|
Name |
Accession |
Description |
Interval |
E-value |
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
89-261 |
2.48e-24 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 102.94 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 89 KKLTKQDNLALIKSL-------NlslskdggkKFKYIENLEKCVKLEVLNLSYNLIGKIEKLDKLLKLRELNLSYNKISK 161
Cdd:cd21340 12 KNITKIDNLSLCKNLkvlylydN---------KITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 162 IEGIENMCNLQKLNLAGNEIEhipvwLGKKL-----------KSLRVLNLKGNKISSLQDISKLKPLQDLI--------- 221
Cdd:cd21340 83 VEGLENLTNLEELHIENQRLP-----PGEKLtfdprslaalsNSLRVLNISGNNIDSLEPLAPLRNLEQLDasnnqisdl 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622996215 222 --------------SLILVENPVVTLPHYLQFTIFHLRSLESLEGQPVTTQDRQ 261
Cdd:cd21340 158 eelldllsswpslrELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQ 211
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
96-364 |
3.34e-22 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 101.16 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 96 NLALIKSLNLSlskdgGKKFKYI-ENLEKCVKLEVLNLSYNLIGKI-EKLDKLLKLRELNLSYNKISKI-EGIENMCNLQ 172
Cdd:COG4886 134 NLTNLKELDLS-----NNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLpEPLGNLTNLE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 173 KLNLAGNEIEHIPVWLGkKLKSLRVLNLKGNKISSLQDISKLKPLQdliSLILVENPVVTLPHYLQFTifHLRSLeSLEG 252
Cdd:COG4886 209 ELDLSGNQLTDLPEPLA-NLTNLETLDLSNNQLTDLPELGNLTNLE---ELDLSNNQLTDLPPLANLT--NLKTL-DLSN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 253 QPVTTQDRQEAFERFSLEEVERLERDLEKKMIETEELKSKQTRFLEEIKNQDKLNKSLKEEAMLQKQSCEELKSDLNTKN 332
Cdd:COG4886 282 NQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSL 361
|
250 260 270
....*....|....*....|....*....|..
gi 1622996215 333 ELPLSWFLAGPFLLILYSSLKLKQKTIELTRA 364
Cdd:COG4886 362 LLTLLLTLGLLGLLEATLLTLALLLLTLLLLL 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
454-1077 |
5.87e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAgkdllykQLSGRLQLVNKLRQEALD 533
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-------RLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAGKQKEIKDLQIAIdsldskdpkhshmKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEEL-------------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 614 LEEQLTEGQIAANEALKKDLEgvisglqeylgtIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivaMDAENMR 693
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEE------------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEE---EALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 694 KELAELESALQEQHEVNASLQQTQgdlsAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNA 773
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 774 LGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLV--RPEEVAARVDELRRKLKLGTGEMNIHSP 851
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 852 SDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQM 931
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 932 ENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATA 1011
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 1012 ---ELTIAKDQLKSLhGTVmkiNQERAEELQEA-ERFSRKAAQAArDLTRAEAEIELL-QNLLRQKGEQFR 1077
Cdd:COG1196 765 lerELERLEREIEAL-GPV---NLLAIEEYEELeERYDFLSEQRE-DLEEARETLEEAiEEIDRETRERFL 830
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-1142 |
2.41e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 462 EKKISAAQTRLSELHDEIEKAEQQI--L----RATEEFKQLEEAIQLKKISEAGkdLLYKQLSGRLQlvnKLRQEALDLE 535
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLepLerqaEKAERYRELKEELKELEAELLL--LKLRELEAELE---ELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 536 LQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmkaqksgkEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLE 615
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEEL-----------------ELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 616 EQLTEgqiaaNEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivamdaENMRKE 695
Cdd:COG1196 316 ERLEE-----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------EELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 696 LAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALG 775
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 776 KAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNhvvdglvRPEEVAARVDELRRKLKLGTGEMNIHspsdvl 855
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG-------FLEGVKAALLLAGLRGLAGAVAVLIG------ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 856 gksladlqkqfseilarskWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNFdkrqhEARIQQMENEI 935
Cdd:COG1196 532 -------------------VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF-----LPLDKIRARAA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 936 HYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVfgldkelkklkkAVATSDKLATAELTI 1015
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV------------TLAGRLREVTLEGEG 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1016 AKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLEmektgvgtgansqVLE 1095
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE-------------ELE 722
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1622996215 1096 IEKLNETMERQRTEIARLQNVLDLTGSDNKGGFENVLEEIAELRREV 1142
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
55-250 |
3.06e-19 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 92.30 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 55 QVEIADENNMLLDYQDHKGADSHAGVRYITEALIKKLTKQDNLALIKSLNLSLSKDGGKKFKYIENLEKCVKLEVLNLSY 134
Cdd:COG4886 43 LSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 135 NLIGKI-EKLDKLLKLRELNLSYNKISKI-EGIENMCNLQKLNLAGNEIEHIPVWLGkKLKSLRVLNLKGNKISSLQD-I 211
Cdd:COG4886 123 NQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELG-NLTNLKELDLSNNQITDLPEpL 201
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622996215 212 SKLKPLQdliSLILVENPVVTLPHylqfTIFHLRSLESL 250
Cdd:COG4886 202 GNLTNLE---ELDLSGNQLTDLPE----PLANLTNLETL 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-1138 |
4.82e-19 |
|
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: 94.35 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 456 TQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAI-----QLKKISEAGKDLLYKQLSGRLQLVnKLRQE 530
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleqQKQILRERLANLERQLEELEAQLE-ELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 531 ALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKhshMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEE 610
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 611 IKDLEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAE 690
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 691 NMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDaeanqlKEELEKVTRLTQLEQSALQAELEKERQAL 770
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE------GYEAAIEAALGGRLQAVVVENLNAAKKAI 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 771 ----KNALGKAQFSE-------EKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVrpeeVAARVDELRRKL 839
Cdd:TIGR02168 563 aflkQNELGRVTFLPldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVL----VVDDLDNALELA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 840 KLGTGEMNIHSPSDVL---------GKSLADLQKQFSEI-LARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQAC 909
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLvrpggvitgGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 910 ERALEAR-----MNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEkkKKLEDAKS 984
Cdd:TIGR02168 719 KELEELSrqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE--AQIEQLKE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 985 QEQVFGLDKELKKLKKAvATSDKLATAELTIA--KDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEI 1062
Cdd:TIGR02168 797 ELKALREALDELRAELT-LLNEEAANLRERLEslERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622996215 1063 ELLQNLLRQKGEQF-RLEMEKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDLTgsdnKGGFENVLEEIAEL 1138
Cdd:TIGR02168 876 EALLNERASLEEALaLLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL----EVRIDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-840 |
4.90e-17 |
|
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: 87.80 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 RQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKhshMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKE 607
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 608 TEEIKDLEEQLTE--GQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIV 685
Cdd:TIGR02168 753 SKELTELEAEIEEleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 686 AMDAENMRKELAE-LESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEkvtRLTQLEQSalQAELE 764
Cdd:TIGR02168 833 IAATERRLEDLEEqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS---ELEELSEE--LRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622996215 765 KERQALKNALGKAQFSEEKEQEN-SELHAKLKHLQDdnNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLK 840
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRlEGLEVRIDNLQE--RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
602-982 |
6.99e-15 |
|
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: 80.49 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 602 SRIAKETEEIKDLEEQLTEGQIAANEALKK--DLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQER 679
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKEleELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 680 DQLEIVAMDAENMRKEL-AELESALQEQHEVNASLQQTQGDLSAYEA---ELEARLNLRDAEANQLKEELEKVT-RLTQL 754
Cdd:TIGR02168 757 TELEAEIEELEERLEEAeEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLErRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 755 EQSALQAELEKERQALKNALGKAQFSEEKEQENsELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLvrpEEVAARVDE 834
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 835 LRRKLKLgtgemnihspsdvlgksladLQKQFSEILARskweRDEAQVRERKLQEEMALQQEKLATGQEEfrqaceraLE 914
Cdd:TIGR02168 913 LRRELEE--------------------LREKLAQLELR----LEGLEVRIDNLQERLSEEYSLTLEEAEA--------LE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 915 ARMNFDKRQHEARIQQMENEIHYLQE-NLKSMEEiqgltdlqLQEADEEKERILAQLRELEK-KKKLEDA 982
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPvNLAAIEE--------YEELKERYDFLTAQKEDLTEaKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-972 |
3.86e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 449 RGHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKiseagkdllyKQLSGRLQLVNKLR 528
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----------AELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 529 QEALDLELQMEKQKQEIAGKQKEIKDLQiaidsldskdpkhshmkaqksgkeqqldimnKQYQQLESRLDEILSRIAKET 608
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELA-------------------------------AQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 609 EEIKDLEEQLTEGQIAANEALKKDLEgvisgLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMD 688
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 689 AENMRKELAELESALQEQHEVNAS------LQQTQGDLSAYEAELEARLNLRDAEANQLKEElekvtRLTQLEQSALQAE 762
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-----VAAAAIEYLKAAK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 763 LEKERQALKNALGKAQFSEEKEQENSELHAKLKhLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLKLG 842
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 843 TGEMNIHSPsdvlGKSLADLQKQFSEILARSKwERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKR 922
Cdd:COG1196 650 TLEGEGGSA----GGSLTGGSRRELLAALLEA-EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622996215 923 QHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRE 972
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| LRR_9 |
pfam14580 |
Leucine-rich repeat; |
130-279 |
5.56e-14 |
|
Leucine-rich repeat;
Pssm-ID: 405295 [Multi-domain] Cd Length: 175 Bit Score: 71.72 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 130 LNLSYNLIGKIEKLDKLL-KLRELNLSYNKISKIEGIENMCNLQKLNLAGNEIEHIPVWLGKKLKSLRVLNLKGNKISSL 208
Cdd:pfam14580 24 LDLRGYKIPIIENLGATLdQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQEL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 209 QDISKLKPLQDLISLILVENPVVTLPHYLQFTIFHLRSLESLEGQPVTTQDRQEAFERFSLEEVERLERDL 279
Cdd:pfam14580 104 GDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQLAKEI 174
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
462-1142 |
1.14e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 462 EKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEaiqlkkISEAGKDllYKQLSGRLQlvnklRQEALDLELQMEKQ 541
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLEP------IRELAER--YAAARERLA-----ELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 542 KQEIAGKQKEIKDLQIAIDSLDskdpkhshmkAQKSGKEQQLDIMNKQYQQLESRLDEIlsriakETEEIKDLEEqlteg 621
Cdd:COG4913 287 QRRLELLEAELEELRAELARLE----------AELERLEARLDALREELDELEAQIRGN------GGDRLEQLER----- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 622 QIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNE----CRKLRDEKETLLQRLTEVEQERDQLEIvamDAENMRKELA 697
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 698 ELESALqeqhevnASLQQTQGDLSAYE----AELEARLNLRDAEAN------QLKEE-------LEKV---TRLTQLeqs 757
Cdd:COG4913 423 ELEAEI-------ASLERRKSNIPARLlalrDALAEALGLDEAELPfvgeliEVRPEeerwrgaIERVlggFALTLL--- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 758 alqAELEKERQALK--NAL---GKAQFSEEKEQENSELHAKLkhlqDDNNLL-KQQLKD--FQNHLNHVvdgLVRPEEVA 829
Cdd:COG4913 493 ---VPPEHYAAALRwvNRLhlrGRLVYERVRTGLPDPERPRL----DPDSLAgKLDFKPhpFRAWLEAE---LGRRFDYV 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 830 --ARVDELRR-----------KLKLGTGEMNIHSPSD---VLGKS----LADLQKQfseiLARSKWERDEAQVRERKLQE 889
Cdd:COG4913 563 cvDSPEELRRhpraitragqvKGNGTRHEKDDRRRIRsryVLGFDnrakLAALEAE----LAELEEELAEAEERLEALEA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 890 EMALQQEKlatgqeefRQACERALEARMNF-DKRQHEARIQQMENEihyLQENLKSMEEIQGLTDlQLQEADEEKERILA 968
Cdd:COG4913 639 ELDALQER--------REALQRLAEYSWDEiDVASAEREIAELEAE---LERLDASSDDLAALEE-QLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 969 QLRELEKK-----KKLEDAKSQEQvfgldkelkklkkavATSDKLATAELTIAKDQLKSLhgtvmkinQERAEELQEAER 1043
Cdd:COG4913 707 ELDELKGEigrleKELEQAEEELD---------------ELQDRLEAAEDLARLELRALL--------EERFAAALGDAV 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1044 FSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLE--MEKTGVGTG--ANSQVLEI-EKL-NETMERQRTEIARLQNvl 1117
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERAMRAFNREwpAETADLDADleSLPEYLALlDRLeEDGLPEYEERFKELLN-- 841
|
730 740
....*....|....*....|....*
gi 1622996215 1118 dltgSDNKGGFENVLEEIAELRREV 1142
Cdd:COG4913 842 ----ENSIEFVADLLSKLRRAIREI 862
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-1063 |
1.41e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 258 QDRQEAFERFSlEEVERLERDLEKKMIETEELKSKQTRFLEEI-KNQDKLNKSLKEEAMLQKQScEELKSDLNTKNElpl 336
Cdd:TIGR02168 284 EELQKELYALA-NEISRLEQQKQILRERLANLERQLEELEAQLeELESKLDELAEELAELEEKL-EELKEELESLEA--- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 337 swflagpfllilysslklkqktiELTRACQKQYELEQelafyKIDAKFEPLNYYPSEYAEIDKApdespyIGKSRYKRNM 416
Cdd:TIGR02168 359 -----------------------ELEELEAELEELES-----RLEELEEQLETLRSKVAQLELQ------IASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 417 FATESYIIDSAQA--VQIKKMEPDEQLRNDHMNLRGHTP-LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEF 493
Cdd:TIGR02168 405 LEARLERLEDRRErlQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 494 KQLEEAI--------QLKKISEAGKDLLYKQ--LSGRLQLVNKLRQEALDLELQMEKQKQEIAGkQKEIKDLQIA---ID 560
Cdd:TIGR02168 485 AQLQARLdslerlqeNLEGFSEGVKALLKNQsgLSGILGVLSELISVDEGYEAAIEAALGGRLQ-AVVVENLNAAkkaIA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 561 SLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQL-------TEGQIAANEALKKDL 633
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvDDLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 634 EGVISGLQEYLGTIKGQATQAQNEcrklrdEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEqhevnasL 713
Cdd:TIGR02168 644 GYRIVTLDGDLVRPGGVITGGSAK------TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE-------L 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 714 QQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALqAELEKERQALKNALGKAQFS-EEKEQENSELHA 792
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL-TELEAEIEELEERLEEAEEElAEAEAEIEELEA 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 793 KLKHLQDDNNLLKQQLKDFQnhlnhvvdglvrpeevaARVDELRRKL-KLGTGEMNIHSPSDVLGKSLADLQKQF---SE 868
Cdd:TIGR02168 790 QIEQLKEELKALREALDELR-----------------AELTLLNEEAaNLRERLESLERRIAATERRLEDLEEQIeelSE 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 869 ILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQAceralearmNFDKRQHEARIQQMENEIHYLQENLKSMEEI 948
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALL---------RSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 949 QGLTDLQLQEADEEKERILAQLRElEKKKKLEDAKSQEQvfgldkelkklkkAVATSDKLATAELTIAKDQLKSLhGTVm 1028
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSE-EYSLTLEEAEALEN-------------KIEDDEEEARRRLKRLENKIKEL-GPV- 987
|
810 820 830
....*....|....*....|....*....|....*.
gi 1622996215 1029 kiNQERAEELQE-AERFSRKAAQAArDLTRAEAEIE 1063
Cdd:TIGR02168 988 --NLAAIEEYEElKERYDFLTAQKE-DLTEAKETLE 1020
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
83-250 |
5.72e-13 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 73.04 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 83 ITEALIKKLTKQDNLALIKSLNLSLSKDGGKKFKYIENLEKCVKLEVLNLSYNLIGKIEKLDKLLKLRELNLSYNkiski 162
Cdd:COG4886 32 LLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 163 EGIENMCNLQKLNLAGNEIEHIPVWLGkKLKSLRVLNLKGNKISSLQdiSKLKPLQDLISLILVENPVVTLPHylqfTIF 242
Cdd:COG4886 107 EELSNLTNLESLDLSGNQLTDLPEELA-NLTNLKELDLSNNQLTDLP--EPLGNLTNLKSLDLSNNQLTDLPE----ELG 179
|
....*...
gi 1622996215 243 HLRSLESL 250
Cdd:COG4886 180 NLTNLKEL 187
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
433-1038 |
1.01e-12 |
|
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: 73.54 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 433 KKMEPDEQLRNDH-------MNLRGHTPLDTQLED----KEKKISAAQTRLSELHDEIEKAEQ-------QILRATEEFK 494
Cdd:TIGR00606 543 DKMDKDEQIRKIKsrhsdelTSLLGYFPNKKQLEDwlhsKSKEINQTRDRLAKLNKELASLEQnknhinnELESKEEQLS 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 495 QLEEAI------------------QLKKISE-----AGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGK-QK 550
Cdd:TIGR00606 623 SYEDKLfdvcgsqdeesdlerlkeEIEKSSKqramlAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDlQS 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 551 EIKDLQIAIDSLDS----KDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLteGQIAAN 626
Cdd:TIGR00606 703 KLRLAPDKLKSTESelkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL--GTIMPE 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 627 EALKKDLE---GVISGLQEYLGTIKGQATQAQNECRKLrDEKETLLQRLTEVEQERDQLEIVAMDAENMRKelaelesAL 703
Cdd:TIGR00606 781 EESAKVCLtdvTIMERFQMELKDVERKIAQQAAKLQGS-DLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-------LI 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 704 QEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVtrltqleQSALQAELEKERQALKNALGKAQFSEEK 783
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-------QSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 784 EQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEvaarvDELRRKlklgtgEMNIHSPSDVLGKSlADLQ 863
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD-----DYLKQK------ETELNTVNAQLEEC-EKHQ 993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 864 KQFSEILARSKWERDEAQVRERKLQEEMALQ--QEKLATGQEEFRQaceralearmnFDKRQHEARIQQMENEIHYLQEN 941
Cdd:TIGR00606 994 EKINEDMRLMRQDIDTQKIQERWLQDNLTLRkrENELKEVEEELKQ-----------HLKEMGQMQVLQMKQEHQKLEEN 1062
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 942 LKSMEeiqgltdlqlqeadEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTIAKdqlK 1021
Cdd:TIGR00606 1063 IDLIK--------------RNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYY---K 1125
|
650
....*....|....*..
gi 1622996215 1022 SLHGTVMKINQERAEEL 1038
Cdd:TIGR00606 1126 TLDQAIMKFHSMKMEEI 1142
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
438-1157 |
2.33e-12 |
|
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: 72.18 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 438 DEQLRNDHMNLRGHTpldTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISeagKDLLYKQL 517
Cdd:pfam12128 229 DIQAIAGIMKIRPEF---TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT---LDDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 518 SGRLqlvnKLRQEALDLELQMEKQKQEIAGKQKEI---KDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLE 594
Cdd:pfam12128 303 RDEL----NGELSAADAAVAKDRSELEALEDQHGAfldADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 595 SRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKKDLEGVISGLQEylgtikgqatQAQNECRKLRDEKETLLQRLTE 674
Cdd:pfam12128 379 RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELRE----------QLEAGKLEFNEEEYRLKSRLGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 675 VEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEA---RLNLRDAEANQLKEELEKVTRL 751
Cdd:pfam12128 449 LKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQaseALRQASRRLEERQSALDELELQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 752 TQLEQSALQAELEKERQALKNALGKAQFSEekeqensELHAKLKHLQDDNNLLKQQLKDFQNHLNhvVDGLVRPEEVAAR 831
Cdd:pfam12128 529 LFPQAGTLLHFLRKEAPDWEQSIGKVISPE-------LLHRTDLDPEVWDGSVGGELNLYGVKLD--LKRIDVPEWAASE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 832 vDELRRKLklgtgemnihspsDVLGKSL---ADLQKQFSEILARSKWERDEAQVRE---RKLQEEMALQQEKLATGQEEF 905
Cdd:pfam12128 600 -EELRERL-------------DKAEEALqsaREKQAAAEEQLVQANGELEKASREEtfaRTALKNARLDLRRLFDEKQSE 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 906 RQACERALEARmnfdKRQHEARIQQMENEIHYLQENLKSMEEIQgltDLQLQEADEEKeriLAQLRELEKKKKLEDAKSQ 985
Cdd:pfam12128 666 KDKKNKALAER----KDSANERLNSLEAQLKQLDKKHQAWLEEQ---KEQKREARTEK---QAYWQVVEGALDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 986 EQVFGLDKELKKLKKAVATS-----DKLATAELTIAK--DQLKSLHGTVMKINQERAEELQ----EAERFSRKAAQAARD 1054
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWykrdlASLGVDPDVIAKlkREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQ 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1055 LTRAEAEIELLQNLLRQKGEQFRLEMEKTGVGTGANSQVLeiEKLNETMERQRTEIARLQNV-LDLTGSDNKGGFENVLE 1133
Cdd:pfam12128 816 LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ--VRLSENLRGLRCEMSKLATLkEDANSEQAQGSIGERLA 893
|
730 740
....*....|....*....|....
