|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-135 |
2.84e-42 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 149.33 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 2 KAYLKSADGFFVLN-KSTTIGKHaDSDLVLQdhlvrgqhhpqwpgpstsiinqehapppglctcrsdaeSADIDNHHALI 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQ--------------------------------------SPGVEEQHAVI 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 81 EFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGSAGMTYELVIEN 135
Cdd:cd22700 42 EYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGDVLRFGFGGLPYELVVDN 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-1006 |
1.05e-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: 88.96 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 273 EMESKYKDALIMNLQAEVADLSQRLSETAAvaAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYsQVLSQTL 352
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 353 AERNTEIESLKNEGENLKRDHAITSGMVTS-------LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSR---C 422
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEEleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 423 SVMKEELRKEEAQKDRREAQ-EKELKLCRSQMQDMEKEVRKLREELKKNYMG---------QNIISKTLREKNKLENFRN 492
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 493 QVIKATFGKTKPFRDKPITDQQACMRDSCSSIDLKKEVELLQHLplsplvSGLQKTVVNILRvSLSWLEETEQLLGDLdI 572
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL------EGFSEGVKALLK-NQSGLSGILGVLSEL-I 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 573 ElsdSDKGFSLCL-IYLLEHYKKIMS-------QSQDLQAQMNASRETQKSLRQEHLAEKE-KLAEKLEQEEKLKAKIQQ 643
Cdd:TIGR02168 530 S---VDEGYEAAIeAALGGRLQAVVVenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 644 LTEEKAALEESIGQEKSRS------EEALEKA-----QARVRELENHLAS------QKEALENSVAQEKRKMREMLEAER 706
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGVlvvddlDNALELAkklrpGYRIVTLDGDLVRpggvitGGSAKTNSSILERRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 707 RKAQDLENQLTQQKEISENNTYEklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMK 786
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 787 TTESQRAETLALKLKETLAELETtktkmiltddrlklQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQTIVSLEER 866
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEE--------------LEAQIEQLKEELKAL----REALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 867 LCQVTQYYQKIEGEITTLKNNdtgpKEEASQDLtAGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLR------- 939
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQ----IEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRseleels 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 940 TDLGEAHSRMSDLRGELSEKQ----KMELERQVALVR----------QQSGELSMLKAKVAQTTGLMEKKDRELKVLREA 1005
Cdd:TIGR02168 901 EELRELESKRSELRRELEELReklaQLELRLEGLEVRidnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
.
gi 1907156419 1006 L 1006
Cdd:TIGR02168 981 I 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
598-846 |
8.59e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 598 QSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELE 677
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 678 NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENntyeklkmRDTLEKEKRKIQDLENRLTKQKEE 757
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 758 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 837
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-LAELLEELAEAAARLLLLLEAEA 501
|
....*....
gi 1907156419 838 QKHGFEEEI 846
Cdd:COG1196 502 DYEGFLEGV 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
585-839 |
1.11e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 585 LIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL---AEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESI-- 655
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELeleeAQAEEYELLAELARLEQDIar 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 656 -GQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTyEKLKMR 734
Cdd:COG1196 307 lEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 735 DTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 814
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*
gi 1907156419 815 ILTDDRLKLQQQSMKALQDERESQK 839
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAA 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-1006 |
1.48e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 404 LRIENREKEYQ-----LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniIS 478
Cdd:PRK03918 155 LGLDDYENAYKnlgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 479 KTLRE----KNKLENFRNQVIKatfgktkpfRDKPITDQQACMRDSCSSI-DLKKEVELLQHlplsplvsglqktvvNIL 553
Cdd:PRK03918 228 KEVKEleelKEEIEELEKELES---------LEGSKRKLEEKIRELEERIeELKKEIEELEE---------------KVK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 554 RV-SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEKLE 632
Cdd:PRK03918 284 ELkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK-KLKELEKRLEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 633 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDL 712
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCPVC 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 713 ENQLTQQKEISENNTYeKLKMRDtLEKEKRKIQDLENRLTKQKEEIELKEQKENVLnnklkdaLVMVEDAQQMKTTESQR 792
Cdd:PRK03918 442 GRELTEEHRKELLEEY-TAELKR-IEKELKEIEEKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 793 AETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD------ERESQKHGFEEEISEYKEQIKQHS-QTIVSLEE 865
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGfESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 866 RLCQVTQYYQkiegEITTLKNndtGPKEeasqdltagppLDSGDKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEA 945
Cdd:PRK03918 593 RLKELEPFYN----EYLELKD---AEKE-----------LEREEKEL--KKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 946 HSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQT-------TGLMEKKDRELKVLREAL 1006
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeLEEREKAKKELEKLEKAL 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
626-867 |
1.11e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 626 KLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEAlENSVAQEKRKMREMLEAE 705
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 706 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQM 785
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 786 KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 865
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 1907156419 866 RL 867
Cdd:COG1196 464 LL 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
610-897 |
1.84e-12 |
|
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: 71.63 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLR--QEHLA-------EKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVREL 676
Cdd:TIGR02168 175 KETERKLErtRENLDrledilnELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 677 ENHLASQKEALENSVAQEKRKMREM----------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD 746
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 747 LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 826
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 827 SMKALQDERESQKHGFEE-EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 897
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
628-902 |
2.00e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 628 AEKLEQEEKLKAKIQQLTEEKAALE--------ESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMR 699
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 700 EMLEAERRKAQdLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 779
Cdd:COG1196 289 EEYELLAELAR-LEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 780 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQT 859
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907156419 860 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAG 902
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-902 |
3.50e-12 |
|
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: 70.87 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 251 SQQDKDEIILLLGREVNRLSDFEMESKYKDAL---IMNLQAEVADLSQRLSETAAVAAARqsnrcdpklqgVDEGDDlRQ 327
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAET-----------RDELKD-YR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 328 KEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIE 407
Cdd:TIGR02169 392 EKLEKLKREINELKRELDR-LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 408 NREKEYQLEALSSRCSVMKEELRKEEAQkdrreaqekelklcRSQMQDMEKEVRKLREELKKNYMGqniISKTLREKNKL 487
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ--------------ARASEERVRGGRAVEEVLKASIQG---VHGTVAQLGSV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 488 ENFRNQVIKATFGKTKPFrdkPITDQQAcmrDSCSSIDLKKEVEL--LQHLPLsplvsglqktvvNILRVSLSWLEE-TE 564
Cdd:TIGR02169 534 GERYATAIEVAAGNRLNN---VVVEDDA---VAKEAIELLKRRKAgrATFLPL------------NKMRDERRDLSIlSE 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 565 QLLGDLDIELSDSDKGFSLCLIYL---------LEHYKKIMSQSQ---------DLQAQMNASRETQKSLRQEHLAEKEK 626
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYVfgdtlvvedIEAARRLMGKYRmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAE 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 627 LAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLE 703
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDElsqELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE-IE 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 704 AERRKAQDLENQLTQQKE------ISENNTYEKLKMR--DTLEKEKRKIQDLENRLTKQKEEIELKEQK----ENVLNNK 771
Cdd:TIGR02169 755 NVKSELKELEARIEELEEdlhkleEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRltleKEYLEKE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 772 LKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKlqqqSMKALQDERESQKHGFEEEISEYKE 851
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG----DLKKERDELEAQLRELERKIEELEA 910
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 852 QIKQHSQTIVSLEERLcqvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAG 902
Cdd:TIGR02169 911 QIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLE 954
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
547-855 |
3.72e-12 |
|
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: 70.86 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 547 KTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEK 626
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 627 LAEKLEQEEKLKAKIQQLTEEKAALeesigqeksrsEEALEKAQARVRELENHLASQKEALENSVAQekrkmremLEAER 706
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKAL-----------REALDELRAELTLLNEEAANLRERLESLERR--------IAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 707 RKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMK 786
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156419 787 TTESQRAETLALKLKETLAELETTKTKMiltDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 855
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
609-885 |
6.07e-12 |
|
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: 70.10 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 609 SRETQKSLR-QEHLAEKEKLA--EKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKE 685
Cdd:TIGR02169 204 RREREKAERyQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 686 ALENSVAQEKRKMREmLEAERRKAQD----LENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK 761
Cdd:TIGR02169 284 LGEEEQLRVKEKIGE-LEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 762 EQKENVLNNKLKDalvMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHG 841
Cdd:TIGR02169 363 KEELEDLRAELEE---VDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 842 FEE-------EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 885
Cdd:TIGR02169 439 LEEekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-758 |
8.11e-12 |
|
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: 69.71 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 365 EGENLKRDHAITSGMVTSLQKDMSAR---------NEQVQQLQEEVNRLRIENREKEYQLEALS---SRCSVMKEELRKE 432
Cdd:TIGR02169 645 EGELFEKSGAMTGGSRAPRGGILFSRsepaelqrlRERLEGLKRELSSLQSELRRIENRLDELSqelSDASRKIGEIEKE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 433 EAQKDRREAQEKE-LKLCRSQMQDMEKEVRKLREELKKNymgqniisktlreknklenfrnqvikatfgktkpfrDKPIT 511
Cdd:TIGR02169 725 IEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELKEL------------------------------------EARIE 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 512 DQQAcmrdscssiDLKKEVELLQHLPLSPLVSGLQKtvvniLRVSLSWLEET----EQLLGDLDIELSDSDkgfslcliy 587
Cdd:TIGR02169 769 ELEE---------DLHKLEEALNDLEARLSHSRIPE-----IQAELSKLEEEvsriEARLREIEQKLNRLT--------- 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKimSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEE 664
Cdd:TIGR02169 826 LEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELER 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 665 ALEKAQARVRELENHLASQKEALENSVAQEK----------------------RKMREMLEAERRKAQDLENQLTQQKEI 722
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEE 983
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907156419 723 SENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 758
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-131 |
1.02e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.90 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 12 FVLNKS-TTIGKHADSDLVLQDHLVrgqhhpqwpgpstsiinqehapppglctcrsdaeSAdidnHHALIEFNEaeGTFV 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTV----------------------------------SR----RHARIRRDG--GGWV 55
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907156419 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYEL 131
Cdd:COG1716 56 LEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELRFRL 95
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
623-1006 |
1.34e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 623 EKEKLAEKLEQEEKLKAKIQQL---TEEKAALEESI--GQEKSRSEEALEKAQARvRELENhlaSQKEALENSVAQEKRK 697
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKkkAEEAKKADEAKKKAEEA-KKAEE---AKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 698 MREmleaERRKAQDLENQLTQQKEISEN--NTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEiELKEQKENVLNNKLK 773
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 774 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 853
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 854 KQHSQTIVSLEERLCQVTQYyqKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQK-EILSQQ 932
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKK 1710
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 933 EIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGElsmlKAKVAQTTGLMEKKDRELKVLREAL 1006
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-984 |
2.02e-11 |
|
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: 68.46 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 251 SQQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEI 330
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 331 ESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENRE 410
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 411 KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKLE-- 488
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELll 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 489 ---------------NFRNQVIKATFGKTKPFRDKPITDQQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNIL 553
Cdd:pfam02463 491 srqkleersqkeskaRSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 554 RVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQD----LQAQMNASRETQKSLRQEHLAEKEKLAE 629
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDdkraKVVEGILKDTELTKLKESAKAKESGLRK 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 630 KLEQE----EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENhLASQKEALENSVAQEKRKMREML--E 703
Cdd:pfam02463 651 GVSLEeglaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK-KEQREKEELKKLKLEAEELLADRvqE 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 704 AERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK-----------RKIQDLENRLTKQKEEIELKEQKENVLNNKL 772
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelslkekelaeEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 773 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQ 852
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 853 IKQhsQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgPPLDSGDKEIACDHLIDDLLMAQKEILSQQ 932
Cdd:pfam02463 890 SKE--EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEE-PEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 933 EIIMKLRTDLGEAHSRMSDLRgELSEKQKMELERQVALVRQQSGELSMLKAK 984
Cdd:pfam02463 967 LAKEELGKVNLMAIEEFEEKE-ERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-122 |
2.14e-11 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 60.28 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 18 TTIGKHADSDLVLQDhlvrgqhhpqwpgpstsiinqehapppglctcrsdaesADIDNHHALIEFNEaEGTFVLQDFNSR 97
Cdd:pfam00498 1 VTIGRSPDCDIVLDD--------------------------------------PSVSRRHAEIRYDG-GGRFYLEDLGST 41
|
90 100
....*....|....*....|....*
gi 1907156419 98 NGTFVNECHIQNVAVKLIPGDILRF 122
Cdd:pfam00498 42 NGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
322-892 |
2.18e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 68.00 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 322 GDDLRQKEIESMKSQINALQKGYsQVLSQTLAERNTEIESLKNEGENLKRDhaitsgmvtslQKDMSARNEQVQQLQEEV 401
Cdd:PRK01156 146 GDPAQRKKILDEILEINSLERNY-DKLKDVIDMLRAEISNIDYLEEKLKSS-----------NLELENIKKQIADDEKSH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 402 NRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLR---EELKK-----NYMG 473
Cdd:PRK01156 214 SITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKeleERHMKiindpVYKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 474 QNIISKTLREKNKLENFRnQVIKATFGKTKPFRD--KPITDQQAcmrDSCSSIDLKKEVELLQH--LPLSPLVSGLQKTV 549
Cdd:PRK01156 294 RNYINDYFKYKNDIENKK-QILSNIDAEINKYHAiiKKLSVLQK---DYNDYIKKKSRYDDLNNqiLELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 550 VNILRVSLsWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQeHLAEKEKLAE 629
Cdd:PRK01156 370 KSIESLKK-KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 630 KLEQEEKLKAKIQQLTEEKAA-LEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKmremLEAERRK 708
Cdd:PRK01156 448 MLNGQSVCPVCGTTLGEEKSNhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK----SINEYNK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 709 AQDLENQLTQQKeISENntyeklkmrdTLEKEKRKIQDLENRLTKQKEEIeLKEQKENVLNNKLKDALVMVEDAQQMKTT 788
Cdd:PRK01156 524 IESARADLEDIK-IKIN----------ELKDKHDKYEEIKNRYKSLKLED-LDSKRTSWLNALAVISLIDIETNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 789 ESQRAETLALKLKETLAELETTKT----KMILTDDRLKLQQQSMKALQDEReSQKHGFEEEISEYKEQIKQHSQTIVSLE 864
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENK-ILIEKLRGKIDNYKKQIAEIDSIIPDLK 670
|
570 580 590
....*....|....*....|....*....|.
