIKLQEELSENDKKIK 275
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 276 ALNHEIEELEKRKDK-ETGGILRSLEDALAEAQRV------------NTKSQSAFDLKKKNLAC-----------EESKR 331
Cdd:COG4717 217 EAQEELEELEEELEQlENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFlvlgllallflLLARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 332 KELEKNMVEDSKTLAAKE----KEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEdgAEATLAGQMMACKN 407
Cdd:COG4717 297 KASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLEELEQEIAA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 408 DISKAQTEAKQA-QMKLKHAQ--QELKNKQAEVKKMDSGYRKDQEALEAV---KRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:COG4717 375 LLAEAGVEDEEElRAALEQAEeyQELKEELEELEEQLEELLGELEELLEAldeEELEEELEELEEELEELEEELEELREE 454
|
330 340
....*....|....*....|....*...
gi 1370513639 482 RRQLSRDIGRLKE--TYEALLARFPNLR 507
Cdd:COG4717 455 LAELEAELEQLEEdgELAELLQELEELK 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-507 |
3.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 171 TRMYEYKKIAAQKTIEKKEAKLKEI---KTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKv 247
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 248 rsAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK--------RKDKETGGILRSLEDALAE--AQRVNTKSQSAF 317
Cdd:PRK03918 451 --KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeselIKLKELAEQLKELEEKLKKynLEELEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 318 DLKKK---------NLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLS 388
Cdd:PRK03918 529 KLKEKliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 389 SNEDGAEATLAgQMMACKNDISKAQTE------------AKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKR 456
Cdd:PRK03918 609 DAEKELEREEK-ELKKLEEELDKAFEElaetekrleelrKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 457 LKEKLEAEMKKLnyEENKEEslLEKRRQLSRDIGRLKETYEALLARFPNLR 507
Cdd:PRK03918 688 RREEIKKTLEKL--KEELEE--REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
144-468 |
3.52e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 144 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 212
Cdd:PRK10246 152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 213 ERSSYLEYQKVM-REIEHLSRLYIAYQFLLAEDTKVRSA-EELKEMQDKVIKLqeELSENDKKIKALNHEIEELEKRkdk 290
Cdd:PRK10246 231 EEKQLLTAQQQQqQSLNWLTRLDELQQEASRRQQALQQAlAAEEKAQPQLAAL--SLAQPARQLRPHWERIQEQSAA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 291 etggilrsLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK------EVKkitdGLHALQE 364
Cdd:PRK10246 306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnELA----GWRAQFS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 365 ASNKDAEALAAAQQHFNAVSAGLS---------SNEDGAEA--------TLAGQMMACKNDISKAQTEAKQAQMKLKHAQ 427
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNalpaitltlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1370513639 428 QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEkLEAEMKKL 468
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-467 |
5.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--------LEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 322 KNLACE-----ESKRKELEKNMVEDSKTLAAkekevkkITDGLHALQEASNKDAEALAAAQQhfnavsaglssnedgAEA 396
Cdd:COG3883 86 EELGERaralyRSGGSVSYLDVLLGSESFSD-------FLDRLSALSKIADADADLLEELKA---------------DKA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 397 TLAGQmmacKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKK 467
Cdd:COG3883 144 ELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
242-499 |
8.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 242 AEDtkVRSAEELKEMQDkVIKLQEELSENDKKIKALNHEIEELEKRKdketggILRSLEDAL-AEAQRVNTKSQSAFDLK 320
Cdd:PTZ00121 1124 AED--ARKAEEARKAED-ARKAEEARKAEDAKRVEIARKAEDARKAE------EARKAEDAKkAEAARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 321 KknlaCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAvsaGLSSNEDGAEATLAG 400
Cdd:PTZ00121 1195 K----AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE---EIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 401 QMMACKNDISKAQTEAKQAQMKLKHAQ----------QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE-------A 463
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaeekkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaaeA 1347
|
250 260 270
....*....|....*....|....*....|....*.
