|
Name |
Accession |
Description |
Interval |
E-value |
| SID |
pfam11778 |
Septation initiation; This family is required for activation of the spg1 GTPase signalling ... |
655-789 |
6.81e-48 |
|
Septation initiation; This family is required for activation of the spg1 GTPase signalling cascade which leads to the initiation of septation and the subsequent termination of mitosis. It may act as a scaffold at the spindle pole body to which other components of the spg1 signalling cascade attach in pombe. In S.cerevisiae it is both required for the proper formation of the spindle pole body outer plaque and may also connect the outer plaque to the central plaque embedded in the nuclear envelope.
Pssm-ID: 403090 Cd Length: 135 Bit Score: 165.84 E-value: 6.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 655 LKKLYGDPSTELNFETVGKSFPHITKEKYDSLGLDILTDLTYVQSQNLIKNLLIVLDIPLKTFLKIVPTIVIQLRCELTL 734
Cdd:pfam11778 1 LKKLEGDKSEKITFENLKKSRPGITKELYETLMVDKVDSLDLVELQNIVKNLILLLEIPFSKLTKKLPLIAIYLKYERPI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 330443493 735 LTKFANDLNLKVFGKQLDFKSRRKVAMNEFLNNHDIAEVKHPLEYDLQALFKYFF 789
Cdd:pfam11778 81 LLKFANRLHYQLFNEPIDFKRFTNEAYEQYLKTHDLNEINHPLEDCLEELYNEIA 135
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-658 |
3.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 196 ESLEENIEVahLENVFRSSKTPDEEQSEYMKLGEIRLSSSSYGGSISKE--------NSLPKVLDELQSQNEEIKALRQK 267
Cdd:PRK03918 269 EELKKEIEE--LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlsrleeeiNGIEERIKELEEKEERLEELKKK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 268 LEEKDDRIQELEE---LNSMNDAKLQRIEDLQKEFHNERKAASKR----LNIVQDRFRKEIKKIREEKITDFQNKNASKK 340
Cdd:PRK03918 347 LKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGLTPEKLEKeleeLEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 341 EKNEVTSAKTKCKAFSQrniLVSELYRkqKQILNlqqendKFLKDINESNNSIVKLRSEVEILKSNLQLSQDENKKlhdn 420
Cdd:PRK03918 427 AIEELKKAKGKCPVCGR---ELTEEHR--KELLE------EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK---- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 421 gsfyEKRLNDVYSYMQNLSLFEKDLGKFILEEMKcghspsmfqngfaKLYPDFQDIKnlenmEQYKQLKGKIELLEKnDR 500
Cdd:PRK03918 492 ----ESELIKLKELAEQLKELEEKLKKYNLEELE-------------KKAEEYEKLK-----EKLIKLKGEIKSLKK-EL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 501 IRLEKIISVFKLINERLHFMQQQHSHKIKYLQKEALTKEQQF-----RLEK--RRWHDILNLKEEnfqkLKSELKEKLIL 573
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerlkELEPfyNEYLELKDAEKE----LEREEKELKKL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 574 SEKIQKnAEDKLNDYMNEHQEIVEKLQnqaliasrwSTQIQESENTHKKITDELAGKQSEILKLEETILSLKEDVFQEKL 653
Cdd:PRK03918 625 EEELDK-AFEELAETEKRLEELRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
....*
gi 330443493 654 NLKKL 658
Cdd:PRK03918 695 TLEKL 699
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
251-639 |
4.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 251 LDELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQK--EFHNERKAASKRLNIVQDRFRKEIKKIREEK 328
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 329 itdfQNKNASKKEKNEVTSAKTKCKAfsqrnILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQ 408
Cdd:COG4717 160 ----ELEEELEELEAELAELQEELEE-----LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 409 LSQDENKKLHDNGSFYEKR---------LNDVYSYMQNLSLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDFQDIKNL 479
Cdd:COG4717 231 QLENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 480 ENMEQYKQ--LKGKIELLEKNDRIRLEKIISVFKLInERLHFMQQQHSHKIKYLQKEALTKEQQFRLEKRRWHDilnlkE 557
Cdd:COG4717 311 PALEELEEeeLEELLAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQLEELEQEIAALLAEAGVED-----E 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 558 ENFQKLKSELKEKLILSEKIQkNAEDKLNDYMNEHQEIVEKLQNQALIA--SRWSTQIQESENTHKKITDELAGKQSEIL 635
Cdd:COG4717 385 EELRAALEQAEEYQELKEELE-ELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAELEAELE 463
|
....