gi 1907156419 865 E---RLCQVTQYYQKIEGEITTLKNNDTGPK 892
Cdd:PRK01156 671 EitsRINDIEDNLKKSRKALDDAKANRARLE 701
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-897 |
2.24e-11 |
|
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: 68.12 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 328 KEIESMKSQINALQKGYsQVLSQTLAER-------NTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEE 400
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDeekinnsNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 401 VNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQ-----------KDRREAQEKELKLCRSQMQDMEKEVRKLR-EELK 468
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDKIKnKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 469 KNYMGQNIISKTLREK------NKLENFRNQVIKATFGKTKPFRDKPI---TDQQACMRDSCSSIDLK-----KEVELLQ 534
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKslesqiSELKKQNNQLKDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKkqlseKQKELEQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 535 HlplSPLVSGLQKTvVNILRVSLSWL--EETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMS---QSQDLQAQMNAS 609
Cdd:TIGR04523 279 N---NKKIKELEKQ-LNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLRQEhLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEalekAQARVRELEnhlaSQKEALE 688
Cdd:TIGR04523 355 ESENSEKQRE-LEEKQNEIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIKKLQ----QEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 689 nsvaQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 768
Cdd:TIGR04523 426 ----KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 769 NNK----------LKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTD---------DRLKLQQQSMK 829
Cdd:TIGR04523 502 NEEkkeleekvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeiEELKQTQKSLK 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 830 ALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 897
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-130 |
2.39e-11 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 60.75 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 11 FFVLNKSTTIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSR--------------------------------------RHARIEVDG--GGVY 53
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907156419 91 LQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd00060 54 LEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFRFE 92
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-751 |
4.02e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 252 QQDKDEIILLLGRE---VNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSnrcdpKLQGVDEGDDLRQK 328
Cdd:COG1196 277 EELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-----ELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 329 EIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR--- 405
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeal 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 406 -IENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQD------MEKEVRKLREELKKNYMGQNIIS 478
Cdd:COG1196 431 aELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAElleelaEAAARLLLLLEAEADYEGFLEGV 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 479 KTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQACMRDSCSSI-DLKKEVELLQHLPLSpLVSGLQktvVNILRVSL 557
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDeVAAAAIEYLKAAKAG-RATFLP---LDKIRARA 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 558 SWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKL 637
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 638 KAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaQEKRKMREMLEAERRKAQDLENQLT 717
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL----EEELEEEALEEQLEAEREELLEELL 742
|
490 500 510
....*....|....*....|....*....|....
gi 1907156419 718 QQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL 751
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-949 |
1.30e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 392 EQVQQLQEEVNRLRIENREkEYQLEALSSRCSVMK-------EELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLR 464
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKaeearkaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 465 EELKKNYMGQ---NIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQACMRDSCSSIDLKKEVELLQHlplspl 541
Cdd:PTZ00121 1319 EAKKKAEEAKkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------ 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 542 VSGLQKTVvnilrvslswlEETEQLLGDLDIELSDSDKGfslcliyllEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL 621
Cdd:PTZ00121 1393 ADEAKKKA-----------EEDKKKADELKKAAAAKKKA---------DEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 622 AEKEKLAEKLEQ--EEKLKA-KIQQLTEEKAALEESigqeKSRSEEALEKAQarvrELENHLASQKEALENSVAQEKRKM 698
Cdd:PTZ00121 1453 AEEAKKAEEAKKkaEEAKKAdEAKKKAEEAKKADEA----KKKAEEAKKKAD----EAKKAAEAKKKADEAKKAEEAKKA 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 699 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAL 776
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 777 VMVE------------DAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEE 844
Cdd:PTZ00121 1605 KKMKaeeakkaeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 845 EISEYK-EQIKQHSQTIVSLEERLCQVTQYYQKIEG-----EITTLKNNDTGPKEEASQDLTAGPPLDSGDKEiACDHLI 918
Cdd:PTZ00121 1685 EDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLK 1763
|
570 580 590
....*....|....*....|....*....|.
gi 1907156419 919 DDLLMAQKEILSQQEIIMKLRTDLGEAHSRM 949
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
70-131 |
4.25e-10 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 57.71 E-value: 4.25e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156419 70 SADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGMTYEL 131
Cdd:cd22704 32 SRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-906 |
3.74e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 287 QAEVA----DLSQRLSETAAVAAARQsnrcdpklqgvdegDDLRQKEIESMKSQINALQKGySQVLSQTLAERNTEIESL 362
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK--------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 363 KNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ 442
Cdd:COG1196 273 RLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 443 EKELKLCRSQMQDMEKEVRKLREELKknymgqniiSKTLREKNKLENFRNQVIKAtfgktkpfrdkpitdqqacmrdscs 522
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAE---------AELAEAEEELEELAEELLEA------------------------- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 523 sidLKKEVELLQHLplsplvSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKgfslcliyLLEHYKKIMSQSQDL 602
Cdd:COG1196 392 ---LRAAAELAAQL------EELEEAEEALLERLERLEEELEELEEALAELEEEEEE--------EEEALEEAAEEEAEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 603 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEesiGQEKSRSEEALEKAQARVRELENHLAS 682
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE---GFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 683 QKEALENSV-----AQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEE 757
Cdd:COG1196 532 VEAAYEAALeaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 758 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 837
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR-RELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156419 838 QKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLD 906
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
597-808 |
5.50e-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: 59.39 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 597 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVREL 676
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 677 ENHLASQKEALENSVA---QEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 753
Cdd:COG4942 96 RAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 754 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL---ALKLKETLAELE 808
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLE 233
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
589-855 |
5.90e-09 |
|
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: 60.14 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNasRETQKSLRQEHLA-EKEKLAEKLEQEEKlKAKIQQLTEEKAALE--------------- 652
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMD--RQAAIYAEQERMAmERERELERIRQEER-KRELERIRQEEIAMEisrmrelerlqmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 653 ---ESIGQE-------KSRSEEALEKAQARVRELENHLASQKEALENSVAQ-EKRKMREMleaERRKAQDLENQltQQKE 721
Cdd:pfam17380 389 qknERVRQEleaarkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREM---ERVRLEEQERQ--QQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 722 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENVLNNKLKDALV--MVEDAQQMKTTESQRAETlalk 799
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLekEMEERQKAIYEEERRREA---- 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 800 lketlaelETTKTKMILTDDRLKLQQQSMKAlqDERESQKHGFEEEiSEYKEQIKQ 855
Cdd:pfam17380 539 --------EEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMERE-REMMRQIVE 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-811 |
6.24e-09 |
|
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: 60.08 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 560 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMN---ASRETQKSLRQEHLAEKEKLAEKLE-QEE 635
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEeRLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 636 KLKAKIQQLTEEKAALEESIGQEKSRSE---EALEKAQARVRELENHLASQKEALENSVaQEKRKMREMLEAERRKAQDL 712
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDkltEEYAELKEELEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 713 ENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQMKTTESQR 792
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDR 480
|
250
....*....|....*....
gi 1907156419 793 AETLALKLKETLAELETTK 811
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQA 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-985 |
6.85e-09 |
|
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: 60.03 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 454 QDMEKEVRKLREELKKNYMGQNIISKTLREK-NKLENFRNQV------IKATFGKTKPFRDKpITDQQACMRDSCSSIDL 526
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDeEKINNSNNKIkileqqIKDLNDKLKKNKDK-INKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 527 KKEVELLQHLPLSPLVSGLQKTVVNILRVS--LSWLE---------------ETEQLLGDLDIELSDSDKGFS------- 582
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLteIKKKEkeleklnnkyndlkkQKEELENELNLLEKEKLNIQKnidkikn 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 583 --LCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKaaleESIGQEKS 660
Cdd:TIGR04523 195 klLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ----NKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 661 RSEEALEKAQARVRELE---NHLASQKEALENSVAQEKRK-MREMLEAERRKAQDLENQLTQ-QKEISE----------- 724
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEkqlNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQnNKIISQlneqisqlkke 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 725 --NNTYEKLKMRDTLEKEKRKIQDLEN----------RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQR 792
Cdd:TIGR04523 351 ltNSESENSEKQRELEEKQNEIEKLKKenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 793 AETLALKLKETLAELETTKTKMILT----DDRLKLQQQSMKALQDERESQKHGFEE----------EISEYKEQIKQHSQ 858
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekELKKLNEEKKELEE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 859 TIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIACDHL---IDDLLMAQKEILSQQEii 935
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE---LKKENLEKEIDEKnkeIEELKQTQKSLKKKQE-- 585
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 936 mKLRTDLGEAHSRMSDLRGELSEK--QKMELERQVALVRQQSGELSMLKAKV 985
Cdd:TIGR04523 586 -EKQELIDQKEKEKKDLIKEIEEKekKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
621-885 |
7.03e-09 |
|
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: 60.08 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 621 LAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES-IGQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMR 699
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 700 EMLEAERRKAQDL--ENQLTQQKEISENnTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENVLN-----NK 771
Cdd:TIGR02169 272 QLLEELNKKIKDLgeEEQLRVKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDkLLAEIEELEReieeeRK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 772 LKDALV-MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYK 850
Cdd:TIGR02169 351 RRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270
....*....|....*....|....*....|....*
gi 1907156419 851 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 885
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
560-852 |
1.06e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 58.54 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 560 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkiMSQSQDLQAQMNASRETQKSLRQE--HLAEKEKLAEKLEQE--- 634
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEEnkALREEAQAAEKALQRaeg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 635 ------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQ--------- 693
Cdd:pfam19220 161 elatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 694 -EKRKMREMLEAERRKAQDLENQLTQQkeisenntyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKL 772
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEA--------------RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 773 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRlklqqqsMKALQDERESQKHGFEEEISEYKEQ 852
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDR-------IAELTKRFEVERAALEQANRRLKEE 379
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-747 |
1.07e-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: 59.30 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 353 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKE 432
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 433 EAQKDRR-------EAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREknKLENFRNQV--IKATFGKTK 503
Cdd:TIGR02168 746 EERIAQLskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELtlLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 504 pFRDKPITDQQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTvvnilrvslswLEETEQLLGDLDIELSDSDkgfsl 583
Cdd:TIGR02168 824 -ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL-----------IEELESELEALLNERASLE----- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 584 cliyllEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQ----LTEEKAALEESIGQEK 659
Cdd:TIGR02168 887 ------EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerLSEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 660 SRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKmrEMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRD 735
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERY--DFLTAQKEDLTEAKETL--EEAIEEIDREARERFKD 1036
|
410
....*....|..