gi 1370513639 464 EMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEAL 499
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
181-411 |
9.90e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 181 AQKTIEKKEA----KLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsRLYIAYQFLLAEDTKVRSAEELKEM 256
Cdd:PTZ00121 1539 AKKAEEKKKAdelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAEEAKKA 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 257 QDKVIKLQE-ELSENDKKIKALNHEIEELEKRKDKEtggiLRSLED-----ALAEAQRVNTKSQSAFDLKK----KNLAC 326
Cdd:PTZ00121 1616 EEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEenkikAAEEAKKAEEDKKKAEEAKKaeedEKKAA 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 327 EESKRKELEKNMVEDSKTLAA----------KEKEVKKI-TDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE 395
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAeekkkaeelkKAEEENKIkAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*.
gi 1370513639 396 ATLAGQMMACKNDISK 411
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDE 1787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
251-501 |
1.07e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-RKDKETGG--ILRSLEDALAEAQRVNTKSQSAFD------LKK 321
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeLTNSESENseKQRELEEKQNEIEKLKKENQSYKQeiknleSQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE---ATL 398
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtqlKVL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 399 AGQMMACKNDISKAQTEAKQAQ---MKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEK----LEAEMKKLNYE 471
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdLEDELNKDDFE 553
|
250 260 270
....*....|....*....|....*....|
gi 1370513639 472 ENKEEsLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:TIGR04523 554 LKKEN-LEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
175-350 |
1.22e-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: 45.50 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 175 EYKKIAAQKTIE----KKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQ----KVMREIEHLSRLYI-------AYQF 239
Cdd:pfam17380 338 EQERMAMEREREleriRQEERKRELERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVKIleeerqrKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 240 LLAEDTKVRSAEElKEMQDKVIKLQEELSENDKKIK----ALNHEIEEL----EKRKDKETGGILRSLEDALAEAQRVNT 311
Cdd:pfam17380 418 QKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRleeqERQQQVERLrqqeEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370513639 312 KSQSaFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK 350
Cdd:pfam17380 497 LEKE-LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-462 |
1.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 175 EYKKIAAQ-KTIEKKEAKLKEIKTILEEEIT--PTIQKLKEERSSYLEYQKVMREI--EHLSRLYIAYQFLLAEDTKVRS 249
Cdd:PRK03918 460 ELKRIEKElKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYEKLKEKLIKLKG 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 250 --------AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKsqsafdlkK 321
Cdd:PRK03918 540 eikslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA--------E 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQeaSNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagq 401
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEE----- 684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 402 mmackndISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE 462
Cdd:PRK03918 685 -------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-420 |
1.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETggilRSLEDALAEAQR-----------VNTKSQSAFDL 319
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR----EELGERARALYRsggsvsyldvlLGSESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 320 KKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180
....*....|....*....|.
gi 1370513639 400 GQMMACKNDISKAQTEAKQAQ 420
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAA 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-498 |
1.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 160 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKVMREIEHLSRLYIAYQ 238
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 239 fllAEDTK----------VRSAEELKEMQDKVIKLQEELSENDKKIkalnheiEELEKRKDKETGGILRSLEDALAEAqr 308
Cdd:PTZ00121 1172 ---AEDAKkaeaarkaeeVRKAEELRKAEDARKAEAARKAEEERKA-------EEARKAEDAKKAEAVKKAEEAKKDA-- 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 309 vntksqsafdlkkknlacEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEAsnKDAEALAAAQQHFNAVSAGLS 388
Cdd:PTZ00121 1240 ------------------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEA--RKADELKKAEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 389 SNEDGAEatlagqmmacknDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKL 468
Cdd:PTZ00121 1299 EEKKKAD------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350
....*....|....*....|....*....|
gi 1370513639 469 NYEENKEESLLEKRRQLSRDIGRLKETYEA 498
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-481 |
1.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 239 FLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKetggilrsLEDALAEAQRvntksqsafd 318
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQA---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 319 lkkknlaceesKRKELEKNMVEDSKTLAAKEKEVKKItdgLHALQEASNK--------DAEALAAAQQHFNAVSAGLSSN 390
Cdd:COG3883 66 -----------EIDKLQAEIAEAEAEIEERREELGER---ARALYRSGGSvsyldvllGSESFSDFLDRLSALSKIADAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 391 EDgaeatLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNY 470
Cdd:COG3883 132 AD-----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
250
....*....|.