gi 1622996215 1134 EIAELRREVSYQNDYISSMADPFK 1157
Cdd:pfam12128 894 QLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1353-1609 |
7.79e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1353 HLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTELEIEKSLKH 1432
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1433 H-----EDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETA 1507
Cdd:COG1196 313 EleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1508 VNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVL 1587
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260
....*....|....*....|..
gi 1622996215 1588 KESEVLLQAKRAELEKLKSQVW 1609
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
478-1095 |
9.78e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 478 EIEKAEQQILRATEEFKQLEEAiqlKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLElqmEKQKQEIAGKQKEIKDLQI 557
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEA---KKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---EARKADELKKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 558 AIDSLDSKDPKHSHMKAQKSGKEQQLdimNKQYQQLESRLDEILSRI--AKETEEIKDLEEQLTEGQIAANEALKKDLEG 635
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 636 VISGLQEYLGTIKGQATQAQ--NECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKElAELESALQEQHEVNASL 713
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA-DEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 714 QQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQ-LEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHA 792
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 793 KLKHLQDDNNLLKQQLKdfqnhlnhvVDGLVRPEEVaaRVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILAR 872
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKK---------ADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 873 SKWERDEAQVRERKLQEEMALQQEKLATGQEEfRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLT 952
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 953 DLQLQEaDEEKERILAQLRELEKKKKLEDAKSQEQvfgldkelkkLKKAVATSDKLATAELTIAKDQLKSLHgtvmKINQ 1032
Cdd:PTZ00121 1679 EAKKAE-EDEKKAAEALKKEAEEAKKAEELKKKEA----------EEKKKAEELKKAEEENKIKAEEAKKEA----EEDK 1743
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 1033 ERAEELQEAERFSRKAAQAARDLTRAEAEIE-----LLQNLLRQKGEQFRLEMEKTGVGTGANSQVLE 1095
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkekeaVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
534-818 |
1.49e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAgKQKEIKDLQIAI--DSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEI 611
Cdd:TIGR02168 205 LERQAEKAERYKE-LKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 612 KDLEEQLTEGQIaaneaLKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIvamDAEN 691
Cdd:TIGR02168 284 EELQKELYALAN-----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---ELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 692 MRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELE----KVTRLTQLEQSALQAELEKER 767
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErledRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 768 QALKNALG-KAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHV 818
Cdd:TIGR02168 436 KELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
648-978 |
2.91e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 648 KGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKEL-AELESALQEQHEVNASLQQTQGDLSAYE-- 724
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIeKEIEQLEQEEEKLKERLEELEEDLSSLEqe 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 725 --------AELEARLNLRDAEANQLKEELEKVTRLTQLEQ----SALQAELEKERQALKNALGKAQFSEEKEQENSE-LH 791
Cdd:TIGR02169 753 ienvkselKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 792 AKLKHLQDDNNLLKQQLKDFQNHLNhvvDGLVRPEEVAARVDELRRKLK-LGTGEMNIHSPSDVLGKSLADLQKQFSEIl 870
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRdLESRLGDLKKERDELEAQLRELERKIEEL- 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 871 arsKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACEralEARMNFDKRQHEARIQQMENEIHYLQE-NLKSMEE-- 947
Cdd:TIGR02169 909 ---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE---IPEEELSLEDVQAELQRVEEEIRALEPvNMLAIQEye 982
|
330 340 350
....*....|....*....|....*....|....*
gi 1622996215 948 --IQGLTDLQLQEA--DEEKERILAQLRELEKKKK 978
Cdd:TIGR02169 983 evLKRLDELKEKRAklEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
479-1143 |
5.54e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 479 IEKAEQQILRATEEFKQLEEaiQLKKIseagkDLLYKQLSGRLQLVNKLRQEALD-LELQMEKQKQEIAGKQKEIKDLQI 557
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEE--NIERL-----DLIIDEKRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 558 AIDSLDskdpkhshmkAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDL--EEQLT-EGQIAANEALKKDLE 634
Cdd:TIGR02169 238 QKEAIE----------RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeEEQLRvKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 635 GVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivaMDAENMRKELAELESALQEqheVNASLQ 714
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEE---VDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 715 QTQGDLSAYEAELEarlnlrdaeanQLKEELEKVTRltqlEQSALQAELEKerqalknalgkaqfseeKEQENSELHAKL 794
Cdd:TIGR02169 382 ETRDELKDYREKLE-----------KLKREINELKR----ELDRLQEELQR-----------------LSEELADLNAAI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 795 KHLQDDNNLLKQQLKDFQNHLNHVVDGLvrpEEVAARVDELRRKLKlgtgemNIHSPSDVLGKSLADLQKQFSEILARSK 874
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKL---EQLAADLSKYEQELY------DLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 875 WERDEaqVRERKLQEEMALQQEKLATGQ--------EEFRQACERALEARMNFDKRQHEA-------------------- 926
Cdd:TIGR02169 501 ASEER--VRGGRAVEEVLKASIQGVHGTvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAvakeaiellkrrkagratfl 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 927 ---RIQQMENEIHYLQE--------NLKSMEE------IQGLTDLQLQEADEEKERILAQLRELEKKKKLEDaKSQEQVF 989
Cdd:TIGR02169 579 plnKMRDERRDLSILSEdgvigfavDLVEFDPkyepafKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFE-KSGAMTG 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 990 GLDKELKKLKKAVATSDKLA--TAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQN 1067
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQrlRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 1068 LLRQKGEQFR-LEMEKTGVGTgansqvlEIEKLNETMERQRTEIARLQNVL-DLTGSDNKGGFENVLEEIAELRREVS 1143
Cdd:TIGR02169 738 RLEELEEDLSsLEQEIENVKS-------ELKELEARIEELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKLEEEVS 808
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-798 |
2.07e-10 |
|
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: 65.86 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRAtEEFKqleeAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEAlDLEL 536
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQ----ALLKEKREYEGYELLKEKEALERQKEAIERQLA-SLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQKEIKDLQIAIDSLDSKdpkhshmkAQKSGKEQQLDImNKQYQQLESRLDEILSRIAKETEEIKDLEE 616
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKK--------IKDLGEEEQLRV-KEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 617 QLTEGqiaanEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQE----RDQLEIVAMDAENM 692
Cdd:TIGR02169 323 RLAKL-----EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 693 RKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRltQLEQsaLQAELEKERQALKN 772
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW--KLEQ--LAADLSKYEQELYD 473
|
330 340
....*....|....*....|....*..
gi 1622996215 773 ALGK-AQFSEEKEQENSELHAKLKHLQ 798
Cdd:TIGR02169 474 LKEEyDRVEKELSKLQRELAEAEAQAR 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
529-776 |
2.25e-10 |
|
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: 64.40 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 529 QEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKET 608
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKAL----------LKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 609 EEIKDLEEQLtegqiaanEALKKDLEGVI-----SGLQEYLGTIKGQ--ATQAQNECRKLRDEKETLLQRLTEVEQERDQ 681
Cdd:COG4942 90 KEIAELRAEL--------EAQKEELAELLralyrLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 682 LEIVAMDAENMRKELAELESALQEQHevnASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRL-TQLEQSALQ 760
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEER---AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAA 238
|
250
....*....|....*.
gi 1622996215 761 AELEKERQALKNALGK 776
Cdd:COG4942 239 AAERTPAAGFAALKGK 254
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
454-1104 |
3.47e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKK-----ISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQlkkiseagkdllykqlsgrlqlvnklr 528
Cdd:PRK02224 192 LKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLE--------------------------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 529 qealdlelqmekqkqEIAGKQKEIKDLQIAIDSLDSKdpkhshmkaqKSGKEQQLDIMNKQYQQLESRLDEILSRIaket 608
Cdd:PRK02224 245 ---------------EHEERREELETLEAEIEDLRET----------IAETEREREELAEEVRDLRERLEELEEER---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 609 EEIKDlEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivaMD 688
Cdd:PRK02224 296 DDLLA-EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE---SE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 689 AENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELekvtrltqleqsalqAELEKERQ 768
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE---------------AELEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 769 ALKNALGKAQ----------------------FSEEKEQENSELHAKLkhlqddnnllkQQLKDFQNHLNHVVDGLVRPE 826
Cdd:PRK02224 437 TARERVEEAEalleagkcpecgqpvegsphveTIEEDRERVEELEAEL-----------EDLEEEVEEVEERLERAEDLV 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 827 EVAARVDELRRKLKLGTGEMNIHSPS-DVLGKSLADLQKQFSEILARSKWERDEAQvrerKLQEEMALQQEKLATGQEEf 905
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETiEEKRERAEELRERAAELEAEAEEKREAAA----EAEEEAEEAREEVAELNSK- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 906 RQACERALEARMNFDKRQheARIQQMENEIHYLQENLKSMEEIQgltdlqlqeaDEEKERiLAQLRelEKKKKLEDAKSQ 985
Cdd:PRK02224 581 LAELKERIESLERIRTLL--AAIADAEDEIERLREKREALAELN----------DERRER-LAEKR--ERKRELEAEFDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 986 EQVFGLDKELKKLKKAVATSDKlATAELTIAKDQLKSLHGTVmKINQERAEELQEaerfsRKAAQAAR--DLTRAEAEIE 1063
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEE-KLDELREERDDLQAEIGAV-ENELEELEELRE-----RREALENRveALEALYDEAE 718
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1622996215 1064 LLQNLLRqkgeQFRLEMEKTGVGTgansqvLEIeKLNETME 1104
Cdd:PRK02224 719 ELESMYG----DLRAELRQRNVET------LER-MLNETFD 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
270-1112 |
6.44e-10 |
|
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: 64.22 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 270 EEVERLERDLEKKMIETEELKSKQTRFLEEIKNQDKLNKSLKEEAMLQKQSCEELKSDLNTKNELPLSWFLAGPFLLILY 349
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 350 SSLKLKQKTIELTRACQKQYELEQELAFYKIDAKFEPLNYYPSEYAEIDKAPDESPYIGKSRykrnmfaTESYIIDSAQA 429
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER-------RKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 430 VQIKKMEPDEQLRNDHMNLrghTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAG 509
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEI---EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 510 KDLLYKQLSGRLQLVNKLRQEALDL---ELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIM 586
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLlkeEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 587 NKQYQQLESRLDEILSRIAKETEEIKDLEEQ-LTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEK 665
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARsGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 666 ETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEEL 745
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 746 EKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRP 825
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 826 EEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEF 905
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 906 RQACERALEARMNFDKRQ--HEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAK 983
Cdd:pfam02463 796 LKAQEEELRALEEELKEEaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 984 SQEQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIE 1063
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1622996215 1064 LLQNLLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEIAR 1112
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
457-912 |
9.24e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDL--LYKQLSGRLQLVNKLRQEALDL 534
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 535 ELQMEKQKQEIAGKQKEIKDLqiaidsldskdpkhshMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDL 614
Cdd:COG4717 162 EEELEELEAELAELQEELEEL----------------LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 615 EEQLTEGQiaaNEALKKDLEGVISGLQEYLGTIKGQATQAQnecrkLRDEKETLLQRLTEVEQERdqLEIVAMDAENMRK 694
Cdd:COG4717 226 EEELEQLE---NELEAAALEERLKEARLLLLIAAALLALLG-----LGGSLLSLILTIAGVLFLV--LGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 695 ELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKV-TRLTQLEQSALQAELEKERQALKNA 773
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELqELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 774 LGKAQFSEEKE-QENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVrPEEVAARVDELRRKLKLGTGEMnihsps 852
Cdd:COG4717 376 LAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-EEELEEELEELEEELEELEEEL------ 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 853 DVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQ-EEMALQQEKLATGQEEFRQACERA 912
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAELLQELEELKAElRELAEEWAALKLALELLEEAREEY 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1372-1608 |
1.04e-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: 63.54 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1372 EKEMEELHHNIDDLLQEKKSLECEVEELhrTVQKRQQQKDFIDGNVESLMTELEIEKSLKHHEDIVDEIECIEKTLLKRR 1451
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEEL--EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1452 SELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHK 1531
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1532 IKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHL-------QVLKESEVLLQAKRAELEKL 1604
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEEL 920
|
....
gi 1622996215 1605 KSQV 1608
Cdd:TIGR02168 921 REKL 924
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
650-1079 |
1.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 650 QATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESA---LQEQHEVNASLQQTQGDLSAYEAE 726
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 727 LEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNAlgkaqfsEEKEQENSELHAKLKHLQDDNNLLKQ 806
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL-------EELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 807 QLKDFQNHLnhvvdglvRPEEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQK----------QFSEILARSKWE 876
Cdd:COG4717 228 ELEQLENEL--------EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllaLLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 877 RDEAQVRERKLQEEMALQQEKLATGQEEFRqaCERALEARMNFDKRQHEARIQQMENEIHYLQENLK---SMEEIQGLTD 953
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQleeLEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 954 LQLQEADEEKERILAQLREL-EKKKKLEDAKSQ-EQVFGLDKELKKLKKAVATSDKLATAELTIA--KDQLKSLHGTVMK 1029
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYqELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEelEEELEELREELAE 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 1030 INQ-----ERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLE 1079
Cdd:COG4717 458 LEAeleqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
542-1141 |
1.86e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 542 KQEIAGKqkEIKDLQIAIDSLDSK----DPKHSHMKAQKSGKEQQLDimnkqyqqlesRLDEILSRIAKETEEIKDLEEQ 617
Cdd:PRK02224 193 KAQIEEK--EEKDLHERLNGLESElaelDEEIERYEEQREQARETRD-----------EADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 618 LTEGQ--IAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLeivamdaenmRKE 695
Cdd:PRK02224 260 IEDLRetIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL----------RDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 696 LAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKvtRLTQLEqsALQAELEKERQALKNA-- 773
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--RREEIE--ELEEEIEELRERFGDApv 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 774 -LGKAQ-FSEEKEQENSELHAKLKHLQDDnnllkqqlkdfqnhlnhvvdgLVRPEEVAARVDELRRKLKLGTGEMNIHSP 851
Cdd:PRK02224 406 dLGNAEdFLEELREERDELREREAELEAT---------------------LRTARERVEEAEALLEAGKCPECGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 852 SDVlgKSLADLQKQFSEILA-RSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEarmnfdkrQHEARIQQ 930
Cdd:PRK02224 465 PHV--ETIEEDRERVEELEAeLEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA--------ERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 931 MENEIHYLQENLKSMEEiqgltdlqlqEADEEKERilAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDklat 1010
Cdd:PRK02224 535 KRERAEELRERAAELEA----------EAEEKREA--AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL---- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1011 AELTIAKDQLKSLhgtvmkinQERAEELQEAERFSRKAAQAARDLTRA------EAEIELLQNLlRQKGEQFrlemektg 1084
Cdd:PRK02224 599 AAIADAEDEIERL--------REKREALAELNDERRERLAEKRERKREleaefdEARIEEARED-KERAEEY-------- 661
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622996215 1085 vgtgansqvleIEKLNETMERQRTEIARLQNVLdltgsdnkGGFENVLEEIAELRRE 1141
Cdd:PRK02224 662 -----------LEQVEEKLDELREERDDLQAEI--------GAVENELEELEELRER 699
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
457-679 |
3.73e-09 |
|
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: 60.55 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEeaiqlKKISEAGKDLlyKQLSGRLqlvNKLRQEALDLEL 536
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-----RRIAALARRI--RALEQEL---AALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSgkeQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEE 616
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 617 QLT------EGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQER 679
Cdd:COG4942 168 ELEaeraelEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
442-1141 |
3.76e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 442 RNDHMN-LRGHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQ----LKKISEAGK-DLLYK 515
Cdd:PTZ00121 1062 AKAHVGqDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaedARKAEEARKaEDARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 516 QLSGRLQLVNKLRQEALDLElqmEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHmKAQKSGKEQQLDIMNKQYQQLES 595
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAE---DARKAEEARKAEDAKKAEAARKAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 596 RLDEILSRI--AKETEEI-KDLEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRL 672
Cdd:PTZ00121 1218 RKAEDAKKAeaVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 673 TEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARlnlrdAEANQLKEELEKVTRLT 752
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA-----ADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 753 QLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQnhlnhvVDGLVRPEEVAARV 832
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK------ADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 833 DELRRKLKLGTGEMNIHSPSDVLGKSlADLQKQFSEilaRSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACE-- 910
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKA-DEAKKKAEE---AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEak 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 911 RALEARMNFDKRQ-HEARIQQMENEIHYLQ--ENLKSMEEIQgltdlQLQEADEEKERILAQLRELEKKKKLEDAKSQE- 986
Cdd:PTZ00121 1523 KADEAKKAEEAKKaDEAKKAEEKKKADELKkaEELKKAEEKK-----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEv 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 987 -QVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQE--RAEELQEAERFSR-KAAQAAR----DLTRA 1058
Cdd:PTZ00121 1598 mKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKiKAAEEAKkaeeDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1059 EaEIELLQNLLRQKGEQFRLEMEKTgvgtganSQVLEIEKLNETMERQRTEIARLQNVLDLTGSDNKGGFENVLEEIAEL 1138
Cdd:PTZ00121 1678 E-EAKKAEEDEKKAAEALKKEAEEA-------KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
...
gi 1622996215 1139 RRE 1141
Cdd:PTZ00121 1750 KKD 1752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1368-1605 |
3.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1368 KRQSEKEMEELHHN---IDDLLQEK----KSLE--CEVEELHRTVQKRQQQKDfidgnveSLMTELEIEKSLKHHEDIVD 1438
Cdd:COG1196 174 KEEAERKLEATEENlerLEDILGELerqlEPLErqAEKAERYRELKEELKELE-------AELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1439 EIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLR 1518
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1519 SLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKR 1598
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
....*..
gi 1622996215 1599 AELEKLK 1605
Cdd:COG1196 407 EAEEALL 413
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
558-789 |
4.43e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 558 AIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQiAANEALKKDLEGVI 637
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE-AEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 638 SGLQE------YLGTIKGQATQAqnecrklrdekeTLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQhevNA 711
Cdd:COG3883 93 RALYRsggsvsYLDVLLGSESFS------------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK---LA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 712 SLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSE 789
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
460-777 |
5.60e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 460 DKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEaiqlkkiseagkdllykqlsgrlqlvnklRQEALDLELQME 539
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE-----------------------------RREALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 540 KQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMkaqksgkEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLT 619
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERLDASSDDLAAL-------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 620 EGQIAANEALKKDLEGVISGLQEYLGTIKGQATQA------QNECRKLRDEKETLLQRLT-------------------- 673
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERelrenlEERIDALRARLNRAEEELEramrafnrewpaetadldad 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 674 -----EVEQERDQLE----------IVAMDAENMRKELAELESALQEQ--------HEVNASLQQTQ-GDLSAYEAELEA 729
Cdd:COG4913 811 leslpEYLALLDRLEedglpeyeerFKELLNENSIEFVADLLSKLRRAireikeriDPLNDSLKRIPfGPGRYLRLEARP 890
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622996215 730 RlnlRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKA 777
Cdd:COG4913 891 R---PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSE 935
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
580-788 |
1.51e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 580 EQQLDIMNKQYQQLESRLDEILSR--IAKETEEIKDLEEQLTE--GQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQ 655
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSEleSQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 656 NEcrklrDEKETLLQRLTEVEQERDQLEIVAMDA----ENMRKELAELESALQEqhEVNASLQQTQGDLSAyeaeLEARL 731
Cdd:COG3206 261 QS-----PVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQ--EAQRILASLEAELEA----LQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622996215 732 NLRDAEANQLKEELEKVTRLtQLEQSALQAELEKERQALKNALGKAQFSEEKEQENS 788
Cdd:COG3206 330 ASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
535-780 |
1.59e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 535 ELQMEKQKQEIAGKQKEIKDLQIAIDSLDskdpkhshmkaqksgkeQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDL 614
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQ-----------------AELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 615 EEQLTEGQIAANEALK------------------KDLEGVISGLQeYLGTIkgqATQAQNECRKLRDEKETLLQRLTEVE 676
Cdd:COG3883 78 EAEIEERREELGERARalyrsggsvsyldvllgsESFSDFLDRLS-ALSKI---ADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 677 QERDQLEIVAMDAENMRKelaELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQ 756
Cdd:COG3883 154 AKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260
....*....|....*....|....