gi 1907156419 736 TLEKEKRKIQDL 747
Cdd:TIGR02168 1037 TFDQVNENFQRV 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-838 |
1.38e-08 |
|
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: 58.24 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 608 ASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLAS---QK 684
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAElekEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 685 EALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 764
Cdd:COG4942 93 AELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 765 ENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQ 838
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-495 |
1.84e-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: 58.53 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 252 QQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAvaaarQSNRCDPKLQGVDEGDDLRQKEIE 331
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-----RLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 332 SMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREK 411
Cdd:TIGR02168 793 QLKEELKALREALDE-LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 412 EYQLEALSSRCSVMKEELrkeEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIskTLREKNKLENFR 491
Cdd:TIGR02168 872 ESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL--EVRIDNLQERLS 946
|
....
gi 1907156419 492 NQVI 495
Cdd:TIGR02168 947 EEYS 950
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
346-878 |
2.01e-08 |
|
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: 58.44 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 346 QVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEY------------ 413
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihtlqqqkt 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 414 ----QLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLRE-----K 484
Cdd:TIGR00618 390 tltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 485 NKLENFRN-QVIKATFGKTKPFRDKPITDQQACMRDSCssidlKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEET 563
Cdd:TIGR00618 470 EREQQLQTkEQIHLQETRKKAVVLARLLELQEEPCPLC-----GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 564 EQLLGDLDIELSDSdKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKI 641
Cdd:TIGR00618 545 EDVYHQLTSERKQR-ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKLQP 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 642 QQLTEEKAALEESIGQEKSRSEEALEkaqarvRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKE 721
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 722 ISEnntYEKLKMRDTLEKEK---RKIQDLENRLTKQKEEIelkEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAL 798
Cdd:TIGR00618 698 MLA---QCQTLLRELETHIEeydREFNEIENASSSLGSDL---AAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 799 KLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE-RESQKHGFEEEISEYKEQIKQHSQTIVSLEER---LCQVTQYY 874
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEiGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKsatLGEITHQL 851
|
....
gi 1907156419 875 QKIE 878
Cdd:TIGR00618 852 LKYE 855
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
593-790 |
2.96e-08 |
|
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: 57.08 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 669
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAAleRRIAALARRIRALEQElAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 670 QARVR-ELENHLASQKEALE--------NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 740
Cdd:COG4942 114 YRLGRqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 741 KRK----IQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES 790
Cdd:COG4942 194 KAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
353-886 |
4.01e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 353 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALssrcsvmkeELRKE 432
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 433 EAQKDRREAQEkELKLCRSQMQDMEKEVRKLREElkknymgqniiSKTLREKNKleNFRNQVIKAtfgktkpfrDKPITD 512
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLRED-----------ADDLEERAE--ELREEAAEL---------ESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 513 QQACMRDSCSSI-DLKKEvellqhlplsplvsglqktvvnilrvslswLEETEQLLGDLDIELSDSDKGFSLCLIYLLEH 591
Cdd:PRK02224 375 AREAVEDRREEIeELEEE------------------------------IEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 592 YKKIMSQSQDLQAQMNASRETQKSLRQ----------EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQeksr 661
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER---- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 662 sEEALEKAQARVRELENhlasQKEALENSVAQEKRKM---REMLEAERRKAQDLENQLTQQKEISEnntyeklKMRDTLE 738
Cdd:PRK02224 501 -AEDLVEAEDRIERLEE----RREDLEELIAERRETIeekRERAEELRERAAELEAEAEEKREAAA-------EAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 739 KEKRKIQDLENRLTKQKEEIELKeqkenvlnNKLKDALVMVEDAQqmkttesQRAETLALKLkETLAELETTKTkmiltd 818
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESL--------ERIRTLLAAIADAE-------DEIERLREKR-EALAELNDERR------ 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 819 DRLKLQQQSMKALQDEREsqkhgfEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 886
Cdd:PRK02224 627 ERLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
287-844 |
5.64e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 287 QAEVADLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGysqvlsqtlAERNTEIESLKNEG 366
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAKKKA 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 367 ENLKRDhaitsgmVTSLQKDMSARN--EQVQQLQEEVNRLRIENREKEYQLEALSSRCSVmkEELRK-EEAQKDRREAQE 443
Cdd:PTZ00121 1401 EEDKKK-------ADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKaEEAKKKAEEAKK 1471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 444 KELKLCRSQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQACMRDSCSS 523
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 524 IDLKKEVELlqhlplsplvsglqKTVVNILRVSLSWLEETEQLLGDLDIE-LSDSDKGFSLCLIYLLEHYKKImsQSQDL 602
Cdd:PTZ00121 1549 DELKKAEEL--------------KKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKM--KAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 603 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEE----KAALEESIGQEKSRSEEALEKAQARVRELEN 678
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 679 HL------ASQKEALENSVAQEKRKMREMLEAERRKAQDLENqlTQQKEISENNTYEKLKMRdtlEKEKRKIQDLENRLT 752
Cdd:PTZ00121 1693 ALkkeaeeAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE--AKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEE 1767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 753 KQKEEIelKEQKENVLNNKL--KDALVMVEDAQQMKTTESQRAETLALKLKETL-----AELETTKTKMILTddrlklqq 825
Cdd:PTZ00121 1768 KKAEEI--RKEKEAVIEEELdeEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLvindsKEMEDSAIKEVAD-------- 1837
|
570
....*....|....*....
gi 1907156419 826 QSMKALQDERESQKHGFEE 844
Cdd:PTZ00121 1838 SKNMQLEEADAFEKHKFNK 1856
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
73-130 |
6.73e-08 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 51.08 E-value: 6.73e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 73 IDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22665 40 VSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVKCQYV 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
394-762 |
7.95e-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: 56.61 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 394 VQQLQEEVNRLRIEnREKEYQLEALSSRcsvmKEELRKEEAQKdRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMG 473
Cdd:TIGR02169 193 IDEKRQQLERLRRE-REKAERYQALLKE----KREYEGYELLK-EKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 474 QNIISKTLREKNKlenfrnQVIKATFGKTKPFRDK--PITDQQACMRDSCSsiDLKKEVELLQhlplsplvSGLQKTVVN 551
Cdd:TIGR02169 267 LEEIEQLLEELNK------KIKDLGEEEQLRVKEKigELEAEIASLERSIA--EKERELEDAE--------ERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 552 ILRVslswLEETEQLLGDLDIELSDSDKgfslcliyllehykkimsqsqdLQAQMNASRETQKSLRQEHLAEKEKLAEKL 631
Cdd:TIGR02169 331 IDKL----LAEIEELEREIEEERKRRDK----------------------LTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 632 EQEEKLKAKIQQLTEEKaaleESIGQEKSRSEEALEKAQARVRELENHLASQKEALeNSVAQEKRKMREMLEAERRKAQd 711
Cdd:TIGR02169 385 DELKDYREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-NELEEEKEDKALEIKKQEWKLE- 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 712 lenQLTQQKEisenntyeklKMRDTLEKEKRKIQDLENRLTKQKEEIELKE 762
Cdd:TIGR02169 459 ---QLAADLS----------KYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
383-813 |
1.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 383 LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALS--SRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEV 460
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 461 RKLREELKK-----NYMGQNIISKTLREKNKLENFRNQVIKATfgKTKPFRDKPITDQQACMRDSCSSIDLKKEVELLQh 535
Cdd:COG4717 173 AELQEELEElleqlSLATEEELQDLAEELEELQQRLAELEEEL--EEAQEELEELEEELEQLENELEAAALEERLKEAR- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 536 lplspLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELsdsdkGFSLCLIYLLEHYKKIMSQSQDlQAQMNASRETQKS 615
Cdd:COG4717 250 -----LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL-----GLLALLFLLLAREKASLGKEAE-ELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 616 LRQEHLAEKEKLAEKLEQEEkLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVreLENHLASQKEALEnSVAQEK 695
Cdd:COG4717 319 EELEELLAALGLPPDLSPEE-LLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELR-AALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 696 RKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRdtLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNklkD 774
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELaELEAELEQLEED---G 469
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907156419 775 ALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTK 813
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-865 |
1.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 328 KEIESMKSQINALQKGYSQV--LSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 405
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIeeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 406 IENREKEYQLEALSSRCSVMKEELRK-EEAQKDRREAQEKELKLCR---------SQMQDMEKEVRKLREELKKNymgQN 475
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEYIKlsefyeeylDELREIEKRLSRLEEEINGI---EE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 476 IISKTLREKNKLENFRNQV--IKATFGKTKPF-----RDKPITDQQACMRDSCSSIDLKKEVELLQhlplspLVSGLQKT 548
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLkeLEKRLEELEERhelyeEAKAKKEELERLKKRLTGLTPEKLEKELE------ELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 549 VVNILRVSLSWLEETEQLLGDLD---IELSDSDKGFSLCLIYLLEHYKK-IMSQSQDLQAQMNASRETQKSLRQEHLAEK 624
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 625 EKLAEKLEQEEKLkAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRK--- 697
Cdd:PRK03918 483 RELEKVLKKESEL-IKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLael 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 698 MREMLEAERRKAqDLENQLTQQKEISENNTYEKLKMRDTLEKE-------KRKIQDLENRLTKQKEEIELKEQKENVLNN 770
Cdd:PRK03918 562 EKKLDELEEELA-ELLKELEELGFESVEELEERLKELEPFYNEylelkdaEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 771 KLKDALVMVEDAQQMKTTES-QRAETLALKLKETLAELETTKtkmiltdDRLKLQQQSMKALQDERESQKhgfeEEISEY 849
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAEL-------EELEKRREEIKKTLEKLKEEL----EEREKA 709
|
570
....*....|....*.
gi 1907156419 850 KEQIKQHSQTIVSLEE 865
Cdd:PRK03918 710 KKELEKLEKALERVEE 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1006 |
1.26e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 292 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLK 370
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 371 RDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsvMKEELRKEEAQKDRREAQEKELKLCR 450
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 451 SQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKLENFRNQVIKatfgktkpfRDKPITDQQACMRDSCSSIDLKKev 530
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDY---REKLEKLKREINELKRELDRLQE---------ELQRLSEELADLNAAIAGIEAKI-- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 531 ellqhlplsPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyLLEHYKKIMSQSQDLQAQMNASR 610
Cdd:TIGR02169 437 ---------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEAEAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 611 ETQKSLR--QEHLAE---------------KEKLAEKLE-------------QEEKLKAKIQQLTEEKAALEESIGQEKS 660
Cdd:TIGR02169 504 ERVRGGRavEEVLKAsiqgvhgtvaqlgsvGERYATAIEvaagnrlnnvvveDDAVAKEAIELLKRRKAGRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 661 RSEEALEKAQAR--VRELENHLASQKEALENSVAQEKRK--MREMLEAERR-----KAQDLENQL-------TQQKEISE 724
Cdd:TIGR02169 584 RDERRDLSILSEdgVIGFAVDLVEFDPKYEPAFKYVFGDtlVVEDIEAARRlmgkyRMVTLEGELfeksgamTGGSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 725 NNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttESQRAETLALKLKETL 804
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 805 AELETtktkmiltddrlKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLE-----ERLCQVTQYYQKIEG 879
Cdd:TIGR02169 740 EELEE------------DLSSLEQEIENVKSELKE--LEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 880 EITTLKnndtGPKEEASQDLTA-GPPLDSGDKEIAcdHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELS- 957
Cdd:TIGR02169 806 EVSRIE----ARLREIEQKLNRlTLEKEYLEKEIQ--ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRd 879
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907156419 958 -EKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREAL 1006
Cdd:TIGR02169 880 lESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
602-798 |
1.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 602 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLA 681
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 682 -----SQKEALENSVAQEKRKMREMLEAE------RRKAQDLENQLTQ-QKEISENNTYEKLKMRDTLEKEKRKIQDLEN 749
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLeelrelEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907156419 750 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAL 798
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
611-875 |
1.68e-07 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 55.07 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 611 ETQKSLRqehlAEKEKLAEKLEQEEKL-KAKIQQLTEEKAALEEsigqEKsrseealEKAQARVRELENHLASQKEALEN 689
Cdd:pfam15070 4 ESLKQLQ----TERDQYAENLKEEGAVwQQKMQQLSEQVRTLRE----EK-------ERSVSQVQELETSLAELKNQAAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 690 SVAQEKRKMREMLEAERRKAQDLEnQLTQQKEISENNTYEKLKMRDTL-----EKEKRkIQDLENRLTKQKEEIELKEQk 764
Cdd:pfam15070 69 PPAEEEQPPAGPSEEEQRLQEEAE-QLQKELEALAGQLQAQVQDNEQLsrlnqEQEQR-LLELERAAERWGEQAEDRKQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 765 envlnnklkdalvMVEDAQQMKTTESqRAETLALKLKETLAELETTKTKmiLTDDRLKLqqqsMKALQDERESQKH---- 840
Cdd:pfam15070 146 -------------ILEDMQSDRATIS-RALSQNRELKEQLAELQNGFVK--LTNENMEL----TSALQSEQHVKKElakk 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907156419 841 --GFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 875
Cdd:pfam15070 206 lgQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQ 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
275-851 |
1.75e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 275 ESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEiESMKSQINALQKGysqvlsqtlAE 354
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKA---------AA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 355 RNTEIESLKNEGENLKR-DHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSvmkEELRK-- 431
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA---DEAKKka 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 432 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKLENFRN--QVIKATFGKTKPFRDKP 509
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeELKKAEEKKKAEEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 510 ITDQQACMRDScssiDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDldielsdsdkgfslcliyll 589
Cdd:PTZ00121 1573 EEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-------------------- 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 590 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKlkaKIQQLTEEKAALEESIGQEKSRSEEALEKA 669
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 670 QARVRELENHLASQ---KEALENSVAQEKRKMREmlEAERRKAQDL------ENQLTQQKEISENNTYEKLKMRDTLEKE 740
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEA--EEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 741 KRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVmVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiLTDDR 820
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV-INDSKEMEDSAIKEVADSKNMQLEEADAFEKHK----FNKNN 1858
|
570 580 590
....*....|....*....|....*....|.