gi 1370513639 471 EENKEESLLEK 481
Cdd:COG3883 207 AAEAAAAAAAA 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-392 |
2.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 182 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE----DTKVRSAE---- 251
Cdd:COG4913 606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaelEAELERLDassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 252 ELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggilrsLEDALAEAQRVNTKSQSAFDLKKKNLaceeskR 331
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LEQAEEELDELQDRLEAAEDLARLEL------R 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513639 332 KELEKnMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNA--------VSAGLSSNED 392
Cdd:COG4913 749 ALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADLESLPE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
128-520 |
3.00e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 128 QDLFCSVGLNVN---NPHFLIMQGRITKVLNMKPPEILSMI--------EEAAGTRMYEYK-KIAAQKTIEKKEAKLKEI 195
Cdd:pfam15921 11 EDLLSSSGITSNrgsSSPFFVSSIRGTIIENTSSTGTFTQIpifpkyevELDSPRKIIAYPgKEHIERVLEEYSHQVKDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 196 KTILEEEitptiQKLKEERSSYLEyQKVMREIEHLSRLYIAYQFLLaeDTKVR---SAEELK-EMQDKVIKLQEELSEND 271
Cdd:pfam15921 91 QRRLNES-----NELHEKQKFYLR-QSVIDLQTKLQEMQMERDAMA--DIRRResqSQEDLRnQLQNTVHELEAAKCLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 272 KKIKALNHEIEELEKRKDKETGgILRSLEDALAEAQRVNTKSQSAFD----LKKKNLACEESK-RKELEKNmvedsktLA 346
Cdd:pfam15921 163 DMLEDSNTQIEQLRKMMLSHEG-VLQEIRSILVDFEEASGKKIYEHDsmstMHFRSLGSAISKiLRELDTE-------IS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 347 AKEKEVKKITDGLHALQEASNKDAEALAaaQQHFNAVSAGLSSNEDgaeatlagQMMACKNDISKAQTEAKQAQMKLKHA 426
Cdd:pfam15921 235 YLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEV--------EITGLTEKASSARSQANSIQSQLEII 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 427 QQELKNKQA----EVKKMDSGYRKDQEALEAVKRLKE-KLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:pfam15921 305 QEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
410 420
....*....|....*....|...
gi 1370513639 502 ----RFPNLRFAYKDPEKNWNRN 520
Cdd:pfam15921 385 dlhkREKELSLEKEQNKRLWDRD 407
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
177-425 |
3.13e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 177 KKIAAQKTIEKKEAKLKEIKtILEEEITPTIQKLkEERSSYLEYQKVmreiehlsrlyiayQFLLAEDTKVRSAEELKEM 256
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFK-ILKDKKDAKIREL-EARVSDLELEKV--------------KLVNAGSERLRAVKDIKQE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 257 QDKVIKlQEELSENDKKIKALNHEI---------EELEKRKDK-------------ETGGILRSLEDALAEAQRVNTKSQ 314
Cdd:pfam15921 655 RDQLLN-EVKTSRNELNSLSEDYEVlkrnfrnksEEMETTTNKlkmqlksaqseleQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 315 SAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDA---EALAAAQQHFNAVSAGLSSNE 391
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVANMEVAL 813
|
250 260 270
....*....|....*....|....*....|....