gi 330443493 636 KLEE 639
Cdd:COG4717 464 QLEE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-428 |
2.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 252 DELQSQNEEIKALRQKLEEKDDRIQELEE-LNSMNDAKL---QRIEDLQKEFHNERKAASK---RLNIVQDRFR---KEI 321
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEkLEELRLEVSeleEEIEELQKELYALANEISRleqQKQILRERLAnleRQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 322 KKIREEKITDFQNKNASKKEKNEV----TSAKTKCKAFSQRNILVSELYRKQKQILNLQQEN-DKFLKDINESNNSIVKL 396
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELeeklEELKEELESLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASL 398
|
170 180 190
....*....|....*....|....*....|..
gi 330443493 397 RSEVEILKSNLQLSQDENKKLHDNGSFYEKRL 428
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
252-413 |
1.53e-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: 42.03 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 252 DELQSQNEEIKALRQKLEEKDDRI----QELEELNSM-----NDAKLQRIE--DLQKEFhNERKAASKRLNIVQDRFRKE 320
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLvgqhgRTAGAMQVEkaQLEKEI-NDRRLELQEFKILKDKKDAK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 321 IKKIrEEKITDFQnknaskKEKNEVTSAKtkckafsqrnilvSELYRKQKQIlnlQQENDKFLKDINESNNSIVKLRSEV 400
Cdd:pfam15921 620 IREL-EARVSDLE------LEKVKLVNAG-------------SERLRAVKDI---KQERDQLLNEVKTSRNELNSLSEDY 676
|
170
....*....|...
gi 330443493 401 EILKSNLQLSQDE 413
Cdd:pfam15921 677 EVLKRNFRNKSEE 689
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SID |
pfam11778 |
Septation initiation; This family is required for activation of the spg1 GTPase signalling ... |
655-789 |
6.81e-48 |
|
Septation initiation; This family is required for activation of the spg1 GTPase signalling cascade which leads to the initiation of septation and the subsequent termination of mitosis. It may act as a scaffold at the spindle pole body to which other components of the spg1 signalling cascade attach in pombe. In S.cerevisiae it is both required for the proper formation of the spindle pole body outer plaque and may also connect the outer plaque to the central plaque embedded in the nuclear envelope.