gi 1907156419 821 LKLQQQSMKALQDERESQKHGFEEEISEYKE 851
Cdd:PTZ00121 1859 ENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
327-853 |
1.77e-07 |
|
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: 55.50 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 327 QKEIESMKSQINAL----------QKGYSQVLSQTLAERNTEIESLKNEGENLK----RDHAITSGM---VTSLQKDMSA 389
Cdd:pfam05483 232 KKEINDKEKQVSLLliqitekenkMKDLTFLLEESRDKANQLEEKTKLQDENLKelieKKDHLTKELediKMSLQRSMST 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 390 RNEQVQQLQEEVNRLRIENREKEYQLEAL---------------SSRCSVmkEELRKEEAQkdRREAQEKELKLCRSQMQ 454
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELnkakaahsfvvtefeATTCSL--EELLRTEQQ--RLEKNEDQLKIITMELQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 455 DMEKEVRKLREELKKNYMGQNIISKTLREKNKLENFRNQVIKatfgktkpfrdkpITDQQACMRDSCSSIDLKKEVEllq 534
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEK-------------IAEELKGKEQELIFLLQAREKE--- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 535 hlplsplVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHyKKIMSQSQDLQAQMNAsretqk 614
Cdd:pfam05483 452 -------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN-KELTQEASDMTLELKK------ 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 615 slRQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnHLASQKEALENSVAQ 693
Cdd:pfam05483 518 --HQEDIINCKKQEERmLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE-YEVLKKEKQMKILEN 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 694 EKRKMREMLEAERRKAQDL--ENQLTQQKEISEN---NTYEKLKMRDTLEKEKRKiQDLENRLTKQKEEIELKEQKENVL 768
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELhqENKALKKKGSAENkqlNAYEIKVNKLELELASAK-QKFEEIIDNYQKEIEDKKISEEKL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 769 NNKLKDALVMVEDAQQMKTTESQRAETlalKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISE 848
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSN 750
|
....*
gi 1907156419 849 YKEQI 853
Cdd:pfam05483 751 IKAEL 755
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
663-817 |
1.93e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 663 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAE----RRKAQDLENQLTQQKEISENNTyeklkmrDTLE 738
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRKL-------ELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 739 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV-----EDAQQM---KTTESQRAETLAL-KLKETLAELET 809
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEA 186
|
....*....
gi 1907156419 810 TKT-KMILT 817
Cdd:PRK12704 187 DKKaKEILA 195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
589-1007 |
2.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKIQQ---LTEEKAALEESIGQEKSRSE 663
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 664 EaLEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRK 743
Cdd:COG4717 150 E-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 744 IQDLENRLTKQKEEIELKEQKE----------------NVLNNKLKDA--------LVMVEDAQQMKTTESQRAETLALK 799
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 800 LKETLAELETTKTKMILTDDRLK-----------------LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSqtIVS 862
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPpdlspeellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 863 LEERLCQVTQyYQKIEGEITTLKNNdtgpkeeasqdltagppLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 942
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 943 GEAHSRMSDLRGELSEkqkMELERQVALVRQqsgELSMLKAKVAQttglMEKKDRELKVLREALR 1007
Cdd:COG4717 449 EELREELAELEAELEQ---LEEDGELAELLQ---ELEELKAELRE----LAEEWAALKLALELLE 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
601-775 |
2.44e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 601 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA---LEKAQARVRELE 677
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 678 NH-----LASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyeklkmrdTLEKEKRKIQDLENRLT 752
Cdd:COG3206 289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA--------------QLEARLAELPELEAELR 354
|
170 180
....*....|....*....|...
gi 1907156419 753 KQKEEIELKEQKENVLNNKLKDA 775
Cdd:COG3206 355 RLEREVEVARELYESLLQRLEEA 377
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-124 |
2.94e-07 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 49.22 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 12 FVLNKST-TIGKHADSDLVLQDHLVRGqhhpqwpgpstsiinqehapppglctcrsdaesadidnHHALIEFNEaeGTFV 90
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSS--------------------------------------RHARIYLQG--SSWY 52
|
90 100 110
....*....|....*....|....*....|....
gi 1907156419 91 LQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 124
Cdd:cd22693 53 LEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-866 |
3.56e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 611 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQqltEEKAALEESIGQEKSRSEEALEKAQARvRELENHLASQKEALENS 690
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 691 VAQEKRKMREMLEA-ERRKAQDLENQLTQQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 769
Cdd:PTZ00121 1285 KAEEKKKADEAKKAeEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 770 NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiltddrlKLQQQSMKALQDERESQKHGFEEEISEY 849
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----------KAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
250
....*....|....*..
gi 1907156419 850 KEQIKQHSQTIVSLEER 866
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEA 1443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
348-1007 |
3.92e-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: 54.35 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 348 LSQTLAERNTEIESLKnegenlkrdhaitsGMVTSLQKDMSARNEQVQQ-----LQEEVNRLRIENREKEYQLEALSSRC 422
Cdd:pfam15921 222 ISKILRELDTEISYLK--------------GRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 423 SVMKEELRKEEAQKDRREAQEK-ELKLCRSQMQDMEKEVRKLREELKKnymgqniiSKTLREkNKLENFRNQVIKATFGK 501
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSELRE--------AKRMYE-DKIEELEKQLVLANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 502 TKPFRDKPITDQQACMRDscssidlkkevellqhlplsplvSGLQKTVVNILRVSLSWLEETEQllgdlDIELSDSDKGF 581
Cdd:pfam15921 359 TEARTERDQFSQESGNLD-----------------------DQLQKLLADLHKREKELSLEKEQ-----NKRLWDRDTGN 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 582 SLCLIYLLEHYKKIMSQSQDLQAQMNASR-ETQKSLRQ---------EHLAEKEKLAEKLEQ-EEKLKAKIQQLTEEKAA 650
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERqmaaiqgknESLEKVSSLTAQLEStKEMLRKVVEELTAKKMT 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 651 LEESIG---------QEKSRSEEA----LEKAQARV----RELEnHLASQKEALENSVAQ---------EKRKMREMLea 704
Cdd:pfam15921 491 LESSERtvsdltaslQEKERAIEAtnaeITKLRSRVdlklQELQ-HLKNEGDHLRNVQTEcealklqmaEKDKVIEIL-- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 705 eRRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLenRLTKQKEEIELKEQKENV---------LNNKLKDA 775
Cdd:pfam15921 568 -RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVsdlelekvkLVNAGSER 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 776 LVMVEDAQQ--------MKTTE------SQRAETLALKLKETLAELETT--KTKMILTDDRLKLQQ-----QSMKALQDE 834
Cdd:pfam15921 645 LRAVKDIKQerdqllneVKTSRnelnslSEDYEVLKRNFRNKSEEMETTtnKLKMQLKSAQSELEQtrntlKSMEGSDGH 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 835 RESQKHGFEEEISEYKEQIKQHSQTIVSLEE---------------------RLCQVTQYYQKIEGEITTLKNNDTGPKE 893
Cdd:pfam15921 725 AMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtnankekhflkeeknklsqELSTVATEKNKMAGELEVLRSQERRLKE 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 894 EASQDLTAgppLDSGDKEIA-CDHLIddllmaQKEilSQQEIIMKLRTDL------GEAHSRMSDLRGELseKQKMELER 966
Cdd:pfam15921 805 KVANMEVA---LDKASLQFAeCQDII------QRQ--EQESVRLKLQHTLdvkelqGPGYTSNSSMKPRL--LQPASFTR 871
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1907156419 967 QVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALR 1007
Cdd:pfam15921 872 THSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELR 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-823 |
4.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 257 EIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAaarqsnrcdPKLQGVDEGDDLRQKEIESMKSQ 336
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------PELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 337 INALQKGYSQVLSQ--TLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMsarnEQVQQLQEEVNRLRIENREKEYQ 414
Cdd:PRK03918 240 IEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 415 LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISK-TLREKNKLENFRNQ 493
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 494 VIKAtfgKTKPFRD-KPITDQQACMRDSCSsiDLKKEVELLQHLPLSPLVSG-----------LQKTVVNILRVSlSWLE 561
Cdd:PRK03918 396 LEKA---KEEIEEEiSKITARIGELKKEIK--ELKKAIEELKKAKGKCPVCGrelteehrkelLEEYTAELKRIE-KELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 562 ETEQLLGDLDIELSDSDKgfslcliyLLEHYKKIMSQsQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE------- 634
Cdd:PRK03918 470 EIEEKERKLRKELRELEK--------VLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKliklkge 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 635 ------------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaqaRVRELE---------NHLASQKEAL 687
Cdd:PRK03918 541 ikslkkelekleelkkklAELEKKLDELEEELAELLKELEELGFESVEELEE---RLKELEpfyneylelKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 688 ENSVAQEKR---KMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKmRDTLEKEKR------KIQDLENR-------- 750
Cdd:PRK03918 618 EKELKKLEEeldKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-EEYLELSRElaglraELEELEKRreeikktl 696
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156419 751 --LTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRA----ETLALKLKETLAELETTKTKMILTDDRLKL 823
Cdd:PRK03918 697 ekLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlskvGEIASEIFEELTEGKYSGVRVKAEENKVKL 775
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
615-942 |
4.24e-07 |
|
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: 54.21 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 615 SLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL-------ENHLASQKEA 686
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldyLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 687 LE---NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQ 763
Cdd:pfam02463 242 LQellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 764 KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 843
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 844 EEISEYKEQIkQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLM 923
Cdd:pfam02463 402 EEEKEAQLLL-ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330
....*....|....*....
gi 1907156419 924 AQKEILSQQEIIMKLRTDL 942
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERS 499
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-469 |
5.57e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 359 IESLKNEGENLKRDHAITsgMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL---RKEEAQ 435
Cdd:COG2433 382 LEELIEKELPEEEPEAER--EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907156419 436 KDRREAQ----EKELKLCRSQMQDMEKEVRKLREELKK 469
Cdd:COG2433 460 EIRKDREisrlDREIERLERELEEERERIEELKRKLER 497
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
629-865 |
6.35e-07 |
|
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: 53.57 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 629 EKLEQ-EEKLKAKIQQLTEEKAALEEsIGQEKSRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMLEAE 705
Cdd:pfam05483 370 QRLEKnEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 706 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD---------LENRLTKQKEE---IELKEQKENVLNNKlK 773
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQEASdmtLELKKHQEDIINCK-K 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 774 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 853
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250
....*....|..