gi 1370513639 392 DGAEAtlagQMMACKNDISKAQTEAkqAQMKLKH 425
Cdd:pfam15921 814 DKASL----QFAECQDIIQRQEQES--VRLKLQH 841
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
191-477 |
3.48e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 191 KLKEIKTILEEEiTPTIQKLKEERSSyleyqkVMREIEHLSrlyiayQFLLAEDTKVRSaeelkeMQDKVIKLQEELSEN 270
Cdd:pfam10174 353 RLEEKESFLNKK-TKQLQDLTEEKST------LAGEIRDLK------DMLDVKERKINV------LQKKIENLQEQLRDK 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 271 DKKIKALNHEIEELEKrKDKETGGILRSLEDALAEAQRVNTKsqsafdLKKKNLACEESKRKELeknmvEDSKtlaakeK 350
Cdd:pfam10174 414 DKQLAGLKERVKSLQT-DSSNTDTALTTLEEALSEKERIIER------LKEQREREDRERLEEL-----ESLK------K 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 351 EVKKITDGLHALQ-EASNKDAEALAAAQQHFNAVSAGLssNEDGAEATLAGQMMACKNDISKAQTEAKQAQM-------- 421
Cdd:pfam10174 476 ENKDLKEKVSALQpELTEKESSLIDLKEHASSLASSGL--KKDSKLKSLEIAVEQKKEECSKLENQLKKAHNaeeavrtn 553
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370513639 422 -----KLKHAQQELKNKQAEVKKMDSGYRKDQEAL---EAVKRLKEKLEAEMKKLNYEENKEES 477
Cdd:pfam10174 554 peindRIRLLEQEVARYKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESLTLRQMKEQN 617
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-298 |
3.98e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 43.36 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSIcfllgisnlsqvrasnlqDLVYKNGQAGITKASVS 80
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEAL------------------DIFLNNKEKFFEDDFLV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 81 ITFDNSDKKQSPLgFEVHDEITVTRQVVI-----GGRNKYLINGVNANNTRvQDLFCSVGLNVNNPHFLIMQGRITKVLN 155
Cdd:pfam13175 61 LYLKDVIKIDKED-LNIFENISFSIDIEIdveflLILFGYLEIKKKYLCLA-SKGKAKEYEKTLHPKGANKADLLLELKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 156 MKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEakLKEIKTILEEEITPTIQKLKEE--RSSYLEYQKVMREIEHLSRL 233
Cdd:pfam13175 139 SDLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYE--LPSLKEEFLNSEKEEIKVDKEDlkKLINELEKSINYHENVLENL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513639 234 YIAYQFLLAE-DTKVRSAEELKEMQDKVI--KLQEELSENDKKIKALNHEIEELeKRKDKETGGILRS 298
Cdd:pfam13175 217 QIKKLLISADrNASDEDSEKINSLLGALKqrIFEEALQEELELTEKLKETQNKL-KEIDKTLAEELKN 283
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
248-499 |
4.68e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-----RKDKETGGILRSLEDA--LAEAQRVNTKSQSAFDLK 320
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikreKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 321 KKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHA-LQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG5022 866 KETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESeIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEG 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 400 GQMMACKNDIS-KAQTEAKqaqmKLKHAQQELKNkqaEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESL 478
Cdd:COG5022 946 PSIEYVKLPELnKLHEVES----KLKETSEEYED---LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL 1018
|
250 260
....*....|....*....|....