gi 1622996215 757 SALQAELEKERQALKNALGKAQFS 780
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGA 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
446-837 |
1.66e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 446 MNLRGHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEqqilratEEFKQLEEAIQlkkiseagkdllykQLSGRLQLV- 524
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELN-------EAESDLEQDYQ--------------AASDHLNLVq 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 525 NKLRQ---------EALDLELQMEKQKQEIAGKQKEIKDLQI----AIDSLDSkdpkhshMKAQKSGKEQQLDIMNK--- 588
Cdd:PRK04863 342 TALRQqekieryqaDLEELEERLEEQNEVVEEADEQQEENEAraeaAEEEVDE-------LKSQLADYQQALDVQQTrai 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 589 QYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKK--DLEGVISGLQEylgtIKGQATQAQNECRKLRDE-- 664
Cdd:PRK04863 415 QYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEvs 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 665 KETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSA---YEAELEARLNLRDAEANQL 741
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKnldDEDELEQLQEELEARLESL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 742 KEELEKVtRLTQLEQSALQAELEKERQALknalgkaqfsEEKEQENSELHAKLKHLQD---DNNLLKQQLKDF-QNHLNH 817
Cdd:PRK04863 571 SESVSEA-RERRMALRQQLEQLQARIQRL----------AARAPAWLAAQDALARLREqsgEEFEDSQDVTEYmQQLLER 639
|
410 420
....*....|....*....|
gi 1622996215 818 VVDGLVRPEEVAARVDELRR 837
Cdd:PRK04863 640 ERELTVERDELAARKQALDE 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-751 |
2.48e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLlyKQLSGRLQLVNKLRQE----AL 532
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRiearLR 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 533 DLELQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIK 612
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDL----------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 613 DLEEQltegqiaanealKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVA---MDA 689
Cdd:TIGR02169 886 DLKKE------------RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeeLSL 953
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 690 ENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRL 751
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
580-953 |
2.59e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 580 EQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTE-GQIAANEALKKDLEGVISGLQEyLGTIKGQATQAQNEC 658
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAE-LEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 659 RKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTqgdlsAYEAELEARL--NLRDA 736
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-----ELRALLEERFaaALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 737 EANQLKEELEKvtrltqlEQSALQAELEKERQALKNALgkAQFSEEKEQENSELHAKLkhlqDDNNllkqqlkDFQNHLN 816
Cdd:COG4913 763 VERELRENLEE-------RIDALRARLNRAEEELERAM--RAFNREWPAETADLDADL----ESLP-------EYLALLD 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 817 HVV-DGLVRPEEvaarvdELRRKLKlgtgEMNIHSPSDVLGK---SLADLQKQFSEI---LARSKWERDEA---QVRERK 886
Cdd:COG4913 823 RLEeDGLPEYEE------RFKELLN----ENSIEFVADLLSKlrrAIREIKERIDPLndsLKRIPFGPGRYlrlEARPRP 892
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 887 LQEEmalqqeklatgqEEFRQACERALEARMNFDKRQHEARIQQMENEIHYL--QENLKSMEEIQGLTD 953
Cdd:COG4913 893 DPEV------------REFRQELRAVTSGASLFDEELSEARFAALKRLIERLrsEEEESDRRWRARVLD 949
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
459-761 |
2.60e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.20 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 459 EDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEaiqlkkiseagkdllykqlsgRLQLVNKL----------- 527
Cdd:COG3096 832 PDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKE---------------------QLQLLNKLlpqanlladet 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 ---RQEALDLEL-QMEKQKQEIAGKQKEIKDLQIAIDSLDSkDPkhshmkaqksgkeQQLDIMNKQYQQLESRLDEILSR 603
Cdd:COG3096 891 ladRLEELREELdAAQEAQAFIQQHGKALAQLEPLVAVLQS-DP-------------EQFEQLQADYLQAKEQQRRLKQQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 604 IAKETEEIK--------DLEEQLTEGQiAANEALKKDLEGV---ISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRL 672
Cdd:COG3096 957 IFALSEVVQrrphfsyeDAVGLLGENS-DLNEKLRARLEQAeeaRREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 673 TEVEQERDQLEIVAmDAEnmrkelAElESALQEQHEVNASLQQTQGDLSayeaELEARLNLRDAEANQLKEELEKVTR-L 751
Cdd:COG3096 1036 QELEQELEELGVQA-DAE------AE-ERARIRRDELHEELSQNRSRRS----QLEKQLTRCEAEMDSLQKRLRKAERdY 1103
|
330
....*....|
gi 1622996215 752 TQLEQSALQA 761
Cdd:COG3096 1104 KQEREQVVQA 1113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-978 |
2.74e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 259 DRQEAFERFSLEEVERLERDLEKKmIETEELKSKqtrfLEEIKNQDKLNKSLKEEAMLqkqscEELKSDLNTKNElplsw 338
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQK-----EAIERQLASLEE----- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 339 flagpfllilysslKLKQKTIELTRACQKQYELEQELAfyKIDAKFEPLNyyPSEYAEIdKAPDESPYIGKSRYKRNMFA 418
Cdd:TIGR02169 252 --------------ELEKLTEEISELEKRLEEIEQLLE--ELNKKIKDLG--EEEQLRV-KEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 419 TESYIIDSAQAVQIKKMEPDEQLRNdhmnlrgHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQL-E 497
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETrD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 498 EAIQLKKISEAGKDLLY---KQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSkdpKHSHMKA 574
Cdd:TIGR02169 386 ELKDYREKLEKLKREINelkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW---KLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 575 QKSGKEQQLDIMNKQYQQLESRLDEILSRIAkETEEIKDLEEQLTEGQIAANEALKKDLEGVIsGLQEYLGTIKGQ---- 650
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVH-GTVAQLGSVGERyata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 651 -------------------ATQAQNECRKLRDEKETLLQrLTEVEQERDQLEIVAMDA---------------------- 689
Cdd:TIGR02169 541 ievaagnrlnnvvveddavAKEAIELLKRRKAGRATFLP-LNKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyv 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 690 ----------ENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLrdAEANQLKEELEKVTRltqlEQSAL 759
Cdd:TIGR02169 620 fgdtlvvediEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEP--AELQRLRERLEGLKR----ELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 760 QAELEKERQALKnalgkaqfseEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLnhvvdglvrpEEVAARVDELRRKL 839
Cdd:TIGR02169 694 QSELRRIENRLD----------ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL----------EELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 840 KLGTGEMnihspsDVLGKSLADLQKQFSEI-LARSKWERDEAQVRERKLQEEMALQQEKLATgQEEFRQACERALEARmN 918
Cdd:TIGR02169 754 ENVKSEL------KELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRL-T 825
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 919 FDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKK 978
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
456-819 |
3.01e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 456 TQLEDKEKKISAAQTRLSELHDEIEKAEQQIL-----RATEEFKQLEEAI--QLKKISEAGKDLLY--KQLSGRLQLVNK 526
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELknQEKKLEEIQNQISQnnKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 527 LRQEALDLEL--------------QMEKQKQEIAGKQKEIKDLQIAIDSLDSKdpkHSHMKAQKSGKEQQLDIMNKQYQQ 592
Cdd:TIGR04523 347 LKKELTNSESensekqreleekqnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQIKKLQQEKEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 593 LESRLDEILSRIAKETEEIKDLEEqltegQIAANEALKKDLEGVISGLQEYLGTIKGqatqaqnECRKLRDEKETLLQRL 672
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTN-----QDSVKELIIKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKEL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 673 TEVEQERDQLEIVAMDAENMRKEL-AELESALQEQHEVNASLQQTQGDLSAYEAE------------LEARLNLRDAEAN 739
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLtKKISSLKEKIEKLESEKKEKESKISDLEDElnkddfelkkenLEKEIDEKNKEIE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 740 QLKEELEKVTRlTQLEQSALQAELEKERQALKNALgkaqfsEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVV 819
Cdd:TIGR04523 572 ELKQTQKSLKK-KQEEKQELIDQKEKEKKDLIKEI------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-621 |
3.02e-08 |
|
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: 56.09 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRqEALD 533
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEEL----------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1622996215 614 LEEQLTEG 621
Cdd:COG1579 164 EREELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1353-1608 |
4.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1353 HLKSKKREerwmRASKRQSEKEMEELHHNIDDLLQEkksLECEVEELHRTVQKRQQQKDFIDGNVESLMTEL-EIEKSLK 1431
Cdd:TIGR02168 233 RLEELREE----LEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1432 HH----EDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETA 1507
Cdd:TIGR02168 306 ILrerlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1508 VNLVKADQQLRSLQAD-------AKDLEQHKIKQEEILKEINKivAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNE 1580
Cdd:TIGR02168 386 SKVAQLELQIASLNNEierlearLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260
....*....|....*....|....*...
gi 1622996215 1581 DHHLQVLKESEVLLQAKRAELEKLKSQV 1608
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARL 491
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
662-985 |
4.81e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 662 RDEKETLLQRLTEVEQE----RDQLEIVAMDAENMRKELAEL---ESALQEQHE--------VNASLQQT------QGDL 720
Cdd:PRK04863 278 ANERRVHLEEALELRRElytsRRQLAAEQYRLVEMARELAELneaESDLEQDYQaasdhlnlVQTALRQQekieryQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 721 SAYEAELEARLNLRdAEANQLKEELEKVTRLTQLEQSALQAELEKERQAL-------------KNALGKAQ-------FS 780
Cdd:PRK04863 358 EELEERLEEQNEVV-EEADEQQEENEARAEAAEEEVDELKSQLADYQQALdvqqtraiqyqqaVQALERAKqlcglpdLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 781 EEKEQE-NSELHAKLKHLQDDNNLLKQQLKDFQNHLNH----------VVDGLVRPEE----------------VAARVD 833
Cdd:PRK04863 437 ADNAEDwLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlvrkIAGEVSRSEAwdvarellrrlreqrhLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 834 ELRRKLKLGTGEMNIHspsdvlgkslADLQKQFSEILARSKWERDEAQVRERkLQEEmalQQEKLATGQEEFRQACERAL 913
Cdd:PRK04863 517 QLRMRLSELEQRLRQQ----------QRAERLLAEFCKRLGKNLDDEDELEQ-LQEE---LEARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 914 EARMNFDkrQHEARIQQMEN---EIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLREL-EKKKKLEDAKSQ 985
Cdd:PRK04863 583 ALRQQLE--QLQARIQRLAArapAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELtVERDELAARKQA 656
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-803 |
5.85e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 243 HLRSLESLEGQPVTTQDRQEAFERFSLEEVERLERDLEKKMIETEELKSKQTRFLEEIKN-QDKLNKSL------KEEAM 315
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNlDDQLQKLLadlhkrEKELS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 316 LQKQSCEELkSDLNTKNELPLSwflagpfllilYSSLKLKQKTIELTR----------ACQKQyeLEQELAfyKIDAKFE 385
Cdd:pfam15921 395 LEKEQNKRL-WDRDTGNSITID-----------HLRRELDDRNMEVQRleallkamksECQGQ--MERQMA--AIQGKNE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 386 PLNYYPSEYAEIDkapdespyigksrykrnmfATESYIIDSAQAVQIKKM--EPDEQLRNDhmnlrghtpLDTQLEDKEK 463
Cdd:pfam15921 459 SLEKVSSLTAQLE-------------------STKEMLRKVVEELTAKKMtlESSERTVSD---------LTASLQEKER 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 464 KISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEA---IQLKKISEAGKD----LLYKQLSGRLQLVNKLRQEALDLEL 536
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqteCEALKLQMAEKDkvieILRQQIENMTQLVGQHGRTAGAMQV 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQKEIKDLQIAidsLDSKDPKHSHMKAQKSGKE-QQLDIMNKQYQQLES------RLDEILSRIAKETE 609
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKIL---KDKKDAKIRELEARVSDLElEKVKLVNAGSERLRAvkdikqERDQLLNEVKTSRN 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 610 EIKDLEEQLtegqiaanEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEketllqrLTEVEQERDQLEIVAMDA 689
Cdd:pfam15921 668 ELNSLSEDY--------EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT-------LKSMEGSDGHAMKVAMGM 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 690 ENM----RKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEkVTRltqleqsALQAELEK 765
Cdd:pfam15921 733 QKQitakRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE-VLR-------SQERRLKE 804
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1622996215 766 ERQALKNALGKA--QFSEEKE----QENSELHAKLKHLQDDNNL 803
Cdd:pfam15921 805 KVANMEVALDKAslQFAECQDiiqrQEQESVRLKLQHTLDVKEL 848
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
148-205 |
8.40e-08 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 50.22 E-value: 8.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 148 KLRELNLSYNKISKIEG--IENMCNLQKLNLAGNEIEHI-PVWLGKkLKSLRVLNLKGNKI 205
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLsPGAFSG-LPSLRYLDLSGNRL 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1339-1605 |
1.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1339 NLENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEK----KSLECEVEELHRTVQKRQQQKDFID 1414
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqiSALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1415 GNVESLMTELEIEKslkhhedivDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTES 1494
Cdd:TIGR02168 754 KELTELEAEIEELE---------ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1495 DAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINkivaakdSDFQCLSKKKEKLTEELQKLQKDIE 1574
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-------SELEALLNERASLEEALALLRSELE 897
|
250 260 270
....*....|....*....|....*....|.
gi 1622996215 1575 MAERNEDHHLQVLKESEVLLQAKRAELEKLK 1605
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1072 |
1.15e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 725 AELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQA---ELEKERQALKNALGKAQFSEEKEQEN-SELHAKLKHLQDD 800
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLrleELREELEELQEELKEAEEELEELTAElQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 801 NNLLKQQLKDFQNHLNhvvdglvrpeEVAARVDELRRKLKlgtgemnihspsdVLGKSLADLQKQFSEILArskwERDEA 880
Cdd:TIGR02168 276 VSELEEEIEELQKELY----------ALANEISRLEQQKQ-------------ILRERLANLERQLEELEA----QLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 881 QVRERKLQEEMALQQEKLATGQEEFrqACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEAD 960
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 961 EEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKklkkavatsdklatAELTIAKDQLKSLHGTVmkinQERAEELQE 1040
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--------------EELEEELEELQEELERL----EEALEELRE 468
|
330 340 350
....*....|....*....|....*....|...
gi 1622996215 1041 AERFSRKAAQAAR-DLTRAEAEIELLQNLLRQK 1072
Cdd:TIGR02168 469 ELEEAEQALDAAErELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
452-978 |
1.45e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 452 TPLDTQLEDKEKKISAAQTRLSELHDEIEKAEqqilratEEFKQLEEAI-QLKKISEagKDLLYKQLSGrlqLVNKLRQE 530
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVkELKELKE--KAEEYIKLSE---FYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 531 ALDLELQMEKQKQEIAGKQKEIKDLqiaidsldskdpkhshmkaqkSGKEQQLDIMNKQYQQLESRLdEILSRIAKETEE 610
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKEL---------------------EEKEERLEELKKKLKELEKRL-EELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 611 IKDLEEQLtegqiaanEALKKDLEGvisglqEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAE 690
Cdd:PRK03918 367 AKAKKEEL--------ERLKKRLTG------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 691 NMRKELAELESALQEQHEVN--ASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAElekerq 768
Cdd:PRK03918 433 KAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK------ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 769 ALKNALGKaqFSEEKEQENSELHAKLKHLQDDnnlLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLKlgtgemNI 848
Cdd:PRK03918 507 ELEEKLKK--YNLEELEKKAEEYEKLKEKLIK---LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA------EL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 849 HSPSDVLG-KSLADLQKQFSEI---------LARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMN 918
Cdd:PRK03918 576 LKELEELGfESVEELEERLKELepfyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 919 FDKRQHEA---RIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKK 978
Cdd:PRK03918 656 YSEEEYEElreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
126-181 |
1.74e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 49.45 E-value: 1.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 126 KLEVLNLSYNLIGKIEK--LDKLLKLRELNLSYNKISKIEG--IENMCNLQKLNLAGNEI 181
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
454-721 |
2.27e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAA----QTRLSELHDEIEKAEQQIlratEEFKQLEEAIQLkkisEAGKDLLYKQLSGrlqlvnkLRQ 529
Cdd:COG3206 162 LEQNLELRREEARKAleflEEQLPELRKELEEAEAAL----EEFRQKNGLVDL----SEEAKLLLQQLSE-------LES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 530 EALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmkaQKSGKEQQLDimnKQYQQLESRLDEILSRIAKETE 609
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPEL------------LQSPVIQQLR---AQLAELEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 610 EIKDLEEQLtegqiaanEALKKDLEgviSGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDA 689
Cdd:COG3206 292 DVIALRAQI--------AALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
250 260 270
....*....|....*....|....*....|..
gi 1622996215 690 ENMRKELAELesaLQEQHEVNASLQQTQGDLS 721
Cdd:COG3206 361 EVARELYESL---LQRLEEARLAEALTVGNVR 389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
494-1073 |
3.12e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 494 KQLEEAIQLKKISEAGKDL--LYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHS- 570
Cdd:PRK03918 149 KVVRQILGLDDYENAYKNLgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEk 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 571 ------HMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEgqiaaNEALKKDLEGVISgLQEYL 644
Cdd:PRK03918 229 evkeleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-----LKELKEKAEEYIK-LSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 645 GTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELES---ALQEQHEVNASLQQTQGDLS 721
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 722 AYEAE-LEARLNLRDAEANQLKEELEKVT-RLTQLEQSAlqAELEKERQALKNALGK-----AQFSEEKEQE-NSELHAK 793
Cdd:PRK03918 383 GLTPEkLEKELEELEKAKEEIEEEISKITaRIGELKKEI--KELKKAIEELKKAKGKcpvcgRELTEEHRKElLEEYTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 794 LKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAA--RVDELRRKLKLGTGEMNIHSPSDVlGKSLADLQKQFSEILA 871
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 872 RSKWERDEAQvRERKLQEEMALQQEKLATGQEEfRQACERALEARMNFDKRQHEARIQQME------NEIHYLQENLKSM 945
Cdd:PRK03918 540 EIKSLKKELE-KLEELKKKLAELEKKLDELEEE-LAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 946 EEIQGLTDLQLQEADEEKERILAQLRELEKK-KKLEDAKSQEQVFGLDKELKKLKKAVATsdklATAELTIAKDQLKSLH 1024
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAG----LRAELEELEKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622996215 1025 GTVMKINQERaEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKG 1073
Cdd:PRK03918 694 KTLEKLKEEL-EEREKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
490-1077 |
3.21e-07 |
|
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: 55.36 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 490 TEEFKQLEEAIQLKKISEAgkdlLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAgkqkEIKDLQIAIDSLDSKDPKH 569
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHA----YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA----VLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 570 SHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKKDLEGVISGLQEylgtIKG 649
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE----ISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 650 QATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEA 729
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 730 RLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAK-------------LKH 796
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgpltrrMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 797 LQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDElrRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWE 876
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ--SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 877 RDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNF-----DKRQHEARIQQMENEihYLQENLKSMEEIQGL 951
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltqeRVREHALSIRVLPKE--LLASRQLALQKMQSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 952 TDlQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLhgtvMKIN 1031
Cdd:TIGR00618 689 KE-QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR----TEAH 763
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1622996215 1032 QERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFR 1077
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
454-730 |
4.20e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQlkkiseagkdllykqlsgrlqlvnKLRQEALD 533
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID------------------------KLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAgkqKEIKDLQIAIDS-------LDSKDPKhshmkaqksgkeqqlDIMNKQyqqleSRLDEILSRIAK 606
Cdd:COG3883 77 AEAEIEERREELG---ERARALYRSGGSvsyldvlLGSESFS---------------DFLDRL-----SALSKIADADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 607 ETEEIKDLEEQLTEgQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVA 686
Cdd:COG3883 134 LLEELKADKAELEA-KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622996215 687 MDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEAR 730
Cdd:COG3883 213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-620 |
5.81e-07 |
|
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: 53.61 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEaiQLKKISEAGKDLLYK------------------ 515
Cdd:COG4942 53 LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--ELEAQKEELAELLRAlyrlgrqpplalllsped 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 516 --QLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSL-DSKDPKHSHMKAQKSGKEQQLDIMNKQYQQ 592
Cdd:COG4942 131 flDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlAELEEERAALEALKAERQKLLARLEKELAE 210
|
170 180
....*....|....*....|....*...