Pssm-ID: 403090 Cd Length: 135 Bit Score: 165.84 E-value: 6.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 655 LKKLYGDPSTELNFETVGKSFPHITKEKYDSLGLDILTDLTYVQSQNLIKNLLIVLDIPLKTFLKIVPTIVIQLRCELTL 734
Cdd:pfam11778 1 LKKLEGDKSEKITFENLKKSRPGITKELYETLMVDKVDSLDLVELQNIVKNLILLLEIPFSKLTKKLPLIAIYLKYERPI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 330443493 735 LTKFANDLNLKVFGKQLDFKSRRKVAMNEFLNNHDIAEVKHPLEYDLQALFKYFF 789
Cdd:pfam11778 81 LLKFANRLHYQLFNEPIDFKRFTNEAYEQYLKTHDLNEINHPLEDCLEELYNEIA 135
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-658 |
3.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 196 ESLEENIEVahLENVFRSSKTPDEEQSEYMKLGEIRLSSSSYGGSISKE--------NSLPKVLDELQSQNEEIKALRQK 267
Cdd:PRK03918 269 EELKKEIEE--LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlsrleeeiNGIEERIKELEEKEERLEELKKK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 268 LEEKDDRIQELEE---LNSMNDAKLQRIEDLQKEFHNERKAASKR----LNIVQDRFRKEIKKIREEKITDFQNKNASKK 340
Cdd:PRK03918 347 LKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGLTPEKLEKeleeLEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 341 EKNEVTSAKTKCKAFSQrniLVSELYRkqKQILNlqqendKFLKDINESNNSIVKLRSEVEILKSNLQLSQDENKKlhdn 420
Cdd:PRK03918 427 AIEELKKAKGKCPVCGR---ELTEEHR--KELLE------EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK---- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 421 gsfyEKRLNDVYSYMQNLSLFEKDLGKFILEEMKcghspsmfqngfaKLYPDFQDIKnlenmEQYKQLKGKIELLEKnDR 500
Cdd:PRK03918 492 ----ESELIKLKELAEQLKELEEKLKKYNLEELE-------------KKAEEYEKLK-----EKLIKLKGEIKSLKK-EL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 501 IRLEKIISVFKLINERLHFMQQQHSHKIKYLQKEALTKEQQF-----RLEK--RRWHDILNLKEEnfqkLKSELKEKLIL 573
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerlkELEPfyNEYLELKDAEKE----LEREEKELKKL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 574 SEKIQKnAEDKLNDYMNEHQEIVEKLQnqaliasrwSTQIQESENTHKKITDELAGKQSEILKLEETILSLKEDVFQEKL 653
Cdd:PRK03918 625 EEELDK-AFEELAETEKRLEELRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
....*
gi 330443493 654 NLKKL 658
Cdd:PRK03918 695 TLEKL 699
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
251-639 |
4.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 251 LDELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQK--EFHNERKAASKRLNIVQDRFRKEIKKIREEK 328
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 329 itdfQNKNASKKEKNEVTSAKTKCKAfsqrnILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQ 408
Cdd:COG4717 160 ----ELEEELEELEAELAELQEELEE-----LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 409 LSQDENKKLHDNGSFYEKR---------LNDVYSYMQNLSLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDFQDIKNL 479
Cdd:COG4717 231 QLENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 480 ENMEQYKQ--LKGKIELLEKNDRIRLEKIISVFKLInERLHFMQQQHSHKIKYLQKEALTKEQQFRLEKRRWHDilnlkE 557
Cdd:COG4717 311 PALEELEEeeLEELLAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQLEELEQEIAALLAEAGVED-----E 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 558 ENFQKLKSELKEKLILSEKIQkNAEDKLNDYMNEHQEIVEKLQNQALIA--SRWSTQIQESENTHKKITDELAGKQSEIL 635
Cdd:COG4717 385 EELRAALEQAEEYQELKEELE-ELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAELEAELE 463
|
....
gi 330443493 636 KLEE 639
Cdd:COG4717 464 QLEE 467
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-428 |
2.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 252 DELQSQNEEIKALRQKLEEKDDRIQELEE-LNSMNDAKL---QRIEDLQKEFHNERKAASK---RLNIVQDRFR---KEI 321
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEkLEELRLEVSeleEEIEELQKELYALANEISRleqQKQILRERLAnleRQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 322 KKIREEKITDFQNKNASKKEKNEV----TSAKTKCKAFSQRNILVSELYRKQKQILNLQQEN-DKFLKDINESNNSIVKL 396
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELeeklEELKEELESLEAELEELEAELEELESRLEELEEQlETLRSKVAQLELQIASL 398
|
170 180 190
....*....|....*....|....*....|..