gi 1370513639 479 LEKRRQLSR---DIGRLKETYEAL 499
Cdd:COG5022 1019 KELPVEVAElqsASKIISSESTEL 1042
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-482 |
7.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370513639 408 DISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKR 482
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-301 |
9.01e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 27 FNAITGLNGSGKSNILDSICFLLGIsnlsqvrASNLQDLVYKNGQAGITKASVSITFDNSDKKqsPLGFEVHdeitvtrq 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADF-------DALVIGLTDERSRNGGIGGIPSLLNGIDPKE--PIEFEIS-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 107 vviggrnKYLINGVNAnntrvqdlfcSVGLNVNNPHFLimqgritkvlnmkppEILSMIEEAAGTRMYEYKKIAaqKTIE 186
Cdd:pfam13304 64 -------EFLEDGVRY----------RYGLDLEREDVE---------------EKLSSKPTLLEKRLLLREDSE--EREP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 187 KKEAKLKEIKTILEEEItpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEE 266
Cdd:pfam13304 110 KFPPEAEELRLGLDVEE--RIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR 187
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370513639 267 LS----ENDKKIKALNHEIEELEKRKDKETGGILRSLED 301
Cdd:pfam13304 188 LVrglkLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
171-498 |
1.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 171 TRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHL-SRLYIAYQFLLAEDTKVRS 249
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkNDIEEQETLLGTIMPEEES 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 250 AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELekrkdketggilrsleDALAEAQRVNTKSQSAfDLKKKNLACEES 329
Cdd:TIGR00606 784 AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS----------------DLDRTVQQVNQEKQEK-QHELDTVVSKIE 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 330 KRKELEKNMVEDSKTLAAKEKEVK----KITDGLHALQEASNKDAEALAAAQQHFNAVSAglSSNEDGAEATLAGQMMAC 405
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKseklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD--AKEQDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 406 KND-ISKAQTEAKQAQMKLKHAQQELKNKQaevkkmdsGYRKDQEAL--EAVKRLKEKLEAEMKKLNYEENKEEsllEKR 482
Cdd:TIGR00606 925 KEElISSKETSNKKAQDKVNDIKEKVKNIH--------GYMKDIENKiqDGKDDYLKQKETELNTVNAQLEECE---KHQ 993
|
330
....*....|....*.
gi 1370513639 483 RQLSRDIGRLKETYEA 498
Cdd:TIGR00606 994 EKINEDMRLMRQDIDT 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-507 |
1.49e-03 |
|
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: 41.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 328 ESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEaTLAGQMMACKN 407
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 408 DISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKeesLLEKRRQLSR 487
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLER 831
|
170 180
....*....|....*....|
gi 1370513639 488 DIGRLKETYEALLARFPNLR 507
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELS 851
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-491 |
2.03e-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: 41.75 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 201 EEITPTIQKLKEERSSYLEyqkVMREIEHLSRLYIAYQFLLAEDTKVRSA------EEL----KEMQDKVIKLQEELSEN 270
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLES---AELRLSHLHFGYKSDETLIASRQEERQEtsaelnQLLrtldDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 271 DKKIKALNHEIEELEKRKdketggilRSLEDALAEaqrvntksQSAFDLKKknlacEESKRKELEkNMVEDSKTLAAKEK 350
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH--------GAFLDADIE--------TAAADQEQ-----LPSWQSELE-NLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 351 EVKKITDGLHALQEASNKDaeALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQEL 430
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 431 KNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGR 491
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
263-501 |
2.07e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 263 LQEELSENDKKIKALNHEIEELEKRKDKETGGI---LRSLEDALAEAQR-VNTKSQSAFDLKKK--NLAC----EESKRK 332
Cdd:pfam10174 441 LEEALSEKERIIERLKEQREREDRERLEELESLkkeNKDLKEKVSALQPeLTEKESSLIDLKEHasSLASsglkKDSKLK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 333 ELEKNMVEDSKTLAAKEKEVKK-------------ITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNED------- 392
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKahnaeeavrtnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENekndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 393 --GAEATLAGQMMACKNdISKAQTEAKQAQMKLKHAQQ-ELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN 469