gi 1622996215 593 LESRLDEILSRIAKETEEIKDLEEQLTE 620
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
460-761 |
5.98e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 460 DKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQlkkiseagkdlLYKQLSGRLQL--VNKLRQEALDLELQ 537
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLS-----------ALNRLLPRLNLlaDETLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 538 M---EKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKsgkeQQLDIMNKQYQQLESRLDEILSRIAKETEEikDL 614
Cdd:PRK04863 903 LdeaEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDY----QQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DA 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 615 EEQLTEGQiAANEALKKDLEgvisGLQEYLGTIKGQATQAQNECRK-------LRDEKETLLQRLTEVEQERDQLEIVAm 687
Cdd:PRK04863 977 AEMLAKNS-DLNEKLRQRLE----QAEQERTRAREQLRQAQAQLAQynqvlasLKSSYDAKRQMLQELKQELQDLGVPA- 1050
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 688 dAENMRKELAELESALQEQhevnasLQQTQGDLSAyeaeLEARLNLRDAEANQLKEELEKVTR-LTQLEQSALQA 761
Cdd:PRK04863 1051 -DSGAEERARARRDELHAR------LSANRSRRNQ----LEKQLTFCEAEMDNLTKKLRKLERdYHEMREQVVNA 1114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-985 |
6.65e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEaiQLKKISEAGKDLL------YKQLSGRLQLVNKL 527
Cdd:TIGR04523 87 LNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEK--QKKENKKNIDKFLteikkkEKELEKLNNKYNDL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 RQEALDLELQMEKQKQEIAGKQKEIKD-------LQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEI 600
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKiknkllkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 601 LSRIAKETEEIKDLEEQLTE---------GQIAANEALKKDLEGVISGL------------QEYLGTIKGQATQAQNECR 659
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKikkqlsekqKELEQNNKKIKELEKQLNQLkseisdlnnqkeQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 660 KLRDEKETLLQRLTEVEQERDQLEIVAMDAEN----MRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRD 735
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 736 AEANQLKEELEKvtrltqLEQSALQAELEKERQALKNALGKAQFSEEKEQeNSELHAKLKHLQDDNNLLKQQLKDFQNHL 815
Cdd:TIGR04523 405 KLNQQKDEQIKK------LQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 816 NHVVDGLvrpeevaarvDELRRKLKLGTGEMnihspsdvlgKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQ 895
Cdd:TIGR04523 478 NKIKQNL----------EQKQKELKSKEKEL----------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 896 EKLATGQEEFrqaceraLEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEK 975
Cdd:TIGR04523 538 SKISDLEDEL-------NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
570
....*....|....*
gi 1622996215 976 K-----KKLEDAKSQ 985
Cdd:TIGR04523 611 KissleKELEKAKKE 625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-1146 |
7.03e-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: 54.30 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAE--QQILRATEEFKQLEEAIQlKKISEAGKDLLYKQLSGRLQLVNKLRQEALDL 534
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 535 ELQMEKQKQEIAGKQKEIKDL----QIAIDSldskdpKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEE 610
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLgeeeQLRVKE------KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 611 IKDLEEQLTEGQIaaneaLKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivamdaE 690
Cdd:TIGR02169 338 IEELEREIEEERK-----RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK------R 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 691 NMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELE-ARLNLRDAEAN--QLKEELEKVT---RLTQLEQSALQAELE 764
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKleQLAADLSKYEqelYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 765 KERQALKNALGKAQFSEEKEQENSelhAKLKHLQDDNNLLKQQLKDF---------------QNHLNHVVdglVRPEEVA 829
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGR---AVEEVLKASIQGVHGTVAQLgsvgeryataievaaGNRLNNVV---VEDDAVA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 830 ARVDELRRKLKLG-------TGEMNIHSPSDVLGKS--------LADLQKQFS--------------------------- 867
Cdd:TIGR02169 561 KEAIELLKRRKAGratflplNKMRDERRDLSILSEDgvigfavdLVEFDPKYEpafkyvfgdtlvvedieaarrlmgkyr 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 868 ------EILARS------KWERDEAQVRERKLQEEMALQQEKLatgqEEFRQACERALEARMNFDKRQHEARIQqmenei 935
Cdd:TIGR02169 641 mvtlegELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERL----EGLKRELSSLQSELRRIENRLDELSQE------ 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 936 hyLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTI 1015
Cdd:TIGR02169 711 --LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1016 AKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQfRLEMEKtgvgtgansqvlE 1095
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-IKSIEK------------E 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1622996215 1096 IEKLNETMERQRTEIARLQN-VLDLTG--SDNKGGFENVLEEIAELRREVSYQN 1146
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAaLRDLESrlGDLKKERDELEAQLRELERKIEELE 909
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
455-702 |
9.14e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 455 DTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQlkkiseagkdllykqlsgrlqlvnKLRQEALDL 534
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE------------------------ALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 535 ELQMEKQKQEIAGKQKEIKD----LQIAIDS-------LDSKDPKH--SHMKAQKSGKEQQLDIMNkQYQQLESRLDEIL 601
Cdd:COG3883 71 QAEIAEAEAEIEERREELGEraraLYRSGGSvsyldvlLGSESFSDflDRLSALSKIADADADLLE-ELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 602 SRIAKETEEIKDLEEQLtegqiaanEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQ 681
Cdd:COG3883 150 AELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250 260
....*....|....*....|.
gi 1622996215 682 LEIVAMDAENMRKELAELESA 702
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAA 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-1118 |
9.44e-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: 53.97 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 384 FEPLNYYPSEYAEIDKAPDESPYIGKSRYKRNMFATESYIIDsaqaVQIKKMEPDEQLRNDHMNLRGHT-PLDTQLEDKE 462
Cdd:pfam15921 48 FTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEEYSHQVKD----LQRRLNESNELHEKQKFYLRQSViDLQTKLQEMQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 463 KKISAA---QTRLSELHDEIEKAEQQILRATEEFKQLEEaiQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQME 539
Cdd:pfam15921 124 MERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKE--DMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 540 KQKQEIAGKQK-EIKDLQIAIDS-LDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQ-----LESRLDEILSRIAKETEEIK 612
Cdd:pfam15921 202 KKIYEHDSMSTmHFRSLGSAISKiLRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEIT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 613 DLEEQLTEGQIAAN------EALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRD---------EKETLL--QRLTEV 675
Cdd:pfam15921 282 GLTEKASSARSQANsiqsqlEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRmyedkieelEKQLVLanSELTEA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 676 EQERDQ-----------LEIVAMDAENMRKELA------------------ELESALQEQHEVNASLQQTQGDLSAYEAE 726
Cdd:pfam15921 362 RTERDQfsqesgnlddqLQKLLADLHKREKELSlekeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 727 LEARLNLRDAEANQLKEELEKVTRLT-QLEQSA-LQAELEKERQALKNALGKAQFS--------EEKEQENSELHAKLKH 796
Cdd:pfam15921 442 CQGQMERQMAAIQGKNESLEKVSSLTaQLESTKeMLRKVVEELTAKKMTLESSERTvsdltaslQEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 797 LQDDNNLLKQQLKDFQNHLNHVvdglvrpEEVAARVDELRRKLklgtgemnihSPSDVLGKSLADLQKQFSEILARSKWE 876
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHL-------RNVQTECEALKLQM----------AEKDKVIEILRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 877 RDEAQVRERKLQEEMALQQEKLatgqEEFRqacerALEARMNFDKRQHEARIQQMENE----IHYLQENLKSMEEIQGLT 952
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLEL----QEFK-----ILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQER 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 953 DLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQvfgldkelKKLKKAVATSDKLATAELTIAKDQLKSLHGT---VMK 1029
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM--------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghAMK 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1030 INQERAEELQeAERFSRKAAQAA-----RDLTRAEAEIELLqnllrqKGEQFRLEMEKTGVGTGANSQVLEIEKLNETME 1104
Cdd:pfam15921 728 VAMGMQKQIT-AKRGQIDALQSKiqfleEAMTNANKEKHFL------KEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
810
....*....|....
gi 1622996215 1105 RQRTEIARLQNVLD 1118
Cdd:pfam15921 801 RLKEKVANMEVALD 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
570-1574 |
9.87e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 570 SHMKAQKSGKEQQLDIMNKQYQQLESRLDEI------LSRIAKETEEIKDLEEQLTEGQIAAneaLKKDLEGvisgLQEY 643
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEDILNELerqlksLERQAEKAERYKELKAELRELELAL---LVLRLEE----LREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 644 LGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAE----NMRKELAELESALQEQHEVNASLQQTQGD 719
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 720 LSAYEAELEARLNLRDAEANQLKEELEKVTRLTQlEQSALQAELEKERQALKNALGKAQfsEEKEQENSELHAKLKHLQD 799
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELE--EQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 800 DNNLLkQQLKDFQNHLNHvvdglvRPEEVAARVDELRRKLklgtgemnihspsdvlgkSLADLQKQfSEILARSKWERDE 879
Cdd:TIGR02168 398 LNNEI-ERLEARLERLED------RRERLQQEIEELLKKL------------------EEAELKEL-QAELEELEEELEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 880 AQVRERKLQEEMALQQEKLATGQEEFRQAceRALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDL--QLQ 957
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAA--ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlsELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 958 EADEEKER-ILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKInqerAE 1036
Cdd:TIGR02168 530 SVDEGYEAaIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV----AK 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1037 ELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLEMEK----------TGVGTGANSQVL----EIEKLNET 1102
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggviTGGSAKTNSSILerrrEIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1103 MERQRTEIARLQNVLDltgsDNKGGFENVLEEIAELRREVSYQNDYISSMADPFKRRGywyfmppppsskvsshssqatk 1182
Cdd:TIGR02168 686 IEELEEKIAELEKALA----ELRKELEELEEELEQLRKELEELSRQISALRKDLARLE---------------------- 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1183 dsgvglkysastpvrkprpgqqdgkegsqpppasgywvySPIRSGLHKLFPSRDADSGGDSQEESELDDQEEppfvpppg 1262
Cdd:TIGR02168 740 ---------------------------------------AEVEQLEERIAQLSKELTELEAEIEELEERLEE-------- 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1263 ymmytvlpdgspvpqgmalyapppplpnnsrpltpgtvvygpppagapmvygppppnfsipfipmgvlhcNVPEHHNLEN 1342
Cdd:TIGR02168 773 ----------------------------------------------------------------------AEEELAEAEA 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1343 EVSRLEDIMQHLKSKKREERWMRASKRqseKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMT 1422
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1423 ELE-----IEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAE 1497
Cdd:TIGR02168 860 EIEeleelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1498 EL-ERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKI-------VAAKDSDFQCLSKKKEKLTEELQKL 1569
Cdd:TIGR02168 940 NLqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeYEELKERYDFLTAQKEDLTEAKETL 1019
|
....*
gi 1622996215 1570 QKDIE 1574
Cdd:TIGR02168 1020 EEAIE 1024
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
526-1145 |
1.17e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.64 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 526 KLRQEALDLELQMEkqkQEIAGKQKeikdLQIAIDSLDSKDPKhshMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIA 605
Cdd:pfam01576 100 KMQQHIQDLEEQLD---EEEAARQK----LQLEKVTTEAKIKK---LEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 606 KETEEIK--------------DLEEQLT--EGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLL 669
Cdd:pfam01576 170 EEEEKAKslsklknkheamisDLEERLKkeEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 670 QRLTEVEQERDQLEIVAMDAENMRKELAE-LESALQEQHEVNASLQQTQGDLSAYEAELEARLNL----------RDAEA 738
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEdLESERAARNKAEKQRRDLGEELEALKTELEDTLDTtaaqqelrskREQEV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 739 NQLKEELEKVTR--------LTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQD-------DNNL 803
Cdd:pfam01576 330 TELKKALEEETRsheaqlqeMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqdsehKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 804 LKQQLKDFQNHLNhvvDGLVRPEEVAARVDELRRKLKLGTGEMN-IHSPSDVLGKSLADLQKQF---SEILARSKWERDE 879
Cdd:pfam01576 410 LEGQLQELQARLS---ESERQRAELAEKLSKLQSELESVSSLLNeAEGKNIKLSKDVSSLESQLqdtQELLQEETRQKLN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 880 AQVRERKLQEEMALQQEKLATgQEEFRQACERALEArMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEA 959
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQLST-LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 960 DEEKERILAQLREL--EKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAeltiakdqlkslhgtvmkinqERAEE 1037
Cdd:pfam01576 565 AAAYDKLEKTKNRLqqELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA---------------------RYAEE 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1038 LQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLEME-----KTGVGtganSQVLEIEKLNETMERQ----RT 1108
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEdlvssKDDVG----KNVHELERSKRALEQQveemKT 699
|
650 660 670
....*....|....*....|....*....|....*..
gi 1622996215 1109 EIARLQNVLDLTgsdnkggfenvleEIAELRREVSYQ 1145
Cdd:pfam01576 700 QLEELEDELQAT-------------EDAKLRLEVNMQ 723
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
530-793 |
1.57e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.13 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 530 EALDLELQMEKQKQEIAGKQKEIKD-LQIAIDSLDskDPKHSHMKAQksgkeqqldimnkQYQQ----LESRLDEILSRI 604
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEaLQSALNWLE--ERKGSLERAK-------------QYQQvidnFPKLSAELRQQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 605 AKETEEIKDLEEQLTegqiaaNEALKKDLEGVISGLQEylgtIKGQATQAQNECRKLRDEKETLLQRLTEVeqerdqlei 684
Cdd:PRK10929 89 NNERDEPRSVPPNMS------TDALEQEILQVSSQLLE----KSRQAQQEQDRAREISDSLSQLPQQQTEA--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 685 vamdaenmRKELAELESALQEQHEVNASLQQTQgdlsayEAELEARLNLRDAEANQLkeELEKVTRLTQLEQSALQAELE 764
Cdd:PRK10929 150 --------RRQLNEIERRLQTLGTPNTPLAQAQ------LTALQAESAALKALVDEL--ELAQLSANNRQELARLRSELA 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622996215 765 KER--------QALKNALgKAQFSEEKEQ--ENSELHAK 793
Cdd:PRK10929 214 KKRsqqldaylQALRNQL-NSQRQREAERalESTELLAE 251
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
534-1134 |
1.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAGKQKEIKDLQIAiDSLDSKDPKHSHMKAQKSGKEQQLDimNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEKDIIDEDID-GNHEGKAEAKAHVGQDEGLKPSYKD--FDFDAKEDNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 614 LEEQLTEGQIAANEALKKDLEgvISGLQEylgTIKGQATQAQNECRKLRDEKETLLQRLTEveqERDQLEIVAMDAENMR 693
Cdd:PTZ00121 1106 TETGKAEEARKAEEAKKKAED--ARKAEE---ARKAEDARKAEEARKAEDAKRVEIARKAE---DARKAEEARKAEDAKK 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 694 KELAELESALQEQHEVNASLQQTQGDlSAYEAELEARL-NLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKN 772
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAE-AARKAEEERKAeEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 773 --ALGKAQFSEEKEQENSELHAKLKHLQDDNNLLK-QQLKDFQNhlNHVVDGLVRPEEVAARVDELRRKLKlgtgemNIH 849
Cdd:PTZ00121 1257 feEARMAHFARRQAAIKAEEARKADELKKAEEKKKaDEAKKAEE--KKKADEAKKKAEEAKKADEAKKKAE------EAK 1328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 850 SPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQ------EEMALQQEKLATGQEEFRQACE---RALEARMNFD 920
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkkEEAKKKADAAKKKAEEKKKADEakkKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 921 KRQHEARIQQMENEIHYLQENLKSMEEIQGLTDlQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKK 1000
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1001 A--VATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERfSRKAAQAARDLTRAEAEiELlqnllrQKGEQFRL 1078
Cdd:PTZ00121 1488 AkkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEEKKKAD-EL------KKAEELKK 1559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 1079 EMEKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDLTGSDNKGGFENVLEE 1134
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
458-1024 |
1.87e-06 |
|
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: 52.92 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 458 LEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEfKQLEEAIQLKKISEAGKDLLYKQLSGRL-QLVNKLRQEALDLEL 536
Cdd:pfam12128 366 LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLA-KIREARDRQLAVAEDDLQALESELREQLeAGKLEFNEEEYRLKS 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQ---KEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:pfam12128 445 RLGELKLRLNQATatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 614 LEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDaENMR 693
Cdd:pfam12128 525 LELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE-EELR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 694 KELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNA 773
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 774 LgkAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVD---GLVRPEEVAARVDELRRKLKLGTGEMNIHS 850
Cdd:pfam12128 684 L--NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDaqlALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 851 PSDVLGKSLADLQKQFSEILAR-SKWERDEAQVRE--RKLQEEMALQQEKLATGQEEFRQACER------ALEARMNFDK 921
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKiERIAVRRQEVLRyfDWYQETWLQRRPRLATQLSNIERAISElqqqlaRLIADTKLRR 841
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 922 RQHEARIQQMENEIHYLQENLKSME-EIQGLTDLQL----QEADEEKERILAQLRELEKKKK--LEDAKSQEQVFGLDKE 994
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSENLRGLRcEMSKLATLKEdansEQAQGSIGERLAQLEDLKLKRDylSESVKKYVEHFKNVIA 921
|
570 580 590
....*....|....*....|....*....|
gi 1622996215 995 LKKLKKAVATSDKLATAELTIAKDQLKSLH 1024
Cdd:pfam12128 922 DHSGSGLAETWESLREEDHYQNDKGIRLLD 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1365-1578 |
2.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1365 RASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTEL-EIEKSLKHHEDIVDEieci 1443
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaELRAELEAQKEELAE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1444 ektLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQT-ESDAEELERRAQETAVNLVKADQQLRSLQA 1522
Cdd:COG4942 109 ---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 1523 DAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAER 1578
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
435-792 |
2.37e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 435 MEPDEQLRNDHMNLrghtpLDTQLEDKEKkISAAQTRLSELHDEIEKAEQQILRATEefkQLEEAIQLKKISEAGKDLLY 514
Cdd:COG3096 325 LEQDYQAASDHLNL-----VQTALRQQEK-IERYQEDLEELTERLEEQEEVVEEAAE---QLAEAEARLEAAEEEVDSLK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 515 KQLSGRlqlvnklrQEALD------LELQMEKQKQEIAGKQKEIKDLqiaidSLDSKDPKHSHMKAQKS-------GKEQ 581
Cdd:COG3096 396 SQLADY--------QQALDvqqtraIQYQQAVQALEKARALCGLPDL-----TPENAEDYLAAFRAKEQqateevlELEQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 582 QLDIMNKQYQQLESRLdEILSRIAKETEEikdleeqlTEGQIAANEALK-----KDLEGVISGLQEYLGTIKgQATQAQN 656
Cdd:COG3096 463 KLSVADAARRQFEKAY-ELVCKIAGEVER--------SQAWQTARELLRryrsqQALAQRLQQLRAQLAELE-QRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 657 ECRKLRDEketLLQRLTEVEQERDQLEIVAMDAEnmrKELAELESALQEQHEVNASLQQTQGDLSAYEAELEAR----LN 732
Cdd:COG3096 533 NAERLLEE---FCQRIGQQLDAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLA 606
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 733 LRDAeANQLKEEL-EKVTRLTQLeQSALQAELEKERQALKNALGKAQFSEEKEQENSELHA 792
Cdd:COG3096 607 AQDA-LERLREQSgEALADSQEV-TAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-752 |
2.77e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 501 QLKKISEAGKDL--LYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLdskdpkhshmkaqksg 578
Cdd:COG4942 18 QADAAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 579 kEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEalkkDLEGVISGLQeYLGTIkgqATQAQNEC 658
Cdd:COG4942 82 -EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE----DFLDAVRRLQ-YLKYL---APARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 659 RKLRDEKETLLQRLTEVEQERDQLEIVamdAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEA 738
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....
gi 1622996215 739 NQLKEELEKVTRLT 752
Cdd:COG4942 230 ARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1338-1578 |
2.88e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1338 HNLENEVSRLED--IMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDG 1415
Cdd:TIGR02169 775 HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1416 NVESLMTEL-EIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTES 1494
Cdd:TIGR02169 855 EIENLNGKKeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1495 DAEELERRAQETAVNLVKAD---QQLRSLQADAKDLEQHKIKQEEILKEINKivaakdsDFQCLSKKKEKLTEELQKLQK 1571
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEdvqAELQRVEEEIRALEPVNMLAIQEYEEVLK-------RLDELKEKRAKLEEERKAILE 1007
|
....*..
gi 1622996215 1572 DIEMAER 1578
Cdd:TIGR02169 1008 RIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1340-1608 |
3.49e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKREERWMR-------ASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDF 1412
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRdeadevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1413 IDGNVESLMTELEIEKSlkHHEDIVDEIEciekTLLKRRSELREAdrlLAEAESELSCTKEKTKNAVEKFTDAKRSLLQT 1492
Cdd:PRK02224 291 LEEERDDLLAEAGLDDA--DAEAVEARRE----ELEDRDEELRDR---LEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1493 ESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKD 1572
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1573 IEMAER--------------NEDHHLQVLKESEVLLQAKRAELEKLKSQV 1608
Cdd:PRK02224 442 VEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
126-167 |
5.67e-06 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 44.54 E-value: 5.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622996215 126 KLEVLNLSYNLIGKIEKLDKLLKLRELNLSYN-KISKIEGIEN 167
Cdd:pfam12799 2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1413-1608 |
7.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1413 IDGNVESLmtELEIEKSLKHHEdIVDEIECIEKTLLKRRselreadrlLAEAESELSCTKEKTKNAVEKFTDAKRSLLQT 1492
Cdd:TIGR02168 198 LERQLKSL--ERQAEKAERYKE-LKAELRELELALLVLR---------LEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1493 ESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKD 1572
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622996215 1573 IEMAERN-------EDHHLQVLKESEVLLQAKRAELEKLKSQV 1608
Cdd:TIGR02168 346 LEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKV 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-748 |
7.19e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 591 QQLESRLDEILSRIAKETEEIKDLEEQLT--EGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKE-- 666
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 667 TLLQRLTEVEQERDQLEivamdaENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELE 746
Cdd:COG1579 93 ALQKEIESLKRRISDLE------DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
..
gi 1622996215 747 KV 748
Cdd:COG1579 167 EL 168
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1346-1610 |
9.23e-06 |
|
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: 50.82 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1346 RLEDIMQHLKSKKREERWMRAskrQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTELE 1425
Cdd:TIGR00606 302 QLNDLYHNHQRTVREKERELV---DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1426 IEkSLKHHEDIVDEIECIEKTLLKRRS-ELREADRLLAEAESELSCTKEktknAVEKFTDAKRSLLQTESDAEELERRAQ 1504
Cdd:TIGR00606 379 LD-GFERGPFSERQIKNFHTLVIERQEdEAKTAAQLCADLQSKERLKQE----QADEIRDEKKGLGRTIELKKEILEKKQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1505 ETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNedHHL 1584
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN--HHT 531
|
250 260
....*....|....*....|....*.