gi 330443493 397 RSEVEILKSNLQLSQDENKKLHDNGSFYEKRL 428
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
191-327 |
7.95e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 191 YVVSNESLEENIEVAhlenvfRSSKTPDEEQSEYMklgEIRLSSSSYGGSISKENSLPKVLDELQSQNEEikaLRQKLEE 270
Cdd:COG2433 371 RVIRGLSIEEALEEL------IEKELPEEEPEAER---EKEHEERELTEEEEEIRRLEEQVERLEAEVEE---LEAELEE 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 330443493 271 KDDRIQELEElnsmndaKLQRIEDLQKEFHNERKAASKRLNIVqDRFRKEIKKIREE 327
Cdd:COG2433 439 KDERIERLER-------ELSEARSEERREIRKDREISRLDREI-ERLERELEEERER 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-520 |
6.91e-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: 46.59 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 244 ENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEELNsmnDAKLQRIEDLQ---KEFHNERKAASKRLNIVQDRFRKE 320
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL---AEAEAEIEELEaqiEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 321 IKKIRE--EKITDFQNKNASKKEKNEVTSAKTKcKAFSQRNILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRS 398
Cdd:TIGR02168 816 NEEAANlrERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 399 EVEILKSNLQLSQDENKKLHDNGSFYEKRLNDVYSYMQNL-----SLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDF 473
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevridNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443493 474 QDIK---------NLENMEQYKQLKGKIELLEKND------RIRLEKIIS------------VFKLINERLHFM 520
Cdd:TIGR02168 975 KRLEnkikelgpvNLAAIEEYEELKERYDFLTAQKedlteaKETLEEAIEeidrearerfkdTFDQVNENFQRV 1048
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
243-417 |
8.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 243 KENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEElnSMNDAKlQRIEDLQKEFHNERKAASKRLNIVQDRFRkeik 322
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--ELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 323 kireekitDFQNKNASKKEKNEVTSAKTkCKAFSQRNILVSELYRKQKQILN----LQQENDKFLKDINESNNSIVKLRS 398
Cdd:COG3883 94 --------ALYRSGGSVSYLDVLLGSES-FSDFLDRLSALSKIADADADLLEelkaDKAELEAKKAELEAKLAELEALKA 164
|
170
....*....|....*....
gi 330443493 399 EVEILKSNLQLSQDENKKL 417
Cdd:COG3883 165 ELEAAKAELEAQQAEQEAL 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-430 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 244 ENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRFRKEIKK 323
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 324 IREEKITDFQNKNASKKEKNEVTSAKTKCKAFSQRNI-LVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEI 402
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180
....*....|....*....|....*...
gi 330443493 403 LKSNLQLSQDENKKLHDNGSFYEKRLND 430
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-651 |
1.23e-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: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 262 KALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLNivqdRFRKEIKKIREEkitdfQNKNASKKE 341
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQE-----EEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 342 KNEvtsaktkckafsqrnilvSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILK-----SNLQLSQDENKK 416
Cdd:TIGR02169 741 ELE------------------EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 417 LHDNGSFYEKRLNDVysymqNLSLFEKDLGKFILEEMKcghspsmfqngfAKLYPDFQDIKNLENMEQYKQLKGKIELLE 496
Cdd:TIGR02169 803 LEEEVSRIEARLREI-----EQKLNRLTLEKEYLEKEI------------QELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 497 KNDRIRlEKIISVFKLINERLHFMQQQHSHKIKYlqKEALTKEQQFRLEKRRWHDILNLKEENFQKLKSELK--EKLILS 574
Cdd:TIGR02169 866 LEEELE-ELEAALRDLESRLGDLKKERDELEAQL--RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiEDPKGE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 575 EKIQKNAEDKLNDYMNEHQEIVEKLQNQALIASRwstQIQESENTHKKItDELAGKQ-------SEILKLEETILSLKED 647
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQRVEEEIRALEPVNML---AIQEYEEVLKRL-DELKEKRakleeerKAILERIEEYEKKKRE 1018
|
....