Cdd:pfam10174 601 kiAELESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLlEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1370513639 470 YEE----NKEESL----LEKRRQLSRdigRLKETYEALLA 501
Cdd:pfam10174 680 STQqslaEKDGHLtnlrAERRKQLEE---ILEMKQEALLA 716
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
251-496 |
2.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKN------- 323
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknksle 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 324 --LACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgaeatlagQ 401
Cdd:TIGR04523 218 sqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK--------Q 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 402 MMACKNDISKAQTEAKQAQMKLKHaqQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKELK--SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
250
....*....|....*
gi 1370513639 482 RRQLSRDIGRLKETY 496
Cdd:TIGR04523 368 KQNEIEKLKKENQSY 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
251-375 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKR--KDKETGGILRSLEDALA-------EAQRVNTKSQSAFDLKK 321
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikKYEEQLGNVRNNKEYEAlqkeiesLKRRISDLEDEILELME 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1370513639 322 KnLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAA 375
Cdd:COG1579 118 R-IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
254-519 |
3.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 254 KEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALaeaqrvNTKSQSAFDLKKKNLACEESKRKE 333
Cdd:PRK01156 472 NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY------NKIESARADLEDIKIKINELKDKH 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 334 LEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALaaaQQHFNAVSAGLSSNEDGA---EATLAGQMMACKNDIS 410
Cdd:PRK01156 546 DKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETN---RSRSNEIKKQLNDLESRLqeiEIGFPDDKSYIDKSIR 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 411 KAQTEAKQAQMKLKHAqQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKrrqLSRDIG 490
Cdd:PRK01156 623 EIENEANNLNNKYNEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDD---AKANRA 698
|
250 260
....*....|....*....|....*....
gi 1370513639 491 RLKETYEALLARFPNLRFAYKDPEKNWNR 519
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLES 727
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
178-500 |
3.79e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 178 KIAAQKTIEKKEAKLKEIKTILEEEiTPTIQKLK-EERSSYLEYQKVMREIEHLSRLYIAYQFL--LAEDTKVRSAEELK 254
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQ-RKAIQELQfENEKVSLKLEEEIQENKDLIKENNATRHLcnLLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 255 emqdkviKLQEELSENDKKIKALNHEIEELekrkdketggiLRSLEDALAEAQrvNTKSQSAFDLK---KKNLACEESKR 331
Cdd:pfam05483 173 -------KYEYEREETRQVYMDLNNNIEKM-----------ILAFEELRVQAE--NARLEMHFKLKedhEKIQHLEEEYK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 332 KELEKNMVEDSKTL---AAKEKEVKKIT-------DGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam05483 233 KEINDKEKQVSLLLiqiTEKENKMKDLTflleesrDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 402 mMACKNDISKAQ------TEAKQAQMK--------------------------LKHAQQELKNKQAEVKKMDSGYRKDQE 449
Cdd:pfam05483 313 -KALEEDLQIATkticqlTEEKEAQMEelnkakaahsfvvtefeattcsleelLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1370513639 450 ALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALL 500
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELI 442
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
242-450 |
4.38e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKikalnhEIEELEKRKDKETGGILRSLEDALAEAQrvntKSQSAFDLKK 321
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKE------RLAAQEQKKQAEEAAKQAALKQKQAEEA----AAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 322 KnlACEESKR-KELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHfnavsaglssnedgAEATLAG 400
Cdd:PRK09510 148 K--AEAEAKRaAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE--------------AEAKKKA 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370513639 401 QMMACKndisKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEA 450
Cdd:PRK09510 212 AAEAKK----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAA 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
360-502 |
5.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 360 HALQEASNKDAEaLAAAQQHFNAVSAGLSSNEDGAEATLAgQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK 439
Cdd:COG3883 13 FADPQIQAKQKE-LSELQAELEAAQAELDALQAELEELNE-EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 440 ---------------------------------MDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLS 486
Cdd:COG3883 91 raralyrsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*.