gi 1907156419 854 KQHSQTIVSLEE 865
Cdd:pfam05483 604 ENKNKNIEELHQ 615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-1002 |
7.10e-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: 53.52 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 330 IESMKSQINALQKgysqvlsQtlAERNTEIESLKNEGENLkrDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENR 409
Cdd:TIGR02168 195 LNELERQLKSLER-------Q--AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 410 EKEYQLEALSSRCSVMKEELrkeeaqkdrrEAQEKELKLCRSQMQDMEKEVRKLREELK----KNYMGQNIISKTLREKN 485
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEI----------EELQKELYALANEISRLEQQKQILRERLAnlerQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 486 KLENFRNQVIKATFgktkpfrdkpitdqqacmrdscssiDLKKEVELLQhlplsplvsGLQKTVVNILRVSLSWLEETEQ 565
Cdd:TIGR02168 334 ELAEELAELEEKLE-------------------------ELKEELESLE---------AELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 566 LLGDLDIELSDsdkgfslcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQE--------HLAEKEKLAEKLEQEEKL 637
Cdd:TIGR02168 380 QLETLRSKVAQ-----------LELQIASLNNEIERLEARLERLEDRRERLQQEieellkklEEAELKELQAELEELEEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 638 KAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELENhLASQKEALENSVAQEKRKMREM--------- 701
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQAldaaereLAQLQARLDSLER-LQENLEGFSEGVKALLKNQSGLsgilgvlse 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 702 ---LEAERRKA---------QDL--ENQLTQQKEIS---ENNT-------YEKLKMRDTLEKEKRKIQDLENRLTKQKEE 757
Cdd:TIGR02168 528 lisVDEGYEAAieaalggrlQAVvvENLNAAKKAIAflkQNELgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 758 IELKEQKENVLNNKLKDALVM--VEDAQQMK-----------------------TTESQRAETLALKLKETLAELETTKT 812
Cdd:TIGR02168 608 VKFDPKLRKALSYLLGGVLVVddLDNALELAkklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 813 KMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPK 892
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 893 EEASQdltAGPPLDSGDKEIA-----CDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQ 967
Cdd:TIGR02168 768 ERLEE---AEEELAEAEAEIEeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDL 843
|
730 740 750
....*....|....*....|....*....|....*
gi 1907156419 968 VALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVL 1002
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
597-867 |
1.08e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 597 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkakiqqltEEKAALEESIGQEKSRSEEALEKAQARV--R 674
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK----------EEEKEKKLQEEELKLLAKEEEELKSELLklE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 675 ELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKiqdLENRLTKQ 754
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL---EEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 755 KEEIELKEQKENVLNNKLKDALVMvEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 834
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270
....*....|....*....|....*....|...
gi 1907156419 835 RESQKHGFEEEISEYKEQIKQHSQTIVSLEERL 867
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
607-901 |
1.23e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 607 NASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEA 686
Cdd:pfam02463 208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 687 LENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKEN 766
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 767 VLNNKLKDALVMVEDAQQMKTTESQRAETLALK---LKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 843
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKseeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 844 EEISEYKEQIKQHSQTIVSlEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTA 901
Cdd:pfam02463 448 EEKEELEKQELKLLKDELE-LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-808 |
1.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 249 DLSQQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAA--VAAARQSNRCDPKLQGVDEGDDLR 326
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 327 QKEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRI 406
Cdd:COG1196 315 EERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 407 ENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNK 486
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 487 LENFRNQVIKATFGKTKPfRDKPITDQQAcmrdscSSIDLKKEVELLQHLPLSPLVSGLqktvvniLRVSLSWLEETEQL 566
Cdd:COG1196 474 LLEAALAELLEELAEAAA-RLLLLLEAEA------DYEGFLEGVKAALLLAGLRGLAGA-------VAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 567 LGDLDIELsdsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTE 646
Cdd:COG1196 540 LEAALAAA----------LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 647 EKAALEESIGQ---EKSRSEEALEKAQARVRELENHLAS---QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQK 720
Cdd:COG1196 610 EADARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 721 EISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKL 800
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*...
gi 1907156419 801 KETLAELE 808
Cdd:COG1196 770 ERLEREIE 777
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
589-865 |
1.37e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.60 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNA-SRETQKSLRQEHLAEKEKLAEKL--EQEEKLKAKIQQLTEEKAALEESIGQEKS--RSE 663
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSETDARIKLAAQEKIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 664 EALEKAQARVreLENHLASQKEALENSVAQEKRkmREMLEAERRkaqDLENQL-TQQKEISENNTYEKlkmrDTLEKEKR 742
Cdd:PLN02939 235 NMLLKDDIQF--LKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 743 KIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvedaqqmkttesqraetlalKLKETLAELETTKtkmiLTDDRLK 822
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907156419 823 LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 865
Cdd:PLN02939 355 LLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
49-219 |
1.43e-06 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 51.69 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 49 SIINQEHAPPPGLCTCRSDAESADI----DNH-------------HALIEFneAEGTFVLQDfNSRNGTFVNECHI---Q 108
Cdd:COG3456 6 RIINSPDLESGSAASATFGRGGGTIgrsaDCDwvlpdpdrsvsrrHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 109 NVAVKLIPGDILRFGSagmtYEL---VIENPSPVSCPWVRGPAPWPSPQPHLS--SSPPDMPFHHGIQPATVQRSWSQGC 183
Cdd:COG3456 83 GRPVRLRDGDRLRIGD----YEIrveISGEDEGADDPLAAAPEPAVSSPSNLSdtEAAPDAALAFSFSLDPLEALDEAAT 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907156419 184 PRPTMVPPAPHQRPMSASGKMFSFVMDPKSPVINQV 219
Cdd:COG3456 159 EAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQL 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
597-764 |
1.94e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 597 SQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 676
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 677 ENH------------------LASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 738
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 1907156419 739 KEKRKIQDLENRLTKQKEEIELKEQK 764
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
595-730 |
2.39e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.56 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 595 IMSQSQDLQAQMNASRETQKSlrQEHLaEKEKLAEKLEQEEKlKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQA 671
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEA--RGRL-ERQKMHDKAKAEEQ-RTKLLELQAESAAVEssgQSRAEALAEAEARLIEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 672 RVRELEnhLASQKEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEIS--ENNTYEK 730
Cdd:PTZ00491 735 EVEQAE--LRAKALRIEAEAELEKLRKRQELELEYEQAQN-ELEIAKAKELAdiEATKFER 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-774 |
3.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMS---------QSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE------EKLKAKIQQLTEEKAALE 652
Cdd:COG4913 230 LVEHFDDLERahealedarEQIELLEPIRELAERYAAARER-LAELEYLRAALRLWfaqrrlELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 653 EsigqEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENN-- 726
Cdd:COG4913 309 A----ELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907156419 727 TYEKLK--MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKD 774
Cdd:COG4913 381 EFAALRaeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
590-1006 |
4.62e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 590 EHYKKIMS----QSQDLQAQMNASREtqkslrqehLAEKEKLAEKlEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA 665
Cdd:pfam15921 74 EHIERVLEeyshQVKDLQRRLNESNE---------LHEKQKFYLR-QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 666 LEKAQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTlekekrKIQ 745
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 746 DLENRLTKQKEEIELKeqkenvlNNKLKDALVMVEDAQQMKTTESQRAETLAL-----KLKETLAELETTKTKMILTDDR 820
Cdd:pfam15921 217 SLGSAISKILRELDTE-------ISYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 821 LKLQQQSmkaLQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYY----QKIEGEITTLKNNDTGPKEEAS 896
Cdd:pfam15921 290 ARSQANS---IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYedkiEELEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 897 QDltagpPLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKL-RTDLGEAHSrMSDLRGELSEKQkMELERQVALvrqqs 975
Cdd:pfam15921 367 QF-----SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwDRDTGNSIT-IDHLRRELDDRN-MEVQRLEAL----- 434
|
410 420 430
....*....|....*....|....*....|.
gi 1907156419 976 gelsmLKAKVAQTTGLMEKKDRELKVLREAL 1006
Cdd:pfam15921 435 -----LKAMKSECQGQMERQMAAIQGKNESL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
600-740 |
6.63e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 600 QDLQAQMNASRETQKSLRQEHLAEKEKLAE-KLEQEEKLKAKIQQLTEEKAALE----------ESIGQEKSRSEEALEK 668
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 669 AQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNtyekLKMRDTLEKE 740
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----LALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
389-653 |
7.57e-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: 49.38 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 389 ARNEQVQQLQEEVNRLRIENREKEYQLEALSsrcsvmkeelRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK 468
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALK----------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 469 KNymgQNIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQacmrdscSSIDLKKEVELLQHlplsplVSGLQKT 548
Cdd:COG4942 87 EL---EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKY------LAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 549 VVNILRVSLSWLEETEQLLGDLDIELSdsdkgfslcliyllEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLA 628
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELE--------------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|....*
gi 1907156419 629 EKLEQEEKLKAKIQQLTEEKAALEE 653
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
553-903 |
7.59e-06 |
|
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: 49.97 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 553 LRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQkslrQEHLAEKEKLAEKLE 632
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ----EEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 633 QEEKLKAKIQQLTEEKAALEESIGQEKSRSE-EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmlEAERRKAQD 711
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKAAPLAAHiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ--QSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 712 LENQLTQQKEISENNTYEKLKMRDTLEKEKrkiqDLENRLTKQKEEIELKEQKENVLNNKLKdalvmVEDAQQmKTTESQ 791
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQH----TLTQHIHTLQQQKTTLTQKLQSLCKELD-----ILQREQ-ATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 792 RAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLEERLCQVT 871
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVL 493
|
330 340 350
....*....|....*....|....*....|..
gi 1907156419 872 QYYQKIEGEITTLKNNDTGPKEEASQDLTAGP 903
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
615-838 |
7.75e-06 |
|
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: 48.99 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 615 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQ---------LTEEKAALEESiGQEKSRSEEALEKAQARVRELEN---HLAS 682
Cdd:pfam09787 4 SAKQELADYKQKAARILQSKEKLIASLKEgsgvegldsSTALTLELEEL-RQERDLLREEIQKLRGQIQQLRTelqELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 683 QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLekeKRKIQDLENRLTKQKEEIELKE 762
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156419 763 QkenvlnnklkdalvmvEDAQQMKTTESQRAETLALKLKETLAE-LETTKTKMILTDDRLklqQQSMKALQDERESQ 838
Cdd:pfam09787 160 Q----------------SSSSQSELENRLHQLTETLIQKQTMLEaLSTEKNSLVLQLERM---EQQIKELQGEGSNG 217
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
69-123 |
8.31e-06 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 45.17 E-value: 8.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 69 ESADIDNHHALIEFnEAEGTFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 123
Cdd:cd22683 36 SDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
596-1007 |
8.60e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 596 MSQSQDLQAQMNAsRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESigqeKSRSEEALEKAQARVR 674
Cdd:PTZ00121 1262 MAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEA----KKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 675 ELEnhlaSQKEALENSVAQEKRKMREMLEAERR-KAQDLENQLTQQKEISENNTYEKLKMRDTL----EKEKRKIQDLEN 749
Cdd:PTZ00121 1337 KAE----EAKKAAEAAKAEAEAAADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaEEDKKKADELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 750 RLTKQKEEIELKEQKENVlnNKLKDALVMVEDAQQM-----KTTESQRAETLALKLKETLAELETTKTkmilTDDRLKLQ 824
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 825 QQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 904
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 905 LDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAK 984
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420
....*....|....*....|...
gi 1907156419 985 VAQTTGLMEKKDRELKVLREALR 1007
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEA 1667
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
548-678 |
9.99e-06 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.86 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 548 TVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLqaqMNASRETQKSLRQEHLAEKEKL 627
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE---LDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 628 AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELEN 678
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKLLQS 285
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
64-123 |
1.10e-05 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 45.35 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 123
Cdd:cd22724 30 CELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-855 |
1.16e-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: 49.40 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 352 LAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsVMKEELRK 431
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKR----------KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR--LEEETAQK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 432 EEAQKDRREAQ------EKELKLCRSQMQDMEKEVRKLREELkknymgqniisktlrEKNKLENFRNQVIKATFGKTKPF 505
Cdd:pfam01576 260 NNALKKIRELEaqiselQEDLESERAARNKAEKQRRDLGEEL---------------EALKTELEDTLDTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 506 RDKPITDQQACMRDSCSSIDLKKEVELLQHlplSPLVSGLQKTVVNILRVSLSWlEETEQLLGDLDIELSDSDKGFSLCL 585
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKH---TQALEELTEQLEQAKRNKANL-EKAKQALESENAELQAELRTLQQAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 586 IYLLEHYKKIMSQSQDLQAQMNASrETQKSLRQEHLAE------------------------------------KEKLAE 629
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSES-ERQRAELAEKLSKlqselesvssllneaegkniklskdvsslesqlqdtQELLQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 630 KLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELENHLASQKEALEnsvaQEKRKMREMLEAERRKA 709
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEE----EEAKRNVERQLSTLQAQLSDMKKKLE----EDAGTLEALEEGKKRLQ 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 710 QDLENqLTQQKEisenntyEKLKMRDTLEKEKRKIQ----DLENRLTKQKEEIELKEQKENVLNNKL---KDALVMVEDA 782
Cdd:pfam01576 552 RELEA-LTQQLE-------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQLVSNLEKKQKKFDQMLaeeKAISARYAEE 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 783 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD-------ERESQKHGFEEEISEYKEQIKQ 855
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhELERSKRALEQQVEEMKTQLEE 703
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
560-721 |
1.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 560 LEETEQLLGDLDIELSDsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQkSLRQEHLAEKEKLAEKLEQEEKLKA 639
Cdd:COG3206 221 LSELESQLAEARAELAE--------AEARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 640 KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRK--AQDLENQLT 717
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLL 371
|
....