gi 330443493 648 VFQE 651
Cdd:TIGR02169 1019 VFME 1022
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
245-648 |
1.96e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 245 NSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEelNSMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRFRKEIKKI 324
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK--SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKII 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 325 REEKitdfQNKNASKKEKNEVTSAKTKckafsqrniLVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILK 404
Cdd:TIGR04523 338 SQLN----EQISQLKKELTNSESENSE---------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 405 SNLQLSQDENKKLHDNGSFYEKRLNDVYSYMQNLSLFEKDLGKFIleemkcghspSMFQNGFAKL--YPDFQDIKNLENM 482
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD----------SVKELIIKNLdnTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 483 EQYKQLKGKIELLEKNDRIR---LEKIISVFKLINERLHFMQQQHS---HKIKYLQKEALTKEQQFR-LEKRRWHDILNL 555
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKekeLKKLNEEKKELEEKVKDLTKKISslkEKIEKLESEKKEKESKISdLEDELNKDDFEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 556 KEENFQKLK-------SELKEKLILSEKIQKNAEDKLNDYMNEHQEIVEKLQNQALIASRWSTQIQESENTHKKITDELA 628
Cdd:TIGR04523 555 KKENLEKEIdeknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
410 420
....*....|....*....|
gi 330443493 629 GKQSEILKLEETILSLKEDV 648
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETI 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-417 |
2.90e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 253 ELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLnivqDRFRKEIKKIREEKITDF 332
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 333 QNKNASKKEKNEVTSAKTKCKAfsQRNILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQLSQD 412
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEA--ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
....*
gi 330443493 413 ENKKL 417
Cdd:COG1196 415 RLERL 419
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-420 |
7.65e-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: 43.13 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 202 IEVAHLENvfRSSKTPDEEQSEYMKLGEIRLSSSSYGGSISKENSLPKVL-DELQSQNEEIKALRQKLEEKDDRIQELEE 280
Cdd:TIGR02169 695 SELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeEDLSSLEQEIENVKSELKELEARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 281 --------LN----SMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRFRKE--IKKIREEKITDFQNKNASKKEK---- 342
Cdd:TIGR02169 773 dlhkleeaLNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQiksi 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 343 -NEVTSAKTKCKAFSQR--------NILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQLSQDE 413
Cdd:TIGR02169 853 eKEIENLNGKKEELEEEleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
....*..
gi 330443493 414 NKKLHDN 420
Cdd:TIGR02169 933 LSEIEDP 939
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-377 |
1.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 244 ENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEElnSMNDAKLQRIEDLQKEFHNERKAASKRLNiVQDRFRKEIKK 323
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEA--QIRGNGGDRLEQLEREIERLERELEERER-RRARLEALLAA 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330443493 324 IREEKITD---FQ-NKNASKKEKNEVTSAKTKC-----KAFSQRNILVSELYRKQKQILNLQQ 377
Cdd:COG4913 371 LGLPLPASaeeFAaLRAEAAALLEALEEELEALeealaEAEAALRDLRRELRELEAEIASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
253-658 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 253 ELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRFRK---EIKKIREEKI 329
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnsDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 330 TDFQNKNASKKEKNEVTSAKTKCKAfsqrnilvsELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQL 409
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKK---------NIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 410 SQDENKKLHDNGSFYEKRLNDVYSYMQNLSLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDFQDIKNL------ENME 483
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 484 QYKQLKGKIELLEKNDRIRLEKIISVFKLINERLHFMQQQHSHKIKYLQKEALTKEQQFRLEKRRW-----------HDI 552
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIsqnnkiisqlnEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 553 LNLKEE------NFQKLKSELKEKLILSEKIQKNAEDKLNDYMNEHQEIVE---KLQNQALIASRWSTQIQESENTHKKI 623
Cdd:TIGR04523 345 SQLKKEltnsesENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDlesKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430
....*....|....*....|....*....|....*
gi 330443493 624 TDELAGKQSEILKLEETILSLKEDVFQEKLNLKKL 658
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
252-413 |
1.53e-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: 42.03 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 252 DELQSQNEEIKALRQKLEEKDDRI----QELEELNSM-----NDAKLQRIE--DLQKEFhNERKAASKRLNIVQDRFRKE 320
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLvgqhgRTAGAMQVEkaQLEKEI-NDRRLELQEFKILKDKKDAK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 321 IKKIrEEKITDFQnknaskKEKNEVTSAKtkckafsqrnilvSELYRKQKQIlnlQQENDKFLKDINESNNSIVKLRSEV 400
Cdd:pfam15921 620 IREL-EARVSDLE------LEKVKLVNAG-------------SERLRAVKDI---KQERDQLLNEVKTSRNELNSLSEDY 676
|
170
....*....|...