gi 1370513639 487 RDIGRLKETYEALLAR 502
Cdd:COG3883 171 AELEAQQAEQEALLAQ 186
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-290 |
5.95e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 1 MHIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKngqaGITKASVS 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDD-SEIE-FDTGINIITGKNGAGKSSIVDAIRFAL----FTDKRTEKIEDMIKK----GKNNLEVE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 81 ITF-DNSDKKQSPLGFEVHDEiTVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:PRK01156 71 LEFrIGGHVYQIRRSIERRGK-GSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEMDSLISGDPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTiLEEEITPTIQKLKEERSSYLEYQKVMREIE-HLSRLYIAYQ 238
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDY-LEEKLKSSNLELENIKKQIADDEKSHSITLkEIERLSIEYN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513639 239 flLAEDTKVRSAEELKEM---QDKVIKLQEELSENDKK---IKALNHEIEELEKRKDK 290
Cdd:PRK01156 229 --NAMDDYNNLKSALNELsslEDMKNRYESEIKTAESDlsmELEKNNYYKELEERHMK 284
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
241-370 |
5.98e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 241 LAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVNTKSQSAFDLK 320
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV--------EELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370513639 321 KKNLACEESKRKELEK--NMVED-SKTLAAKEKEVKKITDGLHALQEASNKDA 370
Cdd:COG2433 454 RSEERREIRKDREISRldREIERlERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
328-498 |
6.03e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 328 ESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLagqmMACKN 407
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ----QEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 408 DISKAQTEAKQAQMKLKHAQQ-ELKNKQAEVKKMDSGYRKDQEAleAVKRLKEKLEAEMKKlnyEENKEESLLEKRRQLS 486
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKrEIEKAQIEIKKNDEEALKAKDH--KAFDLKQESKASEKE---AEDKELEAQKKREPVA 334
|
170
....*....|..
gi 1370513639 487 RDIGRLKETYEA 498
Cdd:pfam05262 335 EDLQKTKPQVEA 346
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
190-502 |
6.28e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 190 AKLKEIKT-ILEEEitPTIQKLKEERSSYLEyqkvmreiehlsrlyiayQFLLAEDTKVRSAEELKEMQDkviklqeELS 268
Cdd:PRK11637 47 DQLKSIQQdIAAKE--KSVRQQQQQRASLLA------------------QLKKQEEAISQASRKLRETQN-------TLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 269 ENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQrvntksQSAFDLKkknLACEESKRKEleknmvedsktlaak 348
Cdd:PRK11637 100 QLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGE------HTGLQLI---LSGEESQRGE--------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 349 ekevkKITDGLHALQEASNKDAEALaaaQQhfnavsaglssnedgAEATLAGQmmackndisKAQTEAKQAQMKL----- 423
Cdd:PRK11637 156 -----RILAYFGYLNQARQETIAEL---KQ---------------TREELAAQ---------KAELEEKQSQQKTllyeq 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 424 KHAQQELKNKQAEVKK----MDSGYRKDQEALEAVK----RLKEKL---EAEMKKLNYEENKE-ESLLEKRRQLSRDIGR 491
Cdd:PRK11637 204 QAQQQKLEQARNERKKtltgLESSLQKDQQQLSELRanesRLRDSIaraEREAKARAEREAREaARVRDKQKQAKRKGST 283
|
330
....*....|...
gi 1370513639 492 LKETYE--ALLAR 502
Cdd:PRK11637 284 YKPTESerSLMSR 296
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-49 |
7.10e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 37.99 E-value: 7.10e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
412-501 |
8.30e-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: 38.98 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 412 AQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYE----ENKEESLLEKRRQLSR 487
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaalEAELAELEKEIAELRA 97
|
90
....*....|....
gi 1370513639 488 DIGRLKETYEALLA 501
Cdd:COG4942 98 ELEAQKEELAELLR 111
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
417-515 |
9.35e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513639 417 KQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQ--EALEAVKRLKEKLEAEMK-KLNYEENKEESLLEKRRQLSRDIGRLK 493
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELReRRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100
....*....|....*....|..
gi 1370513639 494 ETYEALLARFPNLRFAYKDPEK 515
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEK 128
|
|
| |