gi 1907156419 718 QQKE 721
Cdd:COG3206 372 QRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
622-808 |
1.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 622 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREM 701
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 702 LEAERRK-----------AQDLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN 770
Cdd:COG3883 96 YRSGGSVsyldvllgsesFSDFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907156419 771 KLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 808
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
246-494 |
1.45e-05 |
|
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: 48.97 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 246 MDHDLSQQDKDEiillLGREVNRLSDFEMESKYKDALiMNLQAEVADLSQRLsetaavaaARQSNRCDPKLQGVD---EG 322
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM--------AMERERELERIRQEErkrEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 323 DDLRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDHAITSGMVTSLQKDMSARNEQVQQL 397
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 398 QEE----VNRLRIENREKEYQLEAL--------SSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLRE 465
Cdd:pfam17380 441 EEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
250 260
....*....|....*....|....*....
gi 1907156419 466 ELKKNymgQNIISKTLREKNKLENFRNQV 494
Cdd:pfam17380 521 EMEER---QKAIYEEERRREAEEERRKQQ 546
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
367-1004 |
1.58e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 367 ENLKRDHAITSGMVTSLQKDMSARNE--QVQQLQEEVNRLRIENREKEYQLEAlSSRCSVMKEELRKEEAQKDRREAQEK 444
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNElhEKQKFYLRQSVIDLQTKLQEMQMER-DAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 445 ELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLRekNKLENFRNQVIKATFGK----TKPFRDkpitdqqacMRDS 520
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR--SILVDFEEASGKKIYEHdsmsTMHFRS---------LGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 521 CSSI--DLKKEVELLQH--LPLSPLVSGLQKTVVNILRVSLSWLEE-TEQLLGDLDIELSDsdkgfslcliyLLEHYKKI 595
Cdd:pfam15921 222 ISKIlrELDTEISYLKGriFPVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITG-----------LTEKASSA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 596 MSQSQDLQAQMNASRE---TQKSLRQEHLAEKEKLAEKLEQE------------EKLKAKI--------------QQLTE 646
Cdd:pfam15921 291 RSQANSIQSQLEIIQEqarNQNSMYMRQLSDLESTVSQLRSElreakrmyedkiEELEKQLvlanseltearterDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 647 EKAALEESIGQ-----EKSRSEEALEKAQARV----------------RELE--NHLASQKEALENSVAQE-KRKMREML 702
Cdd:pfam15921 371 ESGNLDDQLQKlladlHKREKELSLEKEQNKRlwdrdtgnsitidhlrRELDdrNMEVQRLEALLKAMKSEcQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 703 EAERRKAQDLEN------QLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL--------------TKQKEEIELKE 762
Cdd:pfam15921 451 AAIQGKNESLEKvssltaQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLqekeraieatnaeiTKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 763 QKENVLNNKlKDALVMVE---DAQQMKTTESQRAETLALKLKETLAEL-------------ETTKTKMILTDDRLKLQQq 826
Cdd:pfam15921 531 QELQHLKNE-GDHLRNVQtecEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtagamqvEKAQLEKEINDRRLELQE- 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 827 sMKALQDERESQKHGFEEEISEYK-EQIKqhsqTIVSLEERLCQVTQYYQKIEGEITTLKN--NDTGPKEEASQDLTAGP 903
Cdd:pfam15921 609 -FKILKDKKDAKIRELEARVSDLElEKVK----LVNAGSERLRAVKDIKQERDQLLNEVKTsrNELNSLSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 904 PLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHsrmsdlrgelseKQKMELERQVALVRqqsGELSMLKA 983
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM------------KVAMGMQKQITAKR---GQIDALQS 748
|
730 740
....*....|....*....|.
gi 1907156419 984 KVAQTTGLMEKKDRELKVLRE 1004
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKE 769
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
546-807 |
1.75e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 546 QKTVVNILRVSLSWLEETEQLLGDLDielsdsdkgfslcliylleHYKKIMSQ----SQDLQAQMNASRETQKSLRqEHL 621
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNfpklSAELRQQLNNERDEPRSVP-PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 622 AEKEklaekLEQeEKLKAKIQQLTEEKAALEEsigQEKSR----SEEALEKAQARVRELENHLASQKEALENS---VAQE 694
Cdd:PRK10929 103 STDA-----LEQ-EILQVSSQLLEKSRQAQQE---QDRAReisdSLSQLPQQQTEARRQLNEIERRLQTLGTPntpLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 695 KRKMREMlEAERRKAQDLENQLTQqkeISENNTYEKLKMRDTLEKEKR-----KIQDLENRLTKQ-KEEIE--------L 760
Cdd:PRK10929 174 QLTALQA-ESAALKALVDELELAQ---LSANNRQELARLRSELAKKRSqqldaYLQALRNQLNSQrQREAEralestelL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 761 KEQKENV---------LNNKLKDALvmVEDAQQMKTTESQR--AETLALKLKETLAEL 807
Cdd:PRK10929 250 AEQSGDLpksivaqfkINRELSQAL--NQQAQRMDLIASQQrqAASQTLQVRQALNTL 305
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
619-869 |
1.76e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 619 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG-QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRk 697
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 698 mremLEAERRKAQDLENQLTQQkeISENNTyeklkmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDA-L 776
Cdd:COG4913 314 ----LEARLDALREELDELEAQ--IRGNGG--------------DRLEQLEREIERLERELEERERRRARLEALLAALgL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 777 VMVEDAQQMKTTESQRAETLAlKLKETLAELETTKtkmiltdDRLKLQQQsmkALQDERESQkhgfEEEISEYKEQIKQH 856
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE-ALEEELEALEEAL-------AEAEAALR---DLRRELREL----EAEIASLERRKSNI 438
|
250
....*....|...
gi 1907156419 857 SQTIVSLEERLCQ 869
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-858 |
1.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 605 QMNASRETQKSLRQEHLAEKEKLAE--KLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 682
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 683 QKEALENSVAQEKRKMREMLEAER-RKAQDLEnQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLEnRLTKQKEEIE 759
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVK-KAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 760 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAEtlalklkETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQK 839
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250
....*....|....*....
gi 1907156419 840 HGFEEEISEYKEQIKQHSQ 858
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKAD 1332
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
621-748 |
2.06e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 47.67 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 621 LAEKEKLAEKLEQEE----KLKAKIQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHLASQ 683
Cdd:pfam02841 154 LEERDKLEAKYNQVPrkgvKAEEVLQEFLQSKEAVEEAILQtdqaltakekaieAERAKAEAAEAEQELLREKQKEEEQM 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 684 KEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 748
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEKMEAEREQLLA-EQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-852 |
2.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 624 KEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqeksrseEALEKAQARVRELENHLASQKEalensvaqekrkmremLE 703
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL--------DALQERREALQRLAEYSWDEID----------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 704 AERRKAQDLENQLTQqkeISENNtyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQ 783
Cdd:COG4913 665 SAEREIAELEAELER---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 784 -QMKTTESQRAETLALKLKETLAELETTKtkmILTDDRLKLQQQsMKALQDERESQKHGFEEEISEYKEQ 852
Cdd:COG4913 734 dRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
396-1010 |
2.33e-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: 48.43 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 396 QLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNymgQN 475
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY---LK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 476 IISKTLREKNKLENFRNQVIKATFGKTKPFRDKpITDQQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRV 555
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEK-LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 556 SlSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKImSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEE 635
Cdd:pfam02463 313 E-EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKR-EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 636 KLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 715
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 716 LTQQKEISE-NNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN---NKLKDALVMVEDAQQMKTTESQ 791
Cdd:pfam02463 471 EDLLKETQLvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIsahGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 792 RAETLALKLKETLAELETTKTKmiLTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVT 871
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTE--LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 872 QYYQKIEGEITTLKNNDTGPKE--EASQDLTAGPPLDSGDKEIA-CDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSR 948
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKgvSLEEGLAEKSEVKASLSELTkELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 949 MSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRCGK 1010
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
608-1007 |
2.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 608 ASRETQKSLRQEHLAEKEKLAEkLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELE------NHL 680
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 681 ASQKEALENsvaqEKRKMREMLEAERRKAQDLENQ---LTQQKEISENNTYEKLKMRDTLEKEkrkIQDLENRLTKQKEE 757
Cdd:PRK02224 313 EARREELED----RDEELRDRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 758 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmilTDDRLKLQQQsmkaLQDERES 837
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT-------ARERVEEAEA----LLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 838 QKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNndtgpkeeasqdltagppLDSGDKEIacDHL 917
Cdd:PRK02224 455 PECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------------------LVEAEDRI--ERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 918 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKqkmelERQVALVRQQSGElsmlkakVAQTTGLMEKKDR 997
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK-----REAAAEAEEEAEE-------AREEVAELNSKLA 582
|
410
....*....|
gi 1907156419 998 ELKVLREALR 1007
Cdd:PRK02224 583 ELKERIESLE 592
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
76-123 |
2.41e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 43.86 E-value: 2.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907156419 76 HHALIEFneAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 123
Cdd:cd22694 38 RHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
76-123 |
2.42e-05 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 44.95 E-value: 2.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907156419 76 HHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDILRFG 123
Cdd:cd22679 52 NHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDIVQFG 102
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
393-846 |
2.70e-05 |
|
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: 48.20 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 393 QVQQLQEEVNRLRIENREKEYQLEALSSRCSvmkeelRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYM 472
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALK------RQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 473 GQNIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQACmrdscSSIDLKKEVELLQHLPLSPLVSGLQKTVVNi 552
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL-----QSTNSELEELQERLDLLKAKASEAEQLRQN- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 553 LRVSLSWLEETEQLLGDLDIELSdsdkgfslcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQE--HL--------- 621
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQ------------SQEQDSEIVKNSKSELARIPELEKELERLREHnkHLnenienkll 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 622 --AEKEKLAEKLEQEEKLKAKIQQLTEEKAALE------ESIGQEKSRSEEALEKAQARVRELENH---LASQKEALENS 690
Cdd:pfam05557 226 lkEEVEDLKRKLEREEKYREEAATLELEKEKLEqelqswVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 691 VAQEKRKMREM---LEAERRKAQDLENQLTQQKEISEN-------NTYEKLKMRDTLEKEKrKIQDLENRLTKQKEEIEL 760
Cdd:pfam05557 306 ARQLEKARRELeqeLAQYLKKIEDLNKKLKRHKALVRRlqrrvllLTKERDGYRAILESYD-KELTMSNYSPQLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 761 KEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL-----ALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDER 835
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLerelqALRQQESLADPSYSKEEV----DSLRRKLETLELERQRL 460
|
490
....*....|.
gi 1907156419 836 ESQKHGFEEEI 846
Cdd:pfam05557 461 REQKNELEMEL 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-826 |
2.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 625 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlaSQKEALENSVAQEKRKMREMLEA 704
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 705 ERRKAQDLENQLTQQKEISENNTYEKLKMR-DTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKDALVMVEDA 782
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907156419 783 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 826
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
603-710 |
2.72e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 603 QAQMNASRETQKSLRQehLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlas 682
Cdd:COG2268 223 AEEAELEQEREIETAR--IAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ----- 295
|
90 100
....*....|....*....|....*...