gi 1622996215 1585 QVLKESEVLLQAKRAELEKLKSQVWQ 1610
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSR 557
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
458-982 |
1.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 458 LEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLE--EAIQLKKISEAGKDllYKQLSGRLQLVNKLRQEALDLE 535
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEksHSITLKEIERLSIE--YNNAMDDYNNLKSALNELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 536 LQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLE 615
Cdd:PRK01156 249 DMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAII 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 616 EQLTEGQIAANEALKK-----DLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQerdQLEIVAMDAE 690
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKksrydDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE---ILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 691 NMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAE------ANQLKEE-LEKVTRLTQLEQSALQAEL 763
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEkSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 764 EK-ERQALKNALGKAQFSEEKEQENSElhaKLKHLQDDNNLLKQ---QLKDFQNHLNHVVDGLVRPEEVAAR-----VDE 834
Cdd:PRK01156 486 REiEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESaraDLEDIKIKINELKDKHDKYEEIKNRykslkLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 835 LRRKLKLGTGEM---------NIHSPSDVLGKSLADLQKQFSEILAR---------SKWERDEAQVR----ERKLQEEMA 892
Cdd:PRK01156 563 LDSKRTSWLNALavislidieTNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidKSIREIENEANnlnnKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 893 LQQEKLATGQEEFRQacERALEARMNFDKRQHEARIQQMENEIHY----LQENLKSMEEIQGLTDLQLQEADEEKERILA 968
Cdd:PRK01156 643 ILIEKLRGKIDNYKK--QIAEIDSIIPDLKEITSRINDIEDNLKKsrkaLDDAKANRARLESTIEILRTRINELSDRIND 720
|
570
....*....|....
gi 1622996215 969 QLRELEKKKKLEDA 982
Cdd:PRK01156 721 INETLESMKKIKKA 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1339-1607 |
1.02e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1339 NLENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKrqqqkdfidgnve 1418
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1419 slmtELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESElsctKEKTKNAVEKFTDAKRSLLQTESDAEE 1498
Cdd:PRK03918 292 ----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1499 LER-RAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKdSDFQCLSKKKEKLTEELQKLQKDIEMAE 1577
Cdd:PRK03918 364 YEEaKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI-GELKKEIKELKKAIEELKKAKGKCPVCG 442
|
250 260 270
....*....|....*....|....*....|..
gi 1622996215 1578 R--NEDHHLQVLKESEVLLQAKRAELEKLKSQ 1607
Cdd:PRK03918 443 RelTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
148-179 |
1.18e-05 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 43.77 E-value: 1.18e-05
10 20 30
....*....|....*....|....*....|..
gi 1622996215 148 KLRELNLSYNKISKIEGIENMCNLQKLNLAGN 179
Cdd:pfam12799 2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGN 33
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
458-987 |
1.28e-05 |
|
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: 50.35 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 458 LEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQ 537
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 538 MEKQKQEIAGKQKE---------IKDLQIAIDSLDS--------KDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEi 600
Cdd:TIGR00618 382 HTLQQQKTTLTQKLqslckeldiLQREQATIDTRTSafrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 601 LSRIAKETEEIKDLEEQLTegQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERD 680
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKE--QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 681 QLEIVamdAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQ 760
Cdd:TIGR00618 539 QLETS---EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 761 AELEKERQALKN---ALGKAQFSEEKEQENSELHAKLKHL------------QDDNNLLKQQLKDFQNHLNHVVDGLVRP 825
Cdd:TIGR00618 616 ALLRKLQPEQDLqdvRLHLQQCSQELALKLTALHALQLTLtqervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 826 EEVAARVDELRRKL--KLGTGEMNIHSPSDVLGKSLADLQKQfsEILARSKWERDEAQVRERKLQEEMALQQEKLATGQE 903
Cdd:TIGR00618 696 KEMLAQCQTLLRELetHIEEYDREFNEIENASSSLGSDLAAR--EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 904 EFRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQeadEEKERILAQLRELEKK------- 976
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV---QEEEQFLSRLEEKSATlgeithq 850
|
570
....*....|..
gi 1622996215 977 -KKLEDAKSQEQ 987
Cdd:TIGR00618 851 lLKYEECSKQLA 862
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
579-976 |
1.32e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 579 KEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQL---TEGQIAANE------ALKKDLEGVISGLQEYLGTIKG 649
Cdd:pfam01576 10 KEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEmrarlaARKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 650 QATQAQNECRKLRDEKETLLQRLTEVEQERD--QLEIVAMDAE-----------------------NMRKELAELESALQ 704
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQklQLEKVTTEAKikkleedillledqnsklskerkLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 705 EQHEVNASLQQTQGDLSAYEAELEARLNlrdaEANQLKEELEKVTRLTQLEQSALQ---AELEKERQALKNALGKaqfse 781
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQeqiAELQAQIAELRAQLAK----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 782 eKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKL--KLGTGEMNIHSPSDVLGKSL 859
Cdd:pfam01576 241 -KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLgeELEALKTELEDTLDTTAAQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 860 ADLQKQFSEILARSKWERDEAQVRERKLQEemalQQEKLATGQEEFRQACERALEARMNFDKRQheariQQMENEIHYLQ 939
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQE----MRQKHTQALEELTEQLEQAKRNKANLEKAK-----QALESENAELQ 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 1622996215 940 ENLKSMEEIQgltdlqlQEADEEKERILAQLRELEKK 976
Cdd:pfam01576 391 AELRTLQQAK-------QDSEHKRKKLEGQLQELQAR 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1347-1604 |
1.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1347 LEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDfidgNVESLMTELE- 1425
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE----NVKSELKELEa 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1426 ------------------IEKSLKHH--EDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDA 1485
Cdd:TIGR02169 766 rieeleedlhkleealndLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1486 K--RSLLQTESDA-----EELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKK 1558
Cdd:TIGR02169 846 KeqIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622996215 1559 KEKLTEELQKLQKDI--EMAERNEDHHLQVLKESevlLQAKRAELEKL 1604
Cdd:TIGR02169 926 LEALEEELSEIEDPKgeDEEIPEEELSLEDVQAE---LQRVEEEIRAL 970
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
591-778 |
1.45e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 591 QQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKK----DLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKE 666
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 667 TLLQRLTEVEQERDQL----EIVAMDAE--NMRKELAELESALQEQHEvnaslqqtqgDLSAYEAELEARLNLRDAEANQ 740
Cdd:COG3206 244 ALRAQLGSGPDALPELlqspVIQQLRAQlaELEAELAELSARYTPNHP----------DVIALRAQIAALRAQLQQEAQR 313
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622996215 741 LKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQ 778
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
580-986 |
1.54e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 580 EQQLDIMNKQYQQLESRLDE--ILSRIAKETEEIKDLEEQLTEGQIAANEALKKDLEGV-----ISGLQEYLGTIKgQAT 652
Cdd:COG3096 285 ERALELRRELFGARRQLAEEqyRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALrqqekIERYQEDLEELT-ERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 653 QAQNECRKLRDEKETLLQ-RLTEVEQERDQLeivamdaenmRKELAELESALQEQHEVNASLQQTQGDLSAYEAELE-AR 730
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEaRLEAAEEEVDSL----------KSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGlPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 731 LNLRDAEANQ--LKEELEKVT-RLTQLEQ-----SALQAELEKERQALKNALGKAQFSE--EKEQENSELHAKLKHLQDD 800
Cdd:COG3096 434 LTPENAEDYLaaFRAKEQQATeEVLELEQklsvaDAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 801 NNLLKQQLKdfqnhlnhvvdglvrpeevaarvdELRRKLklgtgemnihspsdvlgKSLADLQKQFSEILARSKWERDEA 880
Cdd:COG3096 514 LQQLRAQLA------------------------ELEQRL-----------------RQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 881 QVRERKLQEemalQQEKLATGQEEFRQACERALEARMNFDkrQHEARIQQMEN---EIHYLQENLKSMEEIQGLTDLQLQ 957
Cdd:COG3096 553 EELEELLAE----LEAQLEELEEQAAEAVEQRSELRQQLE--QLRARIKELAArapAWLAAQDALERLREQSGEALADSQ 626
|
410 420
....*....|....*....|....*....
gi 1622996215 958 EADEEKERILAQLRELEKKKKLEDAKSQE 986
Cdd:COG3096 627 EVTAAMQQLLEREREATVERDELAARKQA 655
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1462-1607 |
1.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1462 AEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKE- 1540
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1541 -------------INKIVAAKD-SDF-------QCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRA 1599
Cdd:COG3883 92 aralyrsggsvsyLDVLLGSESfSDFldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
....*...
gi 1622996215 1600 ELEKLKSQ 1607
Cdd:COG3883 172 ELEAQQAE 179
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
454-988 |
1.59e-05 |
|
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: 49.82 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRAT----EEFKQLEeaiqlkkiseagkdlLYKQLSGRLQlvNKlrq 529
Cdd:pfam10174 231 LQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTedreEEIKQME---------------VYKSHSKFMK--NK--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 530 ealdlelqMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSH----MKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIA 605
Cdd:pfam10174 291 --------IDQLKQELSKKESELLALQTKLETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 606 KETEEIKDLEEQltEGQIAANEALKKD-----------LEGVISGLQEYLGTIKGQATQAQNECRKLRDEK---ETLLQR 671
Cdd:pfam10174 363 KKTKQLQDLTEE--KSTLAGEIRDLKDmldvkerkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntDTALTT 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 672 LTEVEQERDQLeIVAMDAENMRKE---LAELESALQEQHEVNASLQQTQGDLSAYEAELearLNLRDAEANQLKEELEKV 748
Cdd:pfam10174 441 LEEALSEKERI-IERLKEQREREDrerLEELESLKKENKDLKEKVSALQPELTEKESSL---IDLKEHASSLASSGLKKD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 749 TRLTQLEqsalqAELEKERQ---ALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRP 825
Cdd:pfam10174 517 SKLKSLE-----IAVEQKKEecsKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 826 EEvaarvDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQ-EKLATGQEE 904
Cdd:pfam10174 592 EN-----EKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQlEELMGALEK 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 905 FRQACErALEARMNFDKRQHEARIQQMENeihYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKledaKS 984
Cdd:pfam10174 667 TRQELD-ATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKK----KT 738
|
....
gi 1622996215 985 QEQV 988
Cdd:pfam10174 739 QEEV 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
456-969 |
2.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 456 TQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQlkkisEAG---KDLLYKQLSGRLQLVNKLRQEAL 532
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR-----GNGgdrLEQLEREIERLERELEERERRRA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 533 DLELQMEKQKQEIAGKQKEIKDLQIAIdsldskdpkhshmKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIK 612
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEA-------------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 613 DLEEQ---LTEGQIAANEALKKDLEGVISGLQ---EYLgtikgqatQAQNECRKLRDEKETLL--QRLT---EVEQERDQ 681
Cdd:COG4913 430 SLERRksnIPARLLALRDALAEALGLDEAELPfvgELI--------EVRPEEERWRGAIERVLggFALTllvPPEHYAAA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 682 LEIVamDAENMRKEL------AELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLR-------DAEanQLKEELEKV 748
Cdd:COG4913 502 LRWV--NRLHLRGRLvyervrTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRfdyvcvdSPE--ELRRHPRAI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 749 TRLTQLEQS-----------------------ALQAELEKERQALKNALGKAQfseekeQENSELHAKLKHLQDdnnlLK 805
Cdd:COG4913 578 TRAGQVKGNgtrhekddrrrirsryvlgfdnrAKLAALEAELAELEEELAEAE------ERLEALEAELDALQE----RR 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 806 QQLKDFQNHLNHVVDglvrPEEVAARVDELRRKLKlgtgemNIHSPSDVLgKSLADLQKQFSEILARSKWERDEAQVRER 885
Cdd:COG4913 648 EALQRLAEYSWDEID----VASAEREIAELEAELE------RLDASSDDL-AALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 886 KLQEEMALQQEKLATGQEEFRQACERA-LEARMNFDKRQHEARIQQMENEIhylQENLKsmEEIQGLTDlQLQEADEEKE 964
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDAVEREL---RENLE--ERIDALRA-RLNRAEEELE 790
|
....*
gi 1622996215 965 RILAQ 969
Cdd:COG4913 791 RAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
588-1142 |
2.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 588 KQYQQLESRLDEILSRIAKETEEIKDLEEQLTEgqiaaneaLKKDLEGVISGLQEyLGTIKGQATQAQNECRKLRDEKET 667
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPE--------LREELEKLEKEVKE-LEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 668 LLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEK 747
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 748 VTRLTQLEQsaLQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNnlLKQQLKDFQNHLNHVVDGLVRPEE 827
Cdd:PRK03918 337 EERLEELKK--KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 828 VAARVDELRRKLKLGTGEM-NIHSPSDVLGKSL-----ADLQKQFSEILARSKWERDEAQVRERKLQE-----EMALQQE 896
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELkKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKLRKelrelEKVLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 897 KLATGQEEFRQACERALEARMNFDKRQHEARIQQMENeihyLQENLKSME-EIQGLTD--LQLQEADEEKERILAQLREL 973
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK----LKEKLIKLKgEIKSLKKelEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 974 EKKKKLEDAKSQEQVFGLDKELKKLKKAVAT------SDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRK 1047
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1048 AAQAARDLTRAEAEiELLQNLLRQKGEQFRLEMEKtgvgTGANSQVLEIEKLNETMERQRTEIARLQNVLDLtgsdnkgg 1127
Cdd:PRK03918 649 LEELEKKYSEEEYE-ELREEYLELSRELAGLRAEL----EELEKRREEIKKTLEKLKEELEEREKAKKELEK-------- 715
|
570
....*....|....*
gi 1622996215 1128 FENVLEEIAELRREV 1142
Cdd:PRK03918 716 LEKALERVEELREKV 730
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
474-1119 |
2.53e-05 |
|
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: 49.20 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 474 ELHDEIEKAEQQI-------------LRATEEFKQLEEAIQLKKISEAGK-DLLYKQLSGRLQLVNKLRQEALDLELQME 539
Cdd:pfam02463 174 ALKKLIEETENLAeliidleelklqeLKLKEQAKKALEYYQLKEKLELEEeYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 540 KQKQEIAGKQKEIKDLQIAIDSLDSKdpKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLT 619
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEK--EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 620 EGQIAANEALKKDLEGVISglQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERD-QLEIVAMDAENM------ 692
Cdd:pfam02463 332 KEKEEIEELEKELKELEIK--REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAkLKEEELELKSEEekeaql 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 693 -----RKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQ-SALQAELEKE 766
Cdd:pfam02463 410 llelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQlVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 767 RQALKNALGKAQFSEEKEQENS-----------------------------ELHAKLKHLQDDNNLLKQQLKDFQnHLNH 817
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVllalikdgvggriisahgrlgdlgvavenYKVAISTAVIVEVSATADEVEERQ-KLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 818 VVDGLVRPEEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKW------ERDEAQVRERKLQEEM 891
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEgilkdtELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 892 ALQQEKLATGQEEFRQACERALEARMNFDKRQhEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLR 971
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQE-LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 972 ELEKKKKLEDAKSQEQVFGLDKELKK--LKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERfSRKAA 1049
Cdd:pfam02463 728 QEAQDKINEELKLLKQKIDEEEEEEEksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-ELRAL 806
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1050 QAARDLTRAEAEIELLQNLLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDL 1119
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
686-912 |
3.09e-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: 48.22 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 686 AMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTR---LTQLEQSALQAE 762
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 763 LEKERQALKNALGKAQFSEEKEQENSELHAK--------LKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDE 834
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 835 LRRKLKlgtgemnihspsdVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERA 912
Cdd:COG4942 179 LLAELE-------------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
534-767 |
3.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDpkhshmkaQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSE--------EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 614 LEEQLTE-GQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNecrkLRDEKETLLQRL-TEVEQERDQLEIvamDAEN 691
Cdd:COG3206 252 GPDALPElLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA----LRAQIAALRAQLqQEAQRILASLEA---ELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 692 MRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEArlnlrdaeANQLKEELekvtrLTQLEQSALQAELEKER 767
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV--------ARELYESL-----LQRLEEARLAEALTVGN 387
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
76-205 |
6.02e-05 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 47.48 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 76 SHAGVRYITEALikkltkQDNLALiKSLNLSLSKDGGKKFKYI-ENLEKCVKLEVLNLSYNLIGK------IEKLDKLLK 148
Cdd:COG5238 277 GAEGAIALAKAL------QGNTTL-TSLDLSVNRIGDEGAIALaEGLQGNKTLHTLNLAYNGIGAqgaialAKALQENTT 349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 149 LRELNLSYNKISK------IEGIENMCNLQKLNLAGNEI-EHIPVWLGKKLK--SLRVLNLKGNKI 205
Cdd:COG5238 350 LHSLDLSDNQIGDegaialAKYLEGNTTLRELNLGKNNIgKQGAEALIDALQtnRLHTLILDGNLI 415
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
76-181 |
6.86e-05 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 46.96 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 76 SHAGVRYITEALikklTKQDNLALIKSLNLSLSKDGGKKFKyiENLEKCVKLEVLNLSYNLIGK--IEKLDKLLK----- 148
Cdd:cd00116 178 GDAGIRALAEGL----KANCNLEVLDLNNNGLTDEGASALA--ETLASLKSLEVLNLGDNNLTDagAAALASALLspnis 251
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622996215 149 LRELNLSYNKI------SKIEGIENMCNLQKLNLAGNEI 181
Cdd:cd00116 252 LLTLSLSCNDItddgakDLAEVLAEKESLLELDLRGNKF 290
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
170-220 |
7.17e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.13 E-value: 7.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 170 NLQKLNLAGNEIEHIPVWLGKKLKSLRVLNLKGNKISSL--QDISKLKPLQDL 220
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLspGAFSGLPSLRYL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1336-1601 |
7.46e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1336 EHHNLENEVSRLEdimqhLKSKKREERWMRASKRQSE--KEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFI 1413
Cdd:TIGR02168 727 QISALRKDLARLE-----AEVEQLEERIAQLSKELTEleAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1414 DGNVESLMTEL------------EIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEK 1481
Cdd:TIGR02168 802 REALDELRAELtllneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1482 FTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQadaKDLEQHKIKQEEILKEINKIvaakdsdfqclskkKEK 1561
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELR---EKLAQLELRLEGLEVRIDNL--------------QER 944
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622996215 1562 LTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAEL 1601
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
439-774 |
7.84e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 439 EQLRNDHMNLRGHTPLDTQLEDKEKKISAAQTRLSEL---HDEIEKAEQQILRATEEFKQLEEAIQlkkiseagkDLLYK 515
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELE---------ELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 516 QLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDI---------- 585
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglg 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 586 ---------------------------MNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALK--KDLEGV 636
Cdd:COG4717 266 gsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEelLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 637 ISGLQEYLGTIKGQATQAQNECrkLRDEKETLLQR--LTEVEQERDQLEIVAmDAENMRKELAELESALQEQHEVNASL- 713
Cdd:COG4717 346 IEELQELLREAEELEEELQLEE--LEQEIAALLAEagVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELl 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 714 -QQTQGDLSAYEAELEARLNLRDAEANQLKEELEKV-TRLTQLEQSALQAELEKERQALKNAL 774
Cdd:COG4717 423 eALDEEELEEELEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAEL 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
502-976 |
8.45e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 502 LKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDS-----------LDSKDPKHS 570
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEkenkmkdltflLEESRDKAN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 571 HMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEE----------QLTEGQIAANEALKKDLEGVISGL 640
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 641 QEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEV---NASLQQTQ 717
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 718 GDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQL---EQSALQAELEKERqaLKNALGKAQFS----EEKE--QENS 788
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHylkEVEDLKTELEKEK--LKNIELTAHCDklllENKEltQEAS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 789 ELHAKLKHLQDD-NNLLKQ------QLKDFQNHLNHVVDGL--VRpEEVAARVDELrrKLKLGTGEMNIHSPSDVLGKSL 859
Cdd:pfam05483 510 DMTLELKKHQEDiINCKKQeermlkQIENLEEKEMNLRDELesVR-EEFIQKGDEV--KCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 860 ADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEefrqacERALEARMNFDKRQHEARIQQMENEIHYLQ 939
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ------LNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622996215 940 ENLksmeEIQGLTDLQLQEADEEKERILAQLRELEKK 976
Cdd:pfam05483 661 KEI----EDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1373-1589 |
9.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1373 KEMEELHHNIDDLLQEKKSLEcEVEELHRTVQKRQQQKDFIDgnveSLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRS 1452
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELE----YLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1453 ELREADRLLAEAESEL-SCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQEtavnlvkADQQLRSLQ----ADAKDL 1527
Cdd:COG4913 310 ELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR-------LEALLAALGlplpASAEEF 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 1528 EQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNE---DHHLQVLKE 1589
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRD 447
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
457-980 |
1.03e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEA-------IQLKKISEAGKDLLYKQLSGRLQLVNK-LR 528
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKkdhltkeLEDIKMSLQRSMSTQKALEEDLQIATKtIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 529 QEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKdPKHSHMKAQKSgkEQQLDIMNKQYQQLESRLDEILSRIAKET 608
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL-LRTEQQRLEKN--EDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 609 EEIKDLEEQLTEGQ--IAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVA 686
Cdd:pfam05483 405 VELEELKKILAEDEklLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 687 MD----AENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARL----NLRDAEANqLKEELEKVtrltqleqsa 758
Cdd:pfam05483 485 LKnielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLkqieNLEEKEMN-LRDELESV---------- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 759 lQAELEKERQALKNALGKAQFSEEK-EQENSELHAKLKHLQDDNNLLKQQLKDFQNHLnhvvdglvrpEEVAARVDELRR 837
Cdd:pfam05483 554 -REEFIQKGDEVKCKLDKSEENARSiEYEVLKKEKQMKILENKCNNLKKQIENKNKNI----------EELHQENKALKK 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 838 KLKLGTGEMNIHS-PSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQ---EKLATGQEEFRQACERAL 913
Cdd:pfam05483 623 KGSAENKQLNAYEiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKaiaDEAVKLQKEIDKRCQHKI 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 914 E---ARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLR-ELEKKKKLE 980
Cdd:pfam05483 703 AemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiEKEEKEKLK 773
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
588-980 |
1.12e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 588 KQYQQLESRLDEILSRIAKETEEIKDLE------EQLTEGQIAAneALKKDLEGVISGLQEYLGTIKGQATQAQNECRKL 661
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQrlhqafSRFIGSHLAV--AFEADPEAELRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 662 RDEKETLLQRLTEVEQERDQLEIvaMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEArlnLRDAEAN-- 739
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRLNL--LADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSV---LQSDPEQfe 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 740 QLKEELEKVTrlTQLEQSALQAELEKERQALKNALG--KAQFSEEKEQENSE-LHAKLKHLQDDNNLLKQQLKDFQNHL- 815
Cdd:PRK04863 939 QLKQDYQQAQ--QTQRDAKQQAFALTEVVQRRAHFSyeDAAEMLAKNSDLNEkLRQRLEQAEQERTRAREQLRQAQAQLa 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 816 --NHVVDGLVRPEEVAAR-VDELRRKLKlgtgEMNIHSPSDVLGKSLADlQKQFSEILARSKWERDEAQVRERKLQEEMA 892
Cdd:PRK04863 1017 qyNQVLASLKSSYDAKRQmLQELKQELQ----DLGVPADSGAEERARAR-RDELHARLSANRSRRNQLEKQLTFCEAEMD 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 893 LQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIH-----YLQ-ENLKSMEEIqGLTDLQLQEADEEKERi 966
Cdd:PRK04863 1092 NLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHrrelaYLSaDELRSMSDK-ALGALRLAVADNEHLR- 1169
|
410
....*....|....