gi 330443493 401 EILKSNLQLSQDE 413
Cdd:pfam15921 677 EVLKRNFRNKSEE 689
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-417 |
2.96e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 252 DELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRfRKEIKKIREEKITD 331
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 332 FQNKNASKKEKNEVTSAKTkckafSQRNILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQLSQ 411
Cdd:COG1196 353 LEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*.
gi 330443493 412 DENKKL 417
Cdd:COG1196 428 EALAEL 433
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
253-327 |
4.40e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 4.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443493 253 ELQSQNEEIKALRQKLEEKDDRIQELEElnsmndaKLQRIEDLQKEFHNERKAASKRLnivqDRFRKE-IKKIREE 327
Cdd:COG2433 466 EISRLDREIERLERELEEERERIEELKR-------KLERLKELWKLEHSGELVPVKVV----EKFTKEaIRRLEEE 530
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
474-648 |
4.99e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 474 QDIKNLEnmEQYKQLKGKIELLEKNdrirLEKIISVFKLINErlhfmqqqhshKIKYLQKEALTKEQQFRLeKRRWHDIL 553
Cdd:pfam05667 335 EELEELQ--EQLEDLESSIQELEKE----IKKLESSIKQVEE-----------ELEELKEQNEELEKQYKV-KKKTLDLL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 554 NLKEENFQKLKSELKEkliLSEKIQKNA---EDKLNDYMNEHQEIVEKLQNQALIASRWSTQIQESENTHKKITDELAGK 630
Cdd:pfam05667 397 PDAEENIAKLQALVDA---SAQRLVELAgqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQK 473
|
170
....*....|....*...
gi 330443493 631 QSEILKLEETILSLKEDV 648
Cdd:pfam05667 474 EELYKQLVAEYERLPKDV 491
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
243-354 |
5.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 243 KENSLPKVLDELQSQNEEIKALRQKLEEK----DDRIQELEELNSMNDAKLQRIEDLQKEfhnerKAASKRLNIVQDRFR 318
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKqqelEKKEEELEELIEEQLQELERISGLTAE-----EAKEILLEKVEEEAR 168
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 330443493 319 KE----IKKIREEKitdfqNKNASKKEKNEVTSAKTKCKA 354
Cdd:PRK12704 169 HEaavlIKEIEEEA-----KEEADKKAKEILAQAIQRCAA 203
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
482-603 |
8.15e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443493 482 MEQYKQLKgKIELLEKNDRIRLEkiisVFKLINERLHFMQQQHShkiKYLQKEALTKEQQFRLEKRRwhDILNLKEENFQ 561
Cdd:PRK12704 51 AEAIKKEA-LLEAKEEIHKLRNE----FEKELRERRNELQKLEK---RLLQKEENLDRKLELLEKRE--EELEKKEKELE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 330443493 562 KLKSELKEKLILSEKIQKNAEDKLNDYMNEHQE-----IVEKLQNQA 603
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQLQELERISGLTAEeakeiLLEKVEEEA 167
|
|
| |