gi 1907156419 683 QKEAlENSVAQEKRKMREMLEAERRKAQ 710
Cdd:COG2268 296 EKEA-EREEAELEADVRKPAEAEKQAAE 322
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
593-855 |
2.78e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 672
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 673 VRELENHLASQKEalENSVAQEKRKMREMLEAERRKAQ------DLENQLTQQ-KEISenntyEKLKMRDTLEKEKRKIQ 745
Cdd:COG1340 91 REELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKiKELE-----KELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 746 DLENRLTKQKEEI-ELKEQKENVLN--NKLKDALV-MVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRL 821
Cdd:COG1340 164 ELRAELKELRKEAeEIHKKIKELAEeaQELHEEMIeLYKEADELR----KEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1907156419 822 -KLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 855
Cdd:COG1340 240 rELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
67-131 |
2.78e-05 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 44.21 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 67 DAESADI--DNH-----HALIEF----NEAEGTFVLQ------DFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGMT 128
Cdd:cd22676 28 DRRVADIplDHPscskqHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLSTRE 107
|
...
gi 1907156419 129 YEL 131
Cdd:cd22676 108 YVL 110
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
610-852 |
3.12e-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: 47.89 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLRQEHLAEKEKLAEKL-EQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaQARVRELENHLASQKEALE 688
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENkDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECS 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 689 NSVAQEKrKMREMLEAERRKA------QDLENQLTQQKEISENNTYEKLKMRDTL---EKEK----RKIQDLENRLTKQk 755
Cdd:pfam10174 535 KLENQLK-KAHNAEEAVRTNPeindriRLLEQEVARYKEESGKAQAEVERLLGILrevENEKndkdKKIAELESLTLRQ- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 756 eeieLKEQKENVLNNKLKDALVMVEDAQQM----KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQS---- 827
Cdd:pfam10174 613 ----MKEQNKKVANIKHGQQEMKKKGAQLLeearRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSlaek 688
|
250 260
....*....|....*....|....*...
gi 1907156419 828 ---MKALQDERESQKhgfeEEISEYKEQ 852
Cdd:pfam10174 689 dghLTNLRAERRKQL----EEILEMKQE 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
327-746 |
3.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 327 QKEIESMKSQINALQKGYSQV-LSQTLAERNTEIESLKNEGENLKRDHAitsgMVTSLQKDMSARNEQVQQLQEEVNRLR 405
Cdd:COG4717 108 EAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 406 IENREKEYQ--------LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLcRSQMQDMEKEVRKLREELkknyMGQNII 477
Cdd:COG4717 184 EQLSLATEEelqdlaeeLEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLL----LIAAAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 478 SKTLREKNKLENFRNQVIKATFgktkpfrdkpITDQQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKtvvnilrvsl 557
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLF----------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE---------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 558 swlEETEQLLGDLDIELSDSDKGFSLcLIYLLEHYKKIMSQSQDLQAQM--NASRETQKSLRQEHLAEKE----KLAEKL 631
Cdd:COG4717 319 ---EELEELLAALGLPPDLSPEELLE-LLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDEeelrAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 632 EQEEKLKAKIQQLTEE-KAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAER--RK 708
Cdd:COG4717 395 EEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaEL 474
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907156419 709 AQDLENQLTQQKEISEnnTYEKLKM-RDTLEKEKRKIQD 746
Cdd:COG4717 475 LQELEELKAELRELAE--EWAALKLaLELLEEAREEYRE 511
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
610-760 |
3.39e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLRQEHLAEKEKLAEKLEQE-----EKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQK 684
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 685 EALENSVAQEKrkmREMLEAERRKAQDLENQLT-QQKEISENNTYEKLK-MRDTLEKEKRKIQDLENRLTKQKEEIEL 760
Cdd:pfam15709 433 QELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
600-781 |
3.61e-05 |
|
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: 46.46 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 600 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRsEEALEKAQARV---REL 676
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 677 ENhLASQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQKEISEnntyeklKMRDTLEKEKRKIQDLENRLTK 753
Cdd:COG1579 92 EA-LQKEIESLKRRISDLEDEILELmerIEELEEELAELEAELAELEAELE-------EKKAELDEELAELEAELEELEA 163
|
170 180 190
....*....|....*....|....*....|....
gi 1907156419 754 QKEEI------ELKEQKENVLNNKLKDALVMVED 781
Cdd:COG1579 164 EREELaakippELLALYERIRKRKNGLAVVPVEG 197
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
76-129 |
4.05e-05 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 43.85 E-value: 4.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 76 HHALI-----EFNEAEG----TFVLQDFnSRNGTFVNECHIQNVA-VKLIPGDILRFGSAGMTY 129
Cdd:cd22667 42 KHATLtvlhpEANLSDPdtrpELTLKDL-SKYGTFVNGEKLKGGSeVTLKDGDVITFGVLGSKF 104
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
64-131 |
4.36e-05 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 43.38 E-value: 4.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 64 CRSDAESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGMTYEL 131
Cdd:cd22725 30 CELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
619-764 |
4.57e-05 |
|
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: 46.07 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 619 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR---SEEALEKAQARVRELENHLASQKEALENSVAQ-- 693
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARleaAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156419 694 EKRKMREM------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 764
Cdd:COG1579 84 NVRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
590-782 |
4.67e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 590 EHYKKimsQSQDLQAQMNASRETQKSLRQEH----LAEKEKLAEkleQEEKLKAKIQQLTEEKAALEESIGQEKSRSEE- 664
Cdd:PRK10929 211 ELAKK---RSQQLDAYLQALRNQLNSQRQREaeraLESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLi 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 665 ALEKAQA-----RVRELENHLASQK----------EALENSVAQ--EKRKM----REM--LEAERRKAQDLENQLTQQKE 721
Cdd:PRK10929 285 ASQQRQAasqtlQVRQALNTLREQSqwlgvsnalgEALRAQVARlpEMPKPqqldTEMaqLRVQRLRYEDLLNKQPQLRQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 722 ISENNTYeklkmrdTLEKEKRKIqdLENRLTKQKEEIE----------LKEQKENVLNNKLKDALVMVEDA 782
Cdd:PRK10929 365 IRQADGQ-------PLTAEQNRI--LDAQLRTQRELLNsllsggdtliLELTKLKVANSQLEDALKEVNEA 426
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
45-133 |
5.14e-05 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 43.97 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 45 GPSTSIINQEHAPPPGLCTCRSDAESADIDNHHALIEFNEAEGTFV--LQDFNSRNGTFVNECHI-QNVAVKLIPGDILR 121
Cdd:cd22681 38 SPSCYLIGREKGESTEIVVADIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDVIT 117
|
90
....*....|..
gi 1907156419 122 FgSAGMTYELVI 133
Cdd:cd22681 118 F-SKSNDYELVF 128
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
608-794 |
6.00e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 608 ASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLASQKEA 686
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 687 LENSVAQEKRKMR---------------------EMLEAERRKAQDLENQLTQQKEISENntyEKLKMRDTLEKEKRKIQ 745
Cdd:COG3883 88 LGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907156419 746 DLEnrltKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 794
Cdd:COG3883 165 ELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
593-767 |
6.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG------QEKSRSE--- 663
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 664 ----------------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEisennt 727
Cdd:COG3883 106 dvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEAQQA------ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907156419 728 yEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENV 767
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
593-855 |
7.56e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 672
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 673 VrelenhlASQKEALENSVAQEKrkmremlEAERRKAQDLENQLTQQKEISENntyeklkmrdtlEKEKRKIQDLENRLT 752
Cdd:TIGR02794 123 E-------AKAKQAAEAKAKAEA-------EAERKAKEEAAKQAEEEAKAKAA------------AEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 753 KQKEEIELKEQKENVLNNKLKdalvmvedAQQMKTTESQRAETLALKLKETLAELETTKTKMILT-DDRLKLQQQSMKAL 831
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAK--------AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAElGDIFGLASGSNAEK 248
|
250 260
....*....|....*....|....
gi 1907156419 832 QDERESQKHGfeEEISEYKEQIKQ 855
Cdd:TIGR02794 249 QGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
77-124 |
7.89e-05 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 43.42 E-value: 7.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907156419 77 HALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILRFGS 124
Cdd:cd22686 51 HAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
647-875 |
8.08e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 647 EKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAqekrkmremleAERRKAQDLENQLTQQKEISENN 726
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----------EETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 727 TYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK------EQKENVLNNKLkdalvmvEDAQQMKTTESQRAETLALkL 800
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawleEQKEQKREART-------EKQAYWQVVEGALDAQLAL-L 734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 801 KETLAELETTKtkmiltDDRLKLQQQSMKalqdeRESQKHGFEEE-ISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 875
Cdd:pfam12128 735 KAAIAARRSGA------KAELKALETWYK-----RDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFD 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
243-1007 |
8.34e-05 |
|
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: 46.96 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 243 EIFMDHDLSQQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSE-TAAVAAARQSNRCDPKLQGVDE 321
Cdd:TIGR00606 305 DLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEhIRARDSLIQSLATRLELDGFER 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 322 GDDLrQKEIESMKSQINALQKGYSQVLSQTLAERnTEIESLKNEGENLKRDHAITSGMVTSLQKDMsarneqvqqLQEEV 401
Cdd:TIGR00606 385 GPFS-ERQIKNFHTLVIERQEDEAKTAAQLCADL-QSKERLKQEQADEIRDEKKGLGRTIELKKEI---------LEKKQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 402 NRLRIENREKEyQLEALSSRCSVMKEELRKEEA------QKDRREAQEKELKLCRSQMQDMEKEVRKLREELKknymgqn 475
Cdd:TIGR00606 454 EELKFVIKELQ-QLEGSSDRILELDQELRKAERelskaeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME------- 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 476 iisktlrEKNKLENFRNQVIKATfgktkpfRDKPITDQQacMRDscssIDLKKEVELLQHLPLSPLVSGLQKTV------ 549
Cdd:TIGR00606 526 -------QLNHHTTTRTQMEMLT-------KDKMDKDEQ--IRK----IKSRHSDELTSLLGYFPNKKQLEDWLhskske 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 550 VNILRVSLSWLEET------------EQLLGDLDIELSDSDKGFSLC----LIYLLEHYKKIMSQSQDLQAQMNASRETQ 613
Cdd:TIGR00606 586 INQTRDRLAKLNKElasleqnknhinNELESKEEQLSSYEDKLFDVCgsqdEESDLERLKEEIEKSSKQRAMLAGATAVY 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 614 KSLRQEHLAEKEKL-----------AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELE----- 677
Cdd:TIGR00606 666 SQFITQLTDENQSCcpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeke 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 678 -------NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ----QKEISENN-TYEKLKMRD-------TLE 738
Cdd:TIGR00606 746 ipelrnkLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTImerfQMELKDVErKIAQQAAKLqgsdldrTVQ 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 739 KEKRKIQDLENRLTKQKEEIEL-----KEQKENVLN-----NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 808
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELnrkliQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 809 TTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQK-IEGEITTLK-- 885
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNaq 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 886 -NNDTGPKEEASQDL-TAGPPLDSGDKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKME 963
Cdd:TIGR00606 986 lEECEKHQEKINEDMrLMRQDIDTQKI--------------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907156419 964 LERQVALVRQqsgELSMLKAKVAQTTGLMEKKDRELKVLREALR 1007
Cdd:TIGR00606 1052 MKQEHQKLEE---NIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
601-886 |
9.80e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 601 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESIGQE----------------KS 660
Cdd:PTZ00440 956 NLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILNKKIDDLikkqhddiielidkliKE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 661 RSEEALEKAQARVRELEN--------HLASQKEALENSVAQEK-RKMREMLEAERRKAQDLENQLTQQKEISENNTY--- 728
Cdd:PTZ00440 1036 KGKEIEEKVDQYISLLEKmktklssfHFNIDIKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnad 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 729 -EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN----KLKDALVMVEDAQQMKTTESQRAETLALKLKET 803
Cdd:PTZ00440 1116 kEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 804 LAELETTKTKMILTD----DRLKLQQQSMKALQDERE----SQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 875
Cdd:PTZ00440 1196 KKDIDQVKKNMSKERndhlTTFEYNAYYDKATASYENieelTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN 1275
|
330
....*....|.