gi 1622996215 967 lAQLRELEKKKKLE 980
Cdd:PRK04863 1170 -DVLRLSEDPKRPE 1182
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
487-986 |
1.48e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 487 LRATEEFK-----QLEEAIQLKKISEAGKDLLYKQLSgrlQLVNKLRQEALDLELQMEkqkqeiaGKQKEIKDLQIAIDS 561
Cdd:pfam01576 491 LRQLEDERnslqeQLEEEEEAKRNVERQLSTLQAQLS---DMKKKLEEDAGTLEALEE-------GKKRLQRELEALTQQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 562 LDSKDPKHSHMKAQKSGKEQQLD--IMNKQYQ-QLESRLDEILSRIAKETEEIKDLEEQLTEGQIAAnEALKKDLEGVIS 638
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDdlLVDLDHQrQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRA-EAEAREKETRAL 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 639 GLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLE----IVAMDAENMRKELAELESALQEQHEVNASLQ 714
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELErskrALEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 715 QTqgdLSAYEAELEARLNLRDAEANQLKEELEKVTRltqleqsALQAELEKERQALKNAL-GKAQFSEEKEQENSELHAK 793
Cdd:pfam01576 720 VN---MQALKAQFERDLQARDEQGEEKRRQLVKQVR-------ELEAELEDERKQRAQAVaAKKKLELDLKELEAQIDAA 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 794 LKHLQDDNNLLKQ---QLKDFQNHLNhvvDGLVRPEEVAARVDELRRKLKLGTGEMnihspsdvlgksladlqKQFSEIL 870
Cdd:pfam01576 790 NKGREEAVKQLKKlqaQMKDLQRELE---EARASRDEILAQSKESEKKLKNLEAEL-----------------LQLQEDL 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 871 ARSKWERDEAQVRERKLQEEMALQQEKLATGQEEfrqaceralearmnfdKRQHEARIQQMENEIHYLQENLKSMEEIQG 950
Cdd:pfam01576 850 AASERARRQAQQERDELADEIASGASGKSALQDE----------------KRRLEARIAQLEEELEEEQSNTELLNDRLR 913
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622996215 951 LTDLQLQEADEE--KERILAQLRE-----LEKKKKLEDAKSQE 986
Cdd:pfam01576 914 KSTLQVEQLTTElaAERSTSQKSEsarqqLERQNKELKAKLQE 956
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1443-1603 |
1.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1443 IEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQ--ETAVNLVKADQQLRSL 1520
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1521 QADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAernedhhLQVLKESEVLLQAKRAE 1600
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE-------LAELEAELEELEAEREE 167
|
...
gi 1622996215 1601 LEK 1603
Cdd:COG1579 168 LAA 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
458-686 |
1.74e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 458 LEDKEKKISAAQTRLSELHDE----IEKAEQQILRATEEFKQLEeaIQLKKISEAgkdllykqlsgrlqlVNKLRQEALD 533
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDElveeAKTIKAEIEELTDELLNLV--MDIEDPSAA---------------LNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQkqeiagkQKEIKDLQ------IAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKE 607
Cdd:PHA02562 267 IKSKIEQF-------QKVIKMYEkggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 608 TEEIKDLEEQltEGQIAANEALKKDLEGVISGLQEYLGTIKGqatqaqnECRKLRDEKETLLQRLTEVEQERDQLEIVA 686
Cdd:PHA02562 340 LELKNKISTN--KQSLITLVDKAKKVKAAIEELQAEFVDNAE-------ELAKLQDELDKIVKTKSELVKEKYHRGIVT 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
245-705 |
1.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 245 RSLESLEGQPVTTQDRQEAFERfSLEEVERLERDLEKKMIETEELKSKQTRFLEEIKNQDKLNKSL----KEEAML--QK 318
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreieKRLSRLeeEI 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 319 QSCEELKSDLNTKNElPLSWfLAGPFLLILYSSLKLKQKTIELTRACQKQYELEQ---ELAFYKIDAKFEPLNYYPSEYA 395
Cdd:PRK03918 324 NGIEERIKELEEKEE-RLEE-LKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkRLTGLTPEKLEKELEELEKAKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 396 EIDKAPDE-SPYIGKSRYKRNMFATESYIIDSAQAV-QIKKMEPDEQLRNDHMNlrghtPLDTQLEDKEKKISAAQTRLS 473
Cdd:PRK03918 402 EIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKcPVCGRELTEEHRKELLE-----EYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 474 ELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIK 553
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 554 DLQIAIDSLDSKDPKHSHMKAQ------KSGKE-----QQLDIMNKQYQQL---ESRLDEILSRIAKETEEIKDLEEQLT 619
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKEleelgfESVEEleerlKELEPFYNEYLELkdaEKELEREEKELKKLEEELDKAFEELA 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 620 EgqiaaneaLKKDLEGVISGLQEYlgtikgQATQAQNECRKLRDEKETLLQRL----TEVEQERDQLEIVAMDAENMRKE 695
Cdd:PRK03918 637 E--------TEKRLEELRKELEEL------EKKYSEEEYEELREEYLELSRELaglrAELEELEKRREEIKKTLEKLKEE 702
|
490
....*....|
gi 1622996215 696 LAELESALQE 705
Cdd:PRK03918 703 LEEREKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1372-1607 |
2.03e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1372 EKEMEELHHNIDDLLQEKKSLECEVEELHR--TVQKRQQQKDFIDGNVESLMTELEIEKSLKHHEDIVDEIECIEKTLLK 1449
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1450 RRSELREADRLLAEAESELSCTKEKTKNAV-EKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKDLE 1528
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 1529 QhkikqeeilkeinkivaakdsDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKSQ 1607
Cdd:TIGR02169 343 R---------------------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-1565 |
2.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1343 EVSRLEDIMQHLKSKKREERWMRASKR-----QSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNV 1417
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1418 ESLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSElreADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAE 1497
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE---EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 1498 ELERRAQET----AVNLVKADQQLRSLQADAKDLEQHKIKQEEiLKEINKIVAAKDSDFQCLSKKKEKLTEE 1565
Cdd:PTZ00121 1713 EEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
526-783 |
2.49e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 526 KLRQEALDLEL--QMEK-QKQEIAGKQKEIKDLQIAIDSLDSKdpkhshMKAQKSGKEQQldimNKQYQQLESRLDEILS 602
Cdd:PHA02562 154 KLVEDLLDISVlsEMDKlNKDKIRELNQQIQTLDMKIDHIQQQ------IKTYNKNIEEQ----RKKNGENIARKQNKYD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 603 RIAKETEEIKDLEEQLTEgQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKE--TLLQ-------RLT 673
Cdd:PHA02562 224 ELVEEAKTIKAEIEELTD-ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQqisegpdRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 674 EVEQERDQLEIVAMDAENMRKELAELESALQEQ----HEVNASLQQTQGDLSAYeaelearlnlrDAEANQLKEELEKVT 749
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskklLELKNKISTNKQSLITL-----------VDKAKKVKAAIEELQ 371
|
250 260 270
....*....|....*....|....*....|....
gi 1622996215 750 RLTQLEQSALqAELEKERQALKNAlgKAQFSEEK 783
Cdd:PHA02562 372 AEFVDNAEEL-AKLQDELDKIVKT--KSELVKEK 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1365-1578 |
2.85e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1365 RASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDfidgnveSLMTELEiekslkhhedivdeiecie 1444
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-------KLTEEYA------------------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1445 ktllKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLlqtesdaEELERRAQETAVNLVKADQQLRSLQADA 1524
Cdd:TIGR02169 361 ----ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI-------NELKRELDRLQEELQRLSEELADLNAAI 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622996215 1525 KDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAER 1578
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
572-776 |
3.33e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 572 MKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLtegqiaanEALK--KDLEGVISGLQ--EYLGTI 647
Cdd:PRK05771 77 KKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI--------ERLEpwGNFDLDLSLLLgfKYVSVF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 648 KGQATQAQNECRKLRDEKETLLqrltEVEQERDQLEIVAM----DAENMRKELAELEsaLQEQHEvnaslqQTQGDLSAY 723
Cdd:PRK05771 149 VGTVPEDKLEELKLESDVENVE----YISTDKGYVYVVVVvlkeLSDEVEEELKKLG--FERLEL------EEEGTPSEL 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 724 EAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAEL--EKERQALKNALGK 776
Cdd:PRK05771 217 IREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLeiELERAEALSKFLK 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1336-1531 |
3.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1336 EHHNLENEVSRLEDIMQHLKSKKREERWmraskRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDG 1415
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRL-----ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1416 NveslmtelEIEkSLKHhedivdEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKftdAKRSLLQTESD 1495
Cdd:COG4913 338 D--------RLE-QLER------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622996215 1496 AEELERRAQETAVNLVKADQQLRSLQADAKDLEQHK 1531
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
591-808 |
3.61e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 591 QQLESRLDEILSRIAKETEE---IKDLEEQLTegQIAANEALKKDLEgvisglqeylgTIKGQATQAQNECRKLRDEket 667
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDklvQQDLEQTLA--LLDKIDRQKEETE-----------QLKQQLAQAPAKLRQAQAE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 668 lLQRLTEveqerDQLEIVAMDAENMrkELAELESALQEqheVNASLQQTQGDLSAYEAE--------------------- 726
Cdd:PRK11281 103 -LEALKD-----DNDEETRETLSTL--SLRQLESRLAQ---TLDQLQNAQNDLAEYNSQlvslqtqperaqaalyansqr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 727 -------------------------LEARLNLRDAEANQLKEELEKVTRLTQLEQS------ALQAELEKERQALKNALG 775
Cdd:PRK11281 172 lqqirnllkggkvggkalrpsqrvlLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKqrdyltARIQRLEHQLQLLQEAIN 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622996215 776 --KAQFSEE--KEQENSELHAKLKHlqddNNLLKQQL 808
Cdd:PRK11281 252 skRLTLSEKtvQEAQSQDEAARIQA----NPLVAQEL 284
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
600-1142 |
3.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 600 ILSRIAKETEEIKDLEEQLTEGQIAANEALKKDLEGVISGLQEYLgtikgqatQAQNECRKLRDEKETLLQRLTEVEQER 679
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA--------ELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 680 DQLEIvamdaenmrkeLAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSAL 759
Cdd:COG4717 119 EKLEK-----------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 760 QAELEKERQALKNAlgkaqfsEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLnhvvdglvRPEEVAARVDELRRKL 839
Cdd:COG4717 188 LATEEELQDLAEEL-------EELQQRLAELEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARLLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 840 KLGTGEMNIHSPSDVLGKSLADLQK----------QFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRqaC 909
Cdd:COG4717 253 LIAAALLALLGLGGSLLSLILTIAGvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG--L 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 910 ERALEARMNFDKRQHEARIQQMENEIHYLQENLK---SMEEIQGLTDLQLQEADEEKERILAQLRELEKKKkledaksqe 986
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQleeLEQEIAALLAEAGVEDEEELRAALEQAEEYQELK--------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 987 qvfgldkelkklkkavatsdklatAELTIAKDQLKSLHGtvmkinqeraeelqeaerfSRKAAQAARDLTRAEAEIELLQ 1066
Cdd:COG4717 402 ------------------------EELEELEEQLEELLG-------------------ELEELLEALDEEELEEELEELE 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 1067 NllrqkgeqfrlemektgvgtgansqvlEIEKLNETMERQRTEIARLQNVLDLTGSDNKggFENVLEEIAELRREV 1142
Cdd:COG4717 439 E---------------------------ELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAEL 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1340-1548 |
3.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDL-LQEKKSLECEVEELhrtvqkrqqqKDFIDGNVE 1418
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKEL----------EPFYNEYLE 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1419 SLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSctKEKTKNAVEKFTDAKRSLLQTESDAEE 1498
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEE 684
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1499 LERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAK 1548
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
461-556 |
3.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 461 KEKKISAAQtrlSELHDEIEKAEQQILRATEEFKQLEEAIQLKKiseagkdllyKQLSGRLQLVNKLRQEALDLELQMEK 540
Cdd:PRK12704 55 KKEALLEAK---EEIHKLRNEFEKELRERRNELQKLEKRLLQKE----------ENLDRKLELLEKREEELEKKEKELEQ 121
|
90
....*....|....*.
gi 1622996215 541 QKQEIAGKQKEIKDLQ 556
Cdd:PRK12704 122 KQQELEKKEEELEELI 137
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
460-800 |
4.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 460 DKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEE---AIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEAldlEL 536
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---DK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQKEIKdlqiaIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEE 616
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEAR-----IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 617 ---QLTEGQIAANEALKKDLEgvisglqeylgtikgqATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMR 693
Cdd:PTZ00121 1652 lkkAEEENKIKAAEEAKKAEE----------------DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 694 KELAELESALQEQhevnaslqqtqgDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKErqalKNA 773
Cdd:PTZ00121 1716 KKAEELKKAEEEN------------KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE----KEA 1779
|
330 340
....*....|....*....|....*..
gi 1622996215 774 LGKAQFSEEKEQENSELHAKLKHLQDD 800
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
569-748 |
4.38e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 569 HSHMKAQKSGKEQQLDiMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEgqiaaneaLKKDLEGVISGLQEyLGTIK 648
Cdd:pfam13851 22 RNNLELIKSLKEEIAE-LKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEE--------LRKQLENYEKDKQS-LKNLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 649 GQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivaMDAENMRKEL---AELESALQEQhevnaSLQQTQGDLSAYEA 725
Cdd:pfam13851 92 ARLKVLEKELKDLKWEHEVLEQRFEKVERERDELY---DKFEAAIQDVqqkTGLKNLLLEK-----KLQALGETLEKKEA 163
|
170 180
....*....|....*....|....*.
gi 1622996215 726 ELE---ARLNLRDAEANQLKEELEKV 748
Cdd:pfam13851 164 QLNevlAAANLDPDALQAVTEKLEDV 189
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
657-1147 |
4.45e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 657 ECRKLRDE----KETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQtqgdlsAYEAELEarln 732
Cdd:pfam07111 74 ELRRLEEEvrllRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEE------GSQRELE---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 733 lrdaEANQLKEEleKVTRLTQLEQSALqAELEKERQALKNALGKAQFSEEKEQEnselhaKLKHLQDDNNLLKQQLKDFQ 812
Cdd:pfam07111 144 ----EIQRLHQE--QLSSLTQAHEEAL-SSLTSKAEGLEKSLNSLETKRAGEAK------QLAEAQKEAELLRKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 813 NHLNHVVD---------GLVRPEEVAARVDELRRKLKLGTGEMnihspsdvLGKSLADLQKQFsEILarskwerdeaQVR 883
Cdd:pfam07111 211 EELEAQVTlveslrkyvGEQVPPEVHSQTWELERQELLDTMQH--------LQEDRADLQATV-ELL----------QVR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 884 ERKLQEEMALQQEKLATG-------QEEFRQACER----------ALEARMNFDKRQHEARIQQMENEIHYLQENLKSME 946
Cdd:pfam07111 272 VQSLTHMLALQEEELTRKiqpsdslEPEFPKKCRSllnrwrekvfALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 947 EIQGLTDLQLQE--ADEEKERILAQLRELEKKKKLEDAKSQEQvfgldkelkklkkAVATSDKLATAELTIAKDQLKSLH 1024
Cdd:pfam07111 352 QEQAILQRALQDkaAEVEVERMSAKGLQMELSRAQEARRRQQQ-------------QTASAEEQLKFVVNAMSSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1025 GTVMKINQERAEELQEAERFSRKAAQA-------ARDLTRAEAEIE--------------LLQNLLRQKGEQFRLEME-- 1081
Cdd:pfam07111 419 TTMTRVEQAVARIPSLSNRLSYAVRKVhtikglmARKVALAQLRQEscpppppappvdadLSLELEQLREERNRLDAElq 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 1082 ------KTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDLTGSD---NKGGFENVLEEIAELRREVSYQND 1147
Cdd:pfam07111 499 lsahliQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevARQGQQESTEEAASLRQELTQQQE 573
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
608-816 |
4.46e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 608 TEEIKDLEEQLTEGQIAANEALkkdlEGVISGLQEYlgtiKGQATQAQnECRKLRDEKETLLQRL-TEVEQERDQLEIVA 686
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEAL----QSALNWLEER----KGSLERAK-QYQQVIDNFPKLSAELrQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 687 --MDAENMRKELAELESAL--------QEQ---HEVNASLQQTQGDLSayeaelEARLNLRDAEaNQLKEELEKVTRLTQ 753
Cdd:PRK10929 100 pnMSTDALEQEILQVSSQLleksrqaqQEQdraREISDSLSQLPQQQT------EARRQLNEIE-RRLQTLGTPNTPLAQ 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 754 LEQSALQAELEKeRQALKNALGKAQFSEEKEQENSELHAKLkhLQDDNNLLKQQLKDFQNHLN 816
Cdd:PRK10929 173 AQLTALQAESAA-LKALVDELELAQLSANNRQELARLRSEL--AKKRSQQLDAYLQALRNQLN 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1339-1603 |
4.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1339 NLENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDdLLQEKKSLECEVEELHRTVQKRQQQKdfIDGNVE 1418
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKRLTGLTPEK--LEKELE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1419 SLMTE-LEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELscTKEKTKNAVEKFTDAKRSLLQTESDAE 1497
Cdd:PRK03918 395 ELEKAkEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL--TEEHRKELLEEYTAELKRIEKELKEIE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1498 ELERRAQETAVNLVKADQQLRSLQADAKDLEQHKiKQEEILKEIN-KIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMA 1576
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
250 260
....*....|....*....|....*..
gi 1622996215 1577 ERNEDhHLQVLKESEVLLQAKRAELEK 1603
Cdd:PRK03918 552 EELKK-KLAELEKKLDELEEELAELLK 577
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
477-747 |
4.66e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 477 DEIEKAEQQILRATEEFKQLEEAIQ--LKKISE-AGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIagkqKEIK 553
Cdd:TIGR01612 1500 DEADKNAKAIEKNKELFEQYKKDVTelLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKI----KEIK 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 554 DLQIAIDsldskDPKHSHMKAQKSGKEQQLDIMNKQYQQLesRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKKDL 633
Cdd:TIGR01612 1576 KEKFRIE-----DDAAKNDKSNKAAIDIQLSLENFENKFL--KISDIKKKINDCLKETESIEKKISSFSIDSQDTELKEN 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 634 EGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENmrkelaelESALQEQHEvnasL 713
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIK--------EIAIANKEE----I 1716
|
250 260 270
....*....|....*....|....*....|....
gi 1622996215 714 QQTQGDLSAYEAELEARLNLRDAEANQLKEELEK 747
Cdd:TIGR01612 1717 ESIKELIEPTIENLISSFNTNDLEGIDPNEKLEE 1750
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1372-1602 |
4.83e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1372 EKEMEELHHNIDDLLQEKKSLECEVEELH----RTVQKRQQQKDFIDGNVESLMTELEIEKSLKHHEDIVDEIECIEKTL 1447
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEeqreQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1448 LKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLlqtESDAEELERRAQETAVNLVKADQQLRSLQADAKDL 1527
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 1528 EQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQK---DIEMAERNEDHHLQVLKESEVLLQAKRAELE 1602
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-1600 |
4.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1343 EVSRLEDIMQHLKSKKREERWMRASKRQSE--KEMEELH--HNIDDLLQEKKSLECEVEELHRTVQKRQQQKdfidGNVE 1418
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADelKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE----ARIE 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1419 SLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESD--- 1495
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkk 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1496 -AEELERRAQETAvnlvKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQK-DI 1573
Cdd:PTZ00121 1676 kAEEAKKAEEDEK----KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKK 1751
|
250 260
....*....|....*....|....*..
gi 1622996215 1574 EMAERNEDHHLQVLKESEVLLQAKRAE 1600
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
749-1140 |
5.15e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 749 TRLTQLEQSALQAELEKERQALKNALGKAqfSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEV 828
Cdd:COG4717 37 STLLAFIRAMLLERLEKEADELFKPQGRK--PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 829 AARVDELRRKLKLGTgemnihspsdvLGKSLADLQKQFSEILARskWERDEAQVRERK-LQEEMALQQEKLATGQEEFRQ 907
Cdd:COG4717 115 REELEKLEKLLQLLP-----------LYQELEALEAELAELPER--LEELEERLEELReLEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 908 ACERALEArmnfdkrqHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQ 987
Cdd:COG4717 182 LLEQLSLA--------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 988 VFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQN 1067
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 1068 LLRQKGEQFRLEMEKtgvgtgANSQVLEIEKLNETMERQRTEiARLQNVLDLTGSDNKGGFENVLEEIAELRR 1140
Cdd:COG4717 334 LSPEELLELLDRIEE------LQELLREAEELEEELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1340-1606 |
5.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKREERWMRASK-------RQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDF 1412
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTenieeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1413 IDgnvESLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAEsELSCTKEKTKNAVEKFTDAKRSLLQT 1492
Cdd:PRK03918 240 IE---ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1493 ESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDsDFQCLSKKK-----EKLTEELQ 1567
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLtgltpEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622996215 1568 KLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKS 1606
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
455-744 |
5.33e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.59 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 455 DTQLEDKEKKISAAQTRLSEL------HDEIEKAEQQILRATEEF-KQLEEaiQLKKISEAGKDLLYKQLsgrlqlvNKL 527
Cdd:pfam13779 481 DGDLSDAERRLRAAQERLSEAlergasDEEIAKLMQELREALDDYmQALAE--QAQQNPQDLQQPDDPNA-------QEM 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 RQEALDlelQMEKQKQEIA--GKQKEIKD----LQIAIDSLDSKDPKHSHMKAQKSGKEQQ---LDIMNKQyQQLesrLD 598
Cdd:pfam13779 552 TQQDLQ---RMLDRIEELArsGRRAEAQQmlsqLQQMLENLQAGQPQQQQQQGQSEMQQAMdelGDLLREQ-QQL---LD 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 599 EILSRIAKETEEIKDLEEQltEGQiaanealkkDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQe 678
Cdd:pfam13779 625 ETFRQLQQQGGQQQGQPGQ--QGQ---------QGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEELQD- 692
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 679 rdqlEIVAMDAENMRKELAElesALQEQHEVNASLQQTQGDlSAYEAELEARLNLRD---AEANQLKEE 744
Cdd:pfam13779 693 ----ELKELGGKEPGQALGD---AGRAMRDAEEALGQGDLA-GAVDAQGRALEALRKgaqQLAEAMQQQ 753
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
170-213 |
6.04e-04 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 39.15 E-value: 6.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622996215 170 NLQKLNLAGNEIEHIPvwLGKKLKSLRVLNLKGN-KISSLQDISK 213
Cdd:pfam12799 2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNnKITDLSDLAN 44
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
86-216 |
6.22e-04 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 43.88 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 86 ALIKKLTKQDNLALIKSLNLSLSKDGGKKFkyIENLEKCV-KLEVLNLSYNLI--GKIEKLDKLL----KLRELNLSYNK 158
Cdd:cd00116 99 GVLESLLRSSSLQELKLNNNGLGDRGLRLL--AKGLKDLPpALEKLVLGRNRLegASCEALAKALranrDLKELNLANNG 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 159 ISKiEGIENMC-------NLQKLNLAGNEIEHIPV----WLGKKLKSLRVLNLKGNKISSLqDISKLKP 216
Cdd:cd00116 177 IGD-AGIRALAeglkancNLEVLDLNNNGLTDEGAsalaETLASLKSLEVLNLGDNNLTDA-GAAALAS 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
627-812 |
6.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 627 EALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivamdaenmrKELAELESALQEQ 706
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----------AEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 707 HEV----NASLQQTQGDLSAYEAELEA--------RLNLRD-----------------AEANQLKEELEKvtrlTQLEQS 757
Cdd:COG3883 85 REElgerARALYRSGGSVSYLDVLLGSesfsdfldRLSALSkiadadadlleelkadkAELEAKKAELEA----KLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622996215 758 ALQAELEKERQALKNALgkaqfsEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQ 812
Cdd:COG3883 161 ALKAELEAAKAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
548-1141 |
7.28e-04 |
|
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: 44.57 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 548 KQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANE 627
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 628 ALKKdlegvisgLQEYLgTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIvAMDAENMRKELAELESALQEQH 707
Cdd:TIGR00618 241 SHAY--------LTQKR-EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINR-ARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 708 EVNASLQQTqgdlsayEAELEARLNLRDAEANQLKEELEKvtrlTQLEQSALQAELEKERQALKNALGKAQFSEEKEQEN 787
Cdd:TIGR00618 311 RIHTELQSK-------MRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 788 S--ELHAKLKHLQDDNNLLKQQLKDFQNhLNHVVDGL------VRPEEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSL 859
Cdd:TIGR00618 380 HihTLQQQKTTLTQKLQSLCKELDILQR-EQATIDTRtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 860 ADLQKQFSEILARSKWERDEAQVRERKlQEEMALQQEKLATGQEEFRQACERALE----ARMNFDKRQHEARIQQMENEI 935
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQE-TRKKAVVLARLLELQEEPCPLCGSCIHpnpaRQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 936 HYLQENLKSMEEIQGLTDLQLQEADEEKERI------LAQLR-----ELEKKKKLED---------AKSQEQVFGLDKEL 995
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsiLTQCDnrskeDIPNLQNITVrlqdlteklSEAEDMLACEQHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 996 KKLKKAVATSDKLATAELTIAKDQ---LKSLHGTVMKINQERAEELQEAERfsrkaAQAARDLTRAEAEIELLQNLLRQk 1072
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELalkLTALHALQLTLTQERVREHALSIR-----VLPKELLASRQLALQKMQSEKEQ- 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 1073 geqfrlemeKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDLTGSDNKGGFENVLEEIAELRRE 1141
Cdd:TIGR00618 692 ---------LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
696-947 |
7.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 696 LAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKeELEKVTRLTQLEQSALQAELEKERQALKnalg 775
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 776 kaqfseEKEQENSELHAKLKHLQDDnnlLKQQLKD-FQNHLNHVVDGLVRPEEVAARVDELRRklklgtgeMNIHSPSDv 854
Cdd:COG4942 87 ------ELEKEIAELRAELEAQKEE---LAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQY--------LKYLAPAR- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 855 lgKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEfrqacERALEARMNFDKRQHEARIQQMENE 934
Cdd:COG4942 149 --REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE-----RQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|...
gi 1622996215 935 IHYLQENLKSMEE 947
Cdd:COG4942 222 AEELEALIARLEA 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1340-1608 |
7.67e-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: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKRE--ERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTV-----QKRQQQKDF 1412
Cdd:pfam15921 236 LKGRIFPVEDQLEALKSESQNkiELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLeiiqeQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1413 ID--GNVESLMTEL--EIEKSLKHHEDivdEIECIEKTLLKRRSELREA------------------DRLLAE---AESE 1467
Cdd:pfam15921 316 MRqlSDLESTVSQLrsELREAKRMYED---KIEELEKQLVLANSELTEArterdqfsqesgnlddqlQKLLADlhkREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1468 LSCTKEKTKNAVEKFTDAKRSL--LQTESDAEELERRAQETAVNLVKAD------QQLRSLQAdakdleqhkikQEEILK 1539
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIdhLRRELDDRNMEVQRLEALLKAMKSEcqgqmeRQMAAIQG-----------KNESLE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 1540 EINKIVAAKDSDFQCLskkkEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKSQV 1608
Cdd:pfam15921 462 KVSSLTAQLESTKEML----RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
459-810 |
1.07e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.78 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 459 EDKEKKISAAQTRLSELH----------DEIEKAEQQILRATEEF-KQLEEaIQLKKISEAGKDLLYKQLSGRLQlvnKL 527
Cdd:pfam15818 88 EIKEKEIEGLKETLKALQvskyslqkkvSEMEQKLQLHLLAKEDHhKQLNE-IEKYYATITGQFGLVKENHGKLE---QN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 RQEALDLELQM----EKQKQEIAGKQKEIKdlQIAIDSLDSKDPKHSHMKAQKSgkeqQLDIMNKQYQQLESRLDEILSR 603
Cdd:pfam15818 164 VQEAIQLNKRLsalnKKQESEICSLKKELK--KVTSDLIKSKVTCQYKMGEENI----NLTIKEQKFQELQERLNMELEL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 604 IAKETEEIKDLEE-------------QLTEGQIAANEALKKDLEgvisGLQEylgtiKGQATQAQNECR--KLRDEKETL 668
Cdd:pfam15818 238 NKKINEEITHIQEekqdiiisfqhmqQLLQQQTQANTEMEAELK----ALKE-----NNQTLERDNELQreKVKENEEKF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 669 LQRLTEVEQerdQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKv 748
Cdd:pfam15818 309 LNLQNEHEK---ALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENSEMST- 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 749 trlTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKD 810
Cdd:pfam15818 385 ---EKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQVLEKSFKN 443
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
527-1110 |
1.10e-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: 43.66 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 527 LRQEALDLELQMEKQKQEIAGKQKEIKDLqiaIDSLDSKDPKhSHMKAQKSGKEQQLDIMNKQYQQLESRLDEilsriaK 606
Cdd:pfam10174 135 LRKTLEEMELRIETQKQTLGARDESIKKL---LEMLQSKGLP-KKSGEEDWERTRRIAEAEMQLGHLEVLLDQ------K 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 607 ETEEIKDLEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLrdeKETLLQRLTEVEQERDQLEIVA 686
Cdd:pfam10174 205 EKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQML---KTNGLLHTEDREEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 687 MDAENMRKELAELESALQEQhevnaslqqtQGDLSAYEAELEArLNLRDAEANQ----LKEEL---EKVTRLTQLEQSAL 759
Cdd:pfam10174 282 SHSKFMKNKIDQLKQELSKK----------ESELLALQTKLET-LTNQNSDCKQhievLKESLtakEQRAAILQTEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 760 QAELEKERQALKNalgKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVaarVDELRRKL 839
Cdd:pfam10174 351 RLRLEEKESFLNK---KTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ---LAGLKERV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 840 K-LGTGEMNIHSPSDVLGKSLAD-------LQKQfSEILARSKWERDEAQVRERK-LQEEMALQQEKLATGQEEFRQACE 910
Cdd:pfam10174 425 KsLQTDSSNTDTALTTLEEALSEkeriierLKEQ-REREDRERLEELESLKKENKdLKEKVSALQPELTEKESSLIDLKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 911 RALEARMNFDKRqhEARIQQMENEIHYLQENLKSMEEiQGLTDLQLQEADEEKERILAQLRELEK---KKKLEDAKSQEQ 987
Cdd:pfam10174 504 HASSLASSGLKK--DSKLKSLEIAVEQKKEECSKLEN-QLKKAHNAEEAVRTNPEINDRIRLLEQevaRYKEESGKAQAE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 988 VfgldkelkklkkavatsDKLataeLTIAKDQLKSLHGTVMKINQeraeelqeaerFSRKAAQAARDLTRAEAEIELLQN 1067
Cdd:pfam10174 581 V-----------------ERL----LGILREVENEKNDKDKKIAE-----------LESLTLRQMKEQNKKVANIKHGQQ 628
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622996215 1068 LLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEI 1110
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
145-206 |
1.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 43.27 E-value: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622996215 145 KLLKLRELNLSYNKIskiEG-----IENMCNLQKLNLAGNEIE-HIPVWLGKkLKSLRVLNLKGNKIS 206
Cdd:PLN03150 440 KLRHLQSINLSGNSI---RGnippsLGSITSLEVLDLSYNSFNgSIPESLGQ-LTSLRILNLNGNSLS 503
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
666-1117 |
1.46e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 666 ETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQqtqgDLSAYEAELEARLNLRDAEANQLKEEL 745
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVI----ALRRAGGLEAALALVRSGEGKALMDEI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 746 EKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRP 825
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 826 EEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEF 905
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 906 RQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQ 985
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 986 EQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELL 1065
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 1066 QNLLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVL 1117
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
528-883 |
1.79e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 528 RQEALDLELQMEKQKQEIAGKQKEIKDLQIaidSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKE 607
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARI---ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 608 TEEIKDLEEQLTEgQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAM 687
Cdd:pfam05557 78 NRLKKKYLEALNK-KLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 688 DAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELeARLNLRDAEANQLKEELEKVTrltqlEQSALQAELEKER 767
Cdd:pfam05557 157 NLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLN-----ENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 768 QALKNALGKaqfsEEKEQEnselhaKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDEL-RRKLKLGTGEM 846
Cdd:pfam05557 231 EDLKRKLER----EEKYRE------EAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLqQREIVLKEENS 300
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622996215 847 NIHSPSDVLGKSLADLQKQFSEILA-----RSKWERDEAQVR 883
Cdd:pfam05557 301 SLTSSARQLEKARRELEQELAQYLKkiedlNKKLKRHKALVR 342
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1438-1607 |
1.86e-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: 42.44 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1438 DEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQL 1517
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1518 RSLQADAKDL--EQHKIKQEEILKEINKIVAAKDSD-----FQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKES 1590
Cdd:COG4942 100 EAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*..
gi 1622996215 1591 EVLLQAKRAELEKLKSQ 1607
Cdd:COG4942 180 LAELEEERAALEALKAE 196
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
652-787 |
1.90e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 652 TQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAmDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARL 731
Cdd:PRK12705 40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARR-EREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 732 NLRDAEANQLKEELEKVTRLTQLEQ-----SALQAELEKERQALKNA-LGKAQFSEEKEQEN 787
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQArklllKLLDAELEEEKAQRVKKiEEEADLEAERKAQN 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
574-986 |
2.07e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 574 AQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEgqiaaNEALKKDLEGVISGLQEYLGTIKGQATQ 653
Cdd:pfam07888 52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEE-----LEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 654 AQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQeqhevnASLQQTQGDLSAYEAELEARLNL 733
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ------AKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 734 RDAEANQLKEELEKVTRLTQLEQSALQAELEKErqALKNALGKAQFSEEKEQENSELhaklkhlqddnnlLKQQLKDFQN 813
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE--ALLEELRSLQERLNASERKVEG-------------LGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 814 HLNHVVDGLvrpeevaarvdelrRKLKLGTGEMNIHspsdvlgksLADLQKQFSEilARSKWerdeAQVRErKLQEEMAL 893
Cdd:pfam07888 266 QRDRTQAEL--------------HQARLQAAQLTLQ---------LADASLALRE--GRARW----AQERE-TLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 894 QQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIhylqenlksmeeiqgltdlQLQEADEEKERILAQLREL 973
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRV-------------------QLSESRRELQELKASLRVA 376
|
410
....*....|...
gi 1622996215 974 EKKKKLEDAKSQE 986
Cdd:pfam07888 377 QKEKEQLQAEKQE 389
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
582-816 |
2.07e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.75 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 582 QLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLtegqiaanEALKKDLEGVIS---GLQEYLGTIK-GQATQAQne 657
Cdd:pfam05622 184 QLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKL--------EALQKEKERLIIerdTLRETNEELRcAQLQQAE-- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 658 crklrdeketLLQRLTEVEQERDQLEIVAmdAENMRKELAEleSALQEQHEVNASLQQTQGDLSAYEAELEARLNlrdaE 737
Cdd:pfam05622 254 ----------LSQADALLSPSSDPGDNLA--AEIMPAEIRE--KLIRLQHENKMLRLGQEGSYRERLTELQQLLE----D 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 738 ANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLN 816
Cdd:pfam05622 316 ANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQD 394
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1343-1606 |
2.21e-03 |
|
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: 42.80 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1343 EVSRLEDIMQHLKS--KKREERWMRA---------------SKRQSEKEMeeLHHNIDDLLQEKKSLECE---VEELHRT 1402
Cdd:pfam15921 427 EVQRLEALLKAMKSecQGQMERQMAAiqgkneslekvssltAQLESTKEM--LRKVVEELTAKKMTLESSertVSDLTAS 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1403 VQKRQQQKDFIDGNVESLMTELEIE-KSLKHHEDIVDEIECIEKTLLKRRSELREADRLLA------EAESELSCTKEKT 1475
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEilrqqiENMTQLVGQHGRT 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1476 KNAVEkftdAKRSLLQTESDAEELErrAQETAVNLVKADQQLRSLQADAKDLEQHKIK----QEEILKEINKIVAAKDsd 1551
Cdd:pfam15921 585 AGAMQ----VEKAQLEKEINDRRLE--LQEFKILKDKKDAKIRELEARVSDLELEKVKlvnaGSERLRAVKDIKQERD-- 656
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 1552 fQCLSKKKEKlTEELQKLQKDIEMAERNEDHHLQVLKES----EVLLQAKRAELEKLKS 1606
Cdd:pfam15921 657 -QLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMETTtnklKMQLKSAQSELEQTRN 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1447-1608 |
2.22e-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: 42.74 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1447 LLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKD 1526
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1527 LEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKS 1606
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
..
gi 1622996215 1607 QV 1608
Cdd:TIGR02168 832 RI 833
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1340-1604 |
2.23e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKREerwMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVES 1419
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSE---KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1420 LmtELEIEKSLKHHEDIVDEIECIEKTLlkrrSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQT-ESDAEE 1498
Cdd:TIGR04523 417 L--QQEKELLEKEIERLKETIIKNNSEI----KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNlEQKQKE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1499 LERRAQEtavnLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAER 1578
Cdd:TIGR04523 491 LKSKEKE----LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEK 566
|
250 260
....*....|....*....|....*.
gi 1622996215 1579 NEDhhLQVLKESEVLLQAKRAELEKL 1604
Cdd:TIGR04523 567 NKE--IEELKQTQKSLKKKQEEKQEL 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
769-1037 |
2.28e-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: 42.06 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 769 ALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLnhvvdglvrpEEVAARVDELRRKLKLGTGEMNi 848
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL----------AALERRIAALARRIRALEQELA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 849 hspsdVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQAceralEARMNFDKRQHEARI 928
Cdd:COG4942 80 -----ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-----VRRLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 929 QQMEneihYLQENLKSMEEIQgltdLQLQEADEEKERILAQLRelEKKKKLEDAKSQEQvfgldkelkKLKKAVATSDKL 1008
Cdd:COG4942 150 EQAE----ELRADLAELAALR----AELEAERAELEALLAELE--EERAALEALKAERQ---------KLLARLEKELAE 210
|
250 260
....*....|....*....|....*....
gi 1622996215 1009 ATAELTIAKDQLKSLHGTVMKINQERAEE 1037
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF5082 |
pfam16888 |
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized. |
527-648 |
2.36e-03 |
|
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.
Pssm-ID: 407125 [Multi-domain] Cd Length: 122 Bit Score: 39.59 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 527 LRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNK---------------QYQ 591
Cdd:pfam16888 1 LKTEISRLQAQIAQLRSEIAALEEKIERLKEAKTKLDAEKESLHDKKTKLQGPLNSSESWNGsnennydgirsnletSYQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622996215 592 QLESRLDEILSRIakeTEEIKDLEEQLTEgqiaanealkkdLEGVISGLQEYLGTIK 648
Cdd:pfam16888 81 NYVDELDELIDAI---EEEITRLENQINE------------AQGVIDTLQSQLNSLK 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1355-1604 |
2.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1355 KSKKREERWMRASKRQSEKEMEELHHNIDDLlqEKKSLEC-EVEELHRTVQKRQQQKDFIDGNVESLMTELEIEKSlkhh 1433
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAA--KKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK---- 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1434 ediVDEIECIEKtLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAvnlVKA 1513
Cdd:PTZ00121 1427 ---AEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK---KKA 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1514 DQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKL-----TEELQKLQ--KDIEMAERNEDHHLQV 1586
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdelkkAEELKKAEekKKAEEAKKAEEDKNMA 1579
|
250
....*....|....*...
gi 1622996215 1587 LKESEVLLQAKRAELEKL 1604
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEV 1597
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
620-780 |
2.45e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 620 EGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLeivamdaeNMRKELAEL 699
Cdd:pfam00529 64 EAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDL--------ARRRVLAPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 700 ESALQEQH-EVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQ 778
Cdd:pfam00529 136 GGISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAP 215
|
..
gi 1622996215 779 FS 780
Cdd:pfam00529 216 VD 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
662-1066 |
2.53e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 662 RDEKETLLQRLTEVEQERdqleivamdaENMRKELAELESALQEQHEVNASLQQTQGDLsayEAELEA---RLNL-RDAE 737
Cdd:COG3096 277 ANERRELSERALELRREL----------FGARRQLAEEQYRLVEMARELEELSARESDL---EQDYQAasdHLNLvQTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 738 ANQlkeelEKVTRLtQLEQSALQAELEKERQALknalgkaqfsEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLN- 816
Cdd:COG3096 344 RQQ-----EKIERY-QEDLEELTERLEEQEEVV----------EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDv 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 817 ---------HVVDGLVR-----------PEEVAARVDELRRKLKLGTGEmnihspsdVLGK----SLADLQK-QFSEILA 871
Cdd:COG3096 408 qqtraiqyqQAVQALEKaralcglpdltPENAEDYLAAFRAKEQQATEE--------VLELeqklSVADAARrQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 872 ----------RSK-WERDEAQVRERKLQEEMALQQEKLATGQEEFRQACEralearmnfdkRQHEARIQQMENEIHYLQE 940
Cdd:COG3096 480 lvckiageveRSQaWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLR-----------QQQNAERLLEEFCQRIGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 941 nLKSMEEIqgltDLQLQEADEEKERILAQLREL-----EKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAElti 1015
Cdd:COG3096 549 -LDAAEEL----EELLAELEAQLEELEEQAAEAveqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE--- 620
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 1016 akdQLKSLHGtVMKINQERAEELQEAERFSRKAAQAARDLtraEAEIELLQ 1066
Cdd:COG3096 621 ---ALADSQE-VTAAMQQLLEREREATVERDELAARKQAL---ESQIERLS 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-637 |
2.66e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 454 LDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIqLKKISEAGKDLLYKQLSGRLQLVNKLRQEALD 533
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 534 LELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKdpkhshmkaqKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKD 613
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK----------ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
170 180
....*....|....*....|....
gi 1622996215 614 LEEQLTEGQIAANEALKKDLEGVI 637
Cdd:TIGR04523 650 IKETIKEIRNKWPEIIKKIKESKT 673
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
622-809 |
2.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 622 QIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEivamdaenmrKELAELE- 700
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----------AELAELEk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 701 --SALQEQhevnasLQQTQGDLS-----AYEAELEARLNL-----------------------RDAEANQLKEELEKVTR 750
Cdd:COG4942 91 eiAELRAE------LEAQKEELAellraLYRLGRQPPLALllspedfldavrrlqylkylapaRREQAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622996215 751 LTQL------EQSALQAELEKERQALKNALG-KAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLK 809
Cdd:COG4942 165 LRAEleaeraELEALLAELEEERAALEALKAeRQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
597-705 |
3.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 597 LDEILSRIAKET----EEIKDLEEQLTEGQIAAnEALKKDLEgviSGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRL 672
Cdd:COG0542 395 IDEAAARVRMEIdskpEELDELERRLEQLEIEK-EALKKEQD---EASFERLAELRDELAELEEELEALKARWEAEKELI 470
|
90 100 110
....*....|....*....|....*....|...
gi 1622996215 673 TEVEQERDQLEIVAMDAENMRKELAELESALQE 705
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAE 503
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
585-769 |
3.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 585 IMNKQYQQLESRLDEILSRIAKETEEIKdlEEQLTEGQIAaNEALKKDLEGVISGLQEYLgtikgqatqAQNEcRKLRDE 664
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEE-IHKLRNEFEKELRERRNEL---------QKLE-KRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 665 KETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQE-QHEVNASLQQtqgdLSAYEAElEARLNLRDaeanQLKE 743
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQELER----ISGLTAE-EAKEILLE----KVEE 165
|
170 180
....*....|....*....|....*...
gi 1622996215 744 EL--EKVTRLTQLEQsalQAELEKERQA 769
Cdd:PRK12704 166 EArhEAAVLIKEIEE---EAKEEADKKA 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1340-1480 |
4.28e-03 |
|
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: 41.98 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1340 LENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVES 1419
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 1420 LmtELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELScTKEKTKNAVE 1480
Cdd:TIGR02169 446 K--ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASE 503
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
457-790 |
4.37e-03 |
|
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: 41.88 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 457 QLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLEL 536
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 537 QMEKQKQEIAGKQKEikdlqiaidsldskdpKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEE 616
Cdd:pfam02463 777 AEEREKTEKLKVEEE----------------KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 617 QLTEGQIAANEALKKDLEGVISGLQEYLgtiKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKEL 696
Cdd:pfam02463 841 ELKEEQKLEKLAEEELERLEEEITKEEL---LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 697 AELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGK 776
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
330
....*....|....
gi 1622996215 777 AQFSEEKEQENSEL 790
Cdd:pfam02463 998 ERLEEEKKKLIRAI 1011
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
464-835 |
4.68e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 464 KISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQ 543
Cdd:COG5185 202 GTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 544 EIAGKQkeIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQqlDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQI 623
Cdd:COG5185 282 ENANNL--IKQFENTKEKIAEYTKSIDIKKATESLEEQ--LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 624 AANEALK-KDLEGVISGLQEYLGTIKGQA--------TQAQNECRKLRDEKETLLQRLTEVEQERDQL--EIVAMDAEN- 691
Cdd:COG5185 358 AIKEEIEnIVGEVELSKSSEELDSFKDTIestkesldEIPQNQRGYAQEILATLEDTLKAADRQIEELqrQIEQATSSNe 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 692 -MRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDA--EANQLKEELEKVTRLTQLEQSALQAELEKERQ 768
Cdd:COG5185 438 eVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLneELTQIESRVSTLKATLEKLRAKLERQLEGVRS 517
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 769 ALK------NALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDEL 835
Cdd:COG5185 518 KLDqvaeslKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPI 590
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
639-1070 |
4.73e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 41.49 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 639 GLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQG 718
Cdd:COG4995 14 LAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 719 DLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKA-QFSEEKEQENSELHAKLKHL 797
Cdd:COG4995 94 LALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAAlAAAAAAAAAAALLALALALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 798 QDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWER 877
Cdd:COG4995 174 AAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 878 DEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQ 957
Cdd:COG4995 254 AAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 958 EADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEE 1037
Cdd:COG4995 334 ALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLL 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622996215 1038 LQEAERFSRKAAQAARDLT-----------RAEAEIELLQNLLR 1070
Cdd:COG4995 414 AALALLLALAAYAAARLALlalieyiilpdRLYAFVQLYQLLIA 457
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
410-808 |
4.83e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 410 SRYKRNMFATESYIidsaQAVQIKKMEPDEQLRNDHMNLRGHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQ----- 484
Cdd:pfam05557 114 SELRRQIQRAELEL----QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseiv 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 485 --------QILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSG---RLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIK 553
Cdd:pfam05557 190 knskselaRIPELEKELERLREHNKHLNENIENKLLLKEEVEDlkrKLEREEKYREEAATLELEKEKLEQELQSWVKLAQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 554 DLQIAIDSLDSkdpkhshmkaqksgkeqqldimnkqyqqLESRLDEILSRIAKETEEIKDLEEQLtegqiaanealkKDL 633
Cdd:pfam05557 270 DTGLNLRSPED----------------------------LSRRIEQLQQREIVLKEENSSLTSSA------------RQL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 634 EGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVamdAENMRKELAELESALQEQHEVNASL 713
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI---LESYDKELTMSNYSPQLLERIEEAE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 714 QQTQgDLSAYEAELEARLNLRDAEANQLKEELekvtrltqleqSALQAELEKERQalKNALGKAQFSEEK----EQENSE 789
Cdd:pfam05557 387 DMTQ-KMQAHNEEMEAQLSVAEEELGGYKQQA-----------QTLERELQALRQ--QESLADPSYSKEEvdslRRKLET 452
|
410
....*....|....*....
gi 1622996215 790 LHAKLKHLQDDNNLLKQQL 808
Cdd:pfam05557 453 LELERQRLREQKNELEMEL 471
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
656-793 |
5.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 656 NECRKLRDEKETLLQRLTEVEQE----RDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQG------DLSAYEA 725
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDElaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622996215 726 ELE-ARLNLRDAEANQL-----KEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAK 793
Cdd:COG1579 97 EIEsLKRRISDLEDEILelmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
805-1083 |
5.53e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 805 KQQLKDFQNHLNHVVDGLvrpEEVAARVDELrrklklgtgEMNIHSPSDVLGKSLADLQKQfsEILARSKWERDEAQVRE 884
Cdd:COG3096 298 RRQLAEEQYRLVEMAREL---EELSARESDL---------EQDYQAASDHLNLVQTALRQQ--EKIERYQEDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 885 RKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENeIHYlQENLKSMEEIQGLTDL---------- 954
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRA-IQY-QQAVQALEKARALCGLpdltpenaed 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 955 QLQEADEEKERILAQLRELEKKKKLED-AKSQ-EQVFgldKELKKLKKAVATSDKLATA-ELTIAKDQLKSLHGTVMKIN 1031
Cdd:COG3096 442 YLAAFRAKEQQATEEVLELEQKLSVADaARRQfEKAY---ELVCKIAGEVERSQAWQTArELLRRYRSQQALAQRLQQLR 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622996215 1032 QE------RAEELQEAER----FSRKAAQ---AARDLT----RAEAEIELLQNLLRQKGEQfRLEMEKT 1083
Cdd:COG3096 519 AQlaeleqRLRQQQNAERlleeFCQRIGQqldAAEELEellaELEAQLEELEEQAAEAVEQ-RSELRQQ 586
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
609-792 |
6.00e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 609 EEIKDLEEQLT-----EGQIAANEALKKDLEGVISGLQEylGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLE 683
Cdd:pfam05701 233 EELQRLNQQLLsakdlKSKLETASALLLDLKAELAAYME--SKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 684 IVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNL--RDAEANQLKEE--LEKVTRL-TQLEQSA 758
Cdd:pfam05701 311 KAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAELNRtkSEIALVQAKEKeaREKMVELpKQLQQAA 390
|
170 180 190
....*....|....*....|....*....|....*
gi 1622996215 759 LQAELEKER-QALKNALGKAQfsEEKEQENSELHA 792
Cdd:pfam05701 391 QEAEEAKSLaQAAREELRKAK--EEAEQAKAAAST 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1382-1603 |
6.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1382 IDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLmtELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLL 1461
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1462 AEAESELSctkEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVnLVKADQ-QLRSLQADAKDLEQHKIKQEEILKE 1540
Cdd:COG4942 100 EAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARReQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622996215 1541 INKIVAAKDSDfqclSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEK 1603
Cdd:COG4942 176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1345-1549 |
6.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1345 SRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTEL 1424
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1425 -------------EIEKSLKHHEDIVDEI------ECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDA 1485
Cdd:COG4942 107 aellralyrlgrqPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622996215 1486 KRSLLQTESDAEELERRAQEtavNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKD 1549
Cdd:COG4942 187 RAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
526-1070 |
6.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 526 KLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDskdpkhsHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIA 605
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNID-------YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 606 KETEEIKDLEEQLtegqIAANEALKK--DLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETL--------------- 668
Cdd:PRK01156 222 RLSIEYNNAMDDY----NNLKSALNElsSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHmkiindpvyknrnyi 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 669 ------------------------------LQRLTEVEQERDQLEIVAMDAENMRKELAELE-------SALQEQHEVNA 711
Cdd:PRK01156 298 ndyfkykndienkkqilsnidaeinkyhaiIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynSYLKSIESLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 712 SLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALqAELEKERQALKNALGKAQFSEEKEQENSELH 791
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV-SSLNQRIRALRENLDELSRNMEMLNGQSVCP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 792 AKLKHLQDDNNllKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLK-----LGTGEMNIHSPSDVLGKSLADLQKQF 866
Cdd:PRK01156 457 VCGTTLGEEKS--NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeyLESEEINKSINEYNKIESARADLEDI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 867 SEILARSKWERDEAqvrERKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSME 946
Cdd:PRK01156 535 KIKINELKDKHDKY---EEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 947 EIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDaKSQEQVfGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGT 1026
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-KLRGKI-DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA 689
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622996215 1027 VMKINQERAEE-------LQEAERFSRKAAQAARDLTRAEAEIELLQNLLR 1070
Cdd:PRK01156 690 LDDAKANRARLestieilRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
657-989 |
6.72e-03 |
|
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: 41.26 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 657 ECRKLRDEKETLLQrltEVEQERdQLEivamDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDA 736
Cdd:pfam17380 297 EQERLRQEKEEKAR---EVERRR-KLE----EAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 737 EANQLKEELEKVTRLT------------QLEQSALQAELEKERQALKNALGKAQFSEEKEQENSElHAKLKHLQDDNNLL 804
Cdd:pfam17380 369 EIAMEISRMRELERLQmerqqknervrqELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 805 KQQLKDFQNHLNHVVDGLVRPEEvaarvDELRRKLKlgtgemnihspsdvlgksladlqkqfseiLARSKWERDEAQVRE 884
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEE-----ERKRKKLE-----------------------------LEKEKRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 885 RKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEiqgltdlQLQEADEEKE 964
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE-------QMRKATEERS 566
|
330 340
....*....|....*....|....*
gi 1622996215 965 RILAQLRELEKKKKLEDAKSQEQVF 989
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1488-1608 |
6.88e-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: 41.20 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1488 SLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQ 1567
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622996215 1568 KLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKSQV 1608
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
538-1141 |
7.00e-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: 41.19 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 538 MEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEI----------LSRIAKE 607
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLknrlkeiehnLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 608 TEEIKDLEEQLTEGQiAANEALKKDLEGVISGLQEYLGTI-----------KGQATQAQNECRKLRDEKETLLQRLTE-- 674
Cdd:TIGR00606 268 DNEIKALKSRKKQME-KDNSELELKMEKVFQGTDEQLNDLyhnhqrtvrekERELVDCQRELEKLNKERRLLNQEKTEll 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 675 VEQERDQLEIVAMDAENMRKELAELESALQEQ-----------------HEVNASLQQTQGDLSAYE-AELEARLNLRDA 736
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserqiknfHTLVIERQEDEAKTAAQLcADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 737 EANQLKEELEKVTRLTQLEQSAL---QAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNL--LKQQLKDF 811
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetLKKEVKSL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 812 QNHlnhvvdglvrpeevAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEM 891
Cdd:TIGR00606 507 QNE--------------KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 892 ALQQEKLATGQEEFRQACERAleARMNFDKRQHEARIQQMENEIHYLQENLKSMEEiqGLTDLQLQEADEEK-ERILAQL 970
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRL--AKLNKELASLEQNKNHINNELESKEEQLSSYED--KLFDVCGSQDEESDlERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 971 RELEKKKKLEDAKSQ--EQVFGLDKELKKLKKAVATSDKLATAELT-----------IAKDQLKSLHGTVMKINQERAEE 1037
Cdd:TIGR00606 649 EKSSKQRAMLAGATAvySQFITQLTDENQSCCPVCQRVFQTEAELQefisdlqsklrLAPDKLKSTESELKKKEKRRDEM 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1038 LQEAE-------RFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEI 1110
Cdd:TIGR00606 729 LGLAPgrqsiidLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
650 660 670
....*....|....*....|....*....|.
gi 1622996215 1111 ArlQNVLDLTGSDNKGGFENVLEEIAELRRE 1141
Cdd:TIGR00606 809 A--QQAAKLQGSDLDRTVQQVNQEKQEKQHE 837
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
581-981 |
7.31e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 581 QQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQ---------------IAANEALKKDLEGVISGLQ---- 641
Cdd:PRK10246 426 QRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRqrykektqqladvktICEQEARIKDLEAQRAQLQagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 642 ------------EYLGTIKGQATQA-----QNECRKLRDEKETLLQRLTEVEQERDQleivamdAENMRKELAELESAL- 703
Cdd:PRK10246 506 cplcgstshpavEAYQALEPGVNQSrldalEKEVKKLGEEGAALRGQLDALTKQLQR-------DESEAQSLRQEEQALt 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 704 QEQHEVNASL---QQTQGDLSAYEAELEAR------LNLRDAEANQLKEELEKVTRLTQleqsalqaELEKERQALKNAL 774
Cdd:PRK10246 579 QQWQAVCASLnitLQPQDDIQPWLDAQEEHerqlrlLSQRHELQGQIAAHNQQIIQYQQ--------QIEQRQQQLLTAL 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 775 GKAQFS-EEKEQENSELHAK------LKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVA-ARVDELRrklKLGTGEM 846
Cdd:PRK10246 651 AGYALTlPQEDEEASWLATRqqeaqsWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEEtVALDNWR---QVHEQCL 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 847 NIHSPSDVLGK-------SLADLQKQFSEILARSKWER----------DEAQVRERKLQEEMALQQEKLATGQEEFRQAC 909
Cdd:PRK10246 728 SLHSQLQTLQQqdvleaqRLQKAQAQFDTALQASVFDDqqaflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQAL 807
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622996215 910 ERALEARMNFdkRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLED 981
Cdd:PRK10246 808 AQHQQHRPDG--LDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1336-1610 |
7.50e-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: 40.86 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1336 EHHNLENEVSRLEDIMQHLKSKKR--EERWMRASK------RQSEKEMEELH-----HNIddLLQEKKSLECEVEELHRT 1402
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKticqltEEKEAQMEELNkakaaHSF--VVTEFEATTCSLEELLRT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1403 VQKRQQQKDfidGNVESLMTELEIEKSlkhhedivdEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEkf 1482
Cdd:pfam05483 368 EQQRLEKNE---DQLKIITMELQKKSS---------ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1483 TDAKRSLLQTESDAEELERRAQETAVNLVKADQQ--LRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSdfqcLSKKKE 1560
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEhyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE----LTQEAS 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1561 KLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKSQVWQ 1610
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ 559
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
458-1081 |
7.95e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 458 LEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQL-KKIS---------EAGKDLL--YKQLSGRLQLVN 525
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvCKIAgeversqawQTARELLrrYRSQQALAQRLQ 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 526 KLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIA 605
Cdd:COG3096 516 QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 606 KETE---EIKDLEEQLTEGQIAANEALKkDLEGVISGLQeylgtikgqaTQAQNEcRKLRDEKETLLQRLTEVEQERDQL 682
Cdd:COG3096 596 ELAArapAWLAAQDALERLREQSGEALA-DSQEVTAAMQ----------QLLERE-REATVERDELAARKQALESQIERL 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 683 E-----------------------------------------------IVAMDAENMRKELAELESALQEqhevnasLQQ 715
Cdd:COG3096 664 SqpggaedprllalaerlggvllseiyddvtledapyfsalygparhaIVVPDLSAVKEQLAGLEDCPED-------LYL 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 716 TQGDLSAYEAelearlNLRDAEanqlkeELEKvTRLTQLEQSALQAELEKE-----RQALKNALgkAQFSEEKEQEnSEL 790
Cdd:COG3096 737 IEGDPDSFDD------SVFDAE------ELED-AVVVKLSDRQWRYSRFPEvplfgRAAREKRL--EELRAERDEL-AEQ 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 791 HAKLKHLQDDNNLLKQQLKDF-QNHLNHVVDGlvRPEEVAArvdELRRKLKLGTGEMNIHspsdvlgkslADLQKQFSEI 869
Cdd:COG3096 801 YAKASFDVQKLQRLHQAFSQFvGGHLAVAFAP--DPEAELA---ALRQRRSELERELAQH----------RAQEQQLRQQ 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 870 LARSKwerdEAQVRERKLQEEMA-LQQEKLATGQEEFRQACERALEARmNFdKRQHEARIQQMENEIHYLQENLKSMEEI 948
Cdd:COG3096 866 LDQLK----EQLQLLNKLLPQANlLADETLADRLEELREELDAAQEAQ-AF-IQQHGKALAQLEPLVAVLQSDPEQFEQL 939
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 949 QgltdLQLQEADEEKERILAQLrelekkKKLEDAKSQEQVFGLDKELKKLKKAVATSDKL------ATAELTIAKDQLKS 1022
Cdd:COG3096 940 Q----ADYLQAKEQQRRLKQQI------FALSEVVQRRPHFSYEDAVGLLGENSDLNEKLrarleqAEEARREAREQLRQ 1009
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 1023 LHGTVMKINQERA----------EELQEAER--------FSRKAAQAARD----------------------LTRAEAEI 1062
Cdd:COG3096 1010 AQAQYSQYNQVLAslkssrdakqQTLQELEQeleelgvqADAEAEERARIrrdelheelsqnrsrrsqlekqLTRCEAEM 1089
|
730
....*....|....*....
gi 1622996215 1063 ELLQNLLRQKGEQFRLEME 1081
Cdd:COG3096 1090 DSLQKRLRKAERDYKQERE 1108
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
517-784 |
8.33e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 517 LSGRLQLVNKLRQEALDLELQME--------KQKQEIAGKQKEIKD----LQIAIDSLDSKDPKHSHMKAQ--------- 575
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEaefnqkraKFKELYLAKEEDLKRqnavLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 576 --KSGKEQQLDIMNKQYQQLESRLDEILSRIAKETE-----------------------EIKDLEEQLTEGQIAAN--EA 628
Cdd:pfam03528 86 vsENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEvqfhrrleqeraqwnqyresaerEIADLRRRLSEGQEEENleDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 629 LKK------DLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQE-RDQLE-----------IVAMDAE 690
Cdd:pfam03528 166 MKKaqedaeKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAEKScRTDLEmyvavlntqksVLQEDAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 691 NMRKELAELESALQEQHEVNASLQQTQGdlSAYEAELEA-RLNLRDAeanQLKEELEKVTRLTQLEQSALQAELEKERQA 769
Cdd:pfam03528 246 KLRKELHEVCHLLEQERQQHNQLKHTWQ--KANDQFLESqRLLMRDM---QRMESVLTSEQLRQVEEIKKKDQEEHKRAR 320
|
330
....*....|....*
gi 1622996215 770 LKNALGKAQFSEEKE 784
Cdd:pfam03528 321 THKEKETLKSDREHT 335
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
674-797 |
8.87e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622996215 674 EVEQERDQLEIVAMDAENMRKELAELESALQEQ----HEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEEL--EK 747
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEEaessREQLQELEEQLATERSARREAEAELERLQEELRYLEEELrrSK 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622996215 748 VTRLTQLEQsaLQAELEKERQALKNalgKAQFSEEKeqenSELHAKLKHL 797
Cdd:pfam09787 135 ATLQSRIKD--REAEIEKLRNQLTS---KSQSSSSQ----SELENRLHQL 175
|
|
| |