gi 1907156419 876 KIEGEITTLKN 886
Cdd:PTZ00440 1276 KMENALHEIKN 1286
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
600-872 |
1.08e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 600 QDLQAQMNASREtqkslrQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQeksrSEEALEKAQARVRELEN 678
Cdd:PRK11281 39 ADVQAQLDALNK------QKLLEAEDKLVQQdLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 679 HLASQ-KEALEN-SVAQEKRKMREMLEAERRKAQDLE-------NQLTQ----QKEISENNTyeklkmrdtlekekrKIQ 745
Cdd:PRK11281 109 DNDEEtRETLSTlSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQperaQAALYANSQ---------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 746 DLENRLTKQK-EEIELKEQKENVLNNKLkdALVMVEDAQQMKTTE----------SQRAEtlaLKLKETLAELETTKTKM 814
Cdd:PRK11281 174 QIRNLLKGGKvGGKALRPSQRVLLQAEQ--ALLNAQNDLQRKSLEgntqlqdllqKQRDY---LTARIQRLEHQLQLLQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 815 ILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQ 872
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQ 306
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
292-760 |
1.27e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 45.83 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 292 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENLKR 371
Cdd:COG5244 171 ELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSSVRECERSNIHDVLFLVNGILDGVIDELNGELERLRRQLVSLMS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 372 DHAITSGMVTSLQKDMsarnEQVQQLQEEVNRLRienrEKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ--EKEL--K 447
Cdd:COG5244 251 SHGIEVEENSRLKATL----EKFQSLELKVNTLQ----EELYQNKLLKKFYQIYEPFAQAALSSQLQYLAEviESENfgK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 448 LCRSQMQDMeKEVRKLREELKKNYMGQNIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQAC--MRDSCSSID 525
Cdd:COG5244 323 LENIEIHII-LKVLSSISYALHIYTIKNTPDHLETTLQCFVNIAPISMWLSEFLQRKFSSKQETAFSICqfLEDNKDVTL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 526 LKK------EVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKG-FSLCLIYLLEHYKKIMSQ 598
Cdd:COG5244 402 ILKilhpilETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQDNRLFlYPSCDITLSSILTILFSD 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 599 SQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKakiQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEN 678
Cdd:COG5244 482 KLEVFFQGIESLLENITIFPEQPSQQTSDSENIKENSLLS---DRLNEENIRLKEVLVQKENMLTEETKIKIIIGRDLER 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 679 hlASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMrdTLEKEKRKIQDLENRLTKQKEEI 758
Cdd:COG5244 559 --KTLEENIKTLKVELNNKNNKLKEENFNLVNRLKNMELKLYQIKDNNTLNKIYL--DLVSEIMELRETIRRQIKEQKRV 634
|
..
gi 1907156419 759 EL 760
Cdd:COG5244 635 SI 636
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
588-900 |
1.38e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALE 667
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 668 KAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 741
Cdd:pfam07888 126 AHEARIRELEEDIKTltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 742 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmVEDAQQMKTTESQRAETLALKLKETL------------AELET 809
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAaqrdrtqaelhqARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 810 TKTKMILTDDRLKLQQQSMKALQdERESQKHGFEEEiseyKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDT 889
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNR 356
|
330
....*....|.
gi 1907156419 890 GPKEEASQDLT 900
Cdd:pfam07888 357 VQLSESRRELQ 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-887 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 658 EKSRSEEALEKAQARVRELENHlasqKEALENsvAQEKRKMREMLEAERRKAQDLENQLTQQkeisenntyEKLKMRDTL 737
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA----HEALED--AREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 738 EKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAETLALKLKETLAELETTKTKMIL 816
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 817 TDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNN 887
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
635-759 |
1.50e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 635 EKLKAKIQQLTEEKAALEESigqEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKMREMLEAERRKAQDL 712
Cdd:COG0542 414 DELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAekELIEEIQELKEELEQRYGKIPEL 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 713 ENQLTQ-QKEISENNTYEKL--------------------KMrdtLEKEKRKIQDLENRLTK----QKEEIE 759
Cdd:COG0542 491 EKELAElEEELAELAPLLREevteediaevvsrwtgipvgKL---LEGEREKLLNLEEELHErvigQDEAVE 559
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
73-123 |
1.78e-04 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 41.77 E-value: 1.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 73 IDNHHALIEFN----EAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22677 41 ISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
618-748 |
2.10e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.49 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 618 QEHLAEKEKLAEKLEQEEK--LKAK--IQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHL 680
Cdd:cd16269 145 QLYLEDREKLVEKYRQVPRkgVKAEevLQEFLQSKEAEAEAILQadqaltekekeieAERAKAEAAEQERKLLEEQQREL 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 681 ASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLKMRDTLEKEKRKIQDLE 748
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKL-KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
623-877 |
2.22e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 623 EKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQ-EKSRSE--EALEKAQARVRELENhlasQKEAleNSVAQEKRKM 698
Cdd:pfam15905 91 EQDKRLQALEEElEKVEAKLNAAVREKTSLSASVASlEKQLLEltRVNELLKAKFSEDGT----QKKM--SSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 699 REMLEAERRKAQDLENQLTQQKEISENNtyeklkmrdtLEKEKRKIQDLENRL-TKQKEEIELKEQKENVLNNKLKdaLV 777
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKN----------LEHSKGKVAQLEEKLvSTEKEKIEEKSETEKLLEYITE--LS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 778 MVEDAQQMKTTESQRAETLalkLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgfEEEISEYKEQIKQHS 857
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEEL---LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLN 306
|
250 260
....*....|....*....|
gi 1907156419 858 QTIVSLEERLCQVTQYYQKI 877
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
695-999 |
2.53e-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: 45.11 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 695 KRKMREMLEAERRKAQDLENQLTQQKEISENNTY------------------EKLKMRDTLEKEKRKIQDLENRLTKQKE 756
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 757 EIE-LKEQKENVLNnklkDALVMVEDAQQMKTTEsqraETLALKLKETLAELETTKTKMILTDDrlKLQQQSMKALQDER 835
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD--SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 836 ESQKHGFEEEISEYK----------EQIKQHSQTIVSLeerlcQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL 905
Cdd:pfam15921 223 SKILRELDTEISYLKgrifpvedqlEALKSESQNKIEL-----LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 906 DSgdkeiacdhlidDLLMAQKEILSQQEIIMKLRTDLgeaHSRMSDLRGELSEKQKM------ELERQVALVRQQSGELS 979
Cdd:pfam15921 298 QS------------QLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEAR 362
|
330 340
....*....|....*....|
gi 1907156419 980 MLKAKVAQTTGLMEKKDREL 999
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKL 382
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
77-124 |
2.54e-04 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 41.19 E-value: 2.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1907156419 77 HALIEFNEAEGTFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 124
Cdd:cd22678 46 HARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
297-469 |
2.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 297 LSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRD 372
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 373 HAITSGMVTSLQKDMSARNE-----QVQQLQEEVNRLRIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELK 447
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180
....*....|....*....|..
gi 1907156419 448 LCRSQMQDMEKEVRKLREELKK 469
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEA 182
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
619-801 |
2.91e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 619 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVreLENHLASQKEALE---NSVAQEK 695
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAI----SGSQSQLESTDQNA--LETNGQAQRDAILeesRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 696 RKMREMLEAERRKAQ-------------------DLENQL--------TQQKEISENNTYEKLKMRDTLEKEK------- 741
Cdd:NF012221 1623 TTLAQGLDALDSQATyagesgdqwrnpfagglldRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEagvaqge 1702
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 742 RKIQDLENRLTKQKEEIELKEQ----KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK 801
Cdd:NF012221 1703 QNQANAEQDIDDAKADAEKRKDdalaKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
657-815 |
3.10e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 657 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEIsenntyeklkmrdt 736
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ-------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156419 737 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttesqrAETLALKLKETLAELETTKTKMI 815
Cdd:PRK12705 93 LDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP--------EQARKLLLKLLDAELEEEKAQRV 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
610-846 |
3.21e-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: 44.78 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLRQEHLAEKEKLAEKLEQEEK-LKAKIQQLTEEKAALEESIGQEK---SRSEEALEKAQARVRELENHLASQKE 685
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKeLEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 686 ALE------NSVAQEKRKMREMLeaerrkaQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 759
Cdd:pfam01576 83 RLEeeeersQQLQNEKKKMQQHI-------QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 760 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK---ETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 836
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 1907156419 837 SQKHGFEEEI 846
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
365-897 |
3.60e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 365 EGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEvnRLRIENREKEYQLEALSSRCSVMKEELRKEEAqkdRREAQEK 444
Cdd:pfam07111 116 EAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQE--QLSSLTQAHEEALSSLTSKAEGLEKSLNSLET---KRAGEAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 445 ELKLCRSQMQDMEKEVRKLREELK---------KNYMGQNIISKTLREKNKLEnfrNQVIKATFGKTKPFRDkpitDQQA 515
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEaqvtlveslRKYVGEQVPPEVHSQTWELE---RQELLDTMQHLQEDRA----DLQA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 516 CMR------DSCSSIDLKKEVELLQHL-PLSPLVSGLQKTVVNILRvslSWLEETEQLLGDL---DIELSDSDKGFSLCL 585
Cdd:pfam07111 264 TVEllqvrvQSLTHMLALQEEELTRKIqPSDSLEPEFPKKCRSLLN---RWREKVFALMVQLkaqDLEHRDSVKQLRGQV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 586 IYLLEhykKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSrSEEA 665
Cdd:pfam07111 341 AELQE---QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSS-TQIW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 666 LEKAQARVreleNHLASQKEALENSVAQEKRKMREMLEAERRKAqdlenQLTQQKEISENNTYEKLKMRDTLEKEKRKIQ 745
Cdd:pfam07111 417 LETTMTRV----EQAVARIPSLSNRLSYAVRKVHTIKGLMARKV-----ALAQLRQESCPPPPPAPPVDADLSLELEQLR 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 746 DLENRLTK---------QKEEIELKEQKEnvlnnklKDALVMVEDAQQMKTTESQRAETLA---LKLKETL-AELETTKT 812
Cdd:pfam07111 488 EERNRLDAelqlsahliQQEVGRAREQGE-------AERQQLSEVAQQLEQELQRAQESLAsvgQQLEVARqGQQESTEE 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 813 KMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI----KQHSQTIVSLEERLCQVTQYYQKIEgEITTLKnnD 888
Cdd:pfam07111 561 AASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLnearREQAKAVVSLRQIQHRATQEKERNQ-ELRRLQ--D 637
|
....*....
gi 1907156419 889 TGPKEEASQ 897
Cdd:pfam07111 638 EARKEEGQR 646
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
682-904 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 682 SQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEIsenntyeklkmrDTLEKEkrkIQDLENRLTKQKEEIE- 759
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEAlQAEI------------DKLQAE---IAEAEAEIEERREELGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 760 -LKEQKENVLNNKLKDALVMVED-------AQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKAL 831
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156419 832 QDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 904
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
623-746 |
3.75e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 43.66 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 623 EKEKLAEKLEQEEK-----LKAKIQQLTEEKAALEESIGQEKSRseealekaqarvreLENHLASQKEALENSVAQEKRK 697
Cdd:pfam09755 93 EKETLAMNYEQEEEfltndLSRKLTQLRQEKVELEQTLEQEQEY--------------QVNKLMRKIEKLEAETLNKQTN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907156419 698 mremLEAERRKAQDLENQLTQQKEISENNTYEKLkmrDTLEKEKRKIQD 746
Cdd:pfam09755 159 ----LEQLRREKVELENTLEQEQEALVNRLWKRM---DKLEAEKRLLQE 200
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
601-867 |
4.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 601 DLQAQMNASRETQKSLRQEHLAEKEKLA---------EKLEQ-EEKLKAKIQQLTEEKAALEESIGQeKSRSEEALEKAQ 670
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERyQADLEELEERLEEQNEVVEEADEQ-QEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 671 ARVRELENHLASQKEALEnsvAQEKR--------------------------KMREMLEAERRKAQDLENQLTQ--QK-- 720
Cdd:PRK04863 390 EEVDELKSQLADYQQALD---VQQTRaiqyqqavqalerakqlcglpdltadNAEDWLEEFQAKEQEATEELLSleQKls 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 721 ---------------------EISENN----------TYEKLKMRD-TLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 768
Cdd:PRK04863 467 vaqaahsqfeqayqlvrkiagEVSRSEawdvarellrRLREQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 769 NNKLKDALV----------MVEDAQQMKTTESQRAETLALKLKET---LAELETTKTKMILTDDRL-KLQQQS------- 827
Cdd:PRK04863 547 GKNLDDEDEleqlqeeleaRLESLSESVSEARERRMALRQQLEQLqarIQRLAARAPAWLAAQDALaRLREQSgeefeds 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907156419 828 ------MKALQD-ERESQ--KHGFEEEISEYKEQIKQHSQTIVSLEERL 867
Cdd:PRK04863 627 qdvteyMQQLLErERELTveRDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
64-103 |
4.39e-04 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 39.08 E-value: 4.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907156419 64 CRSDAESADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVN 103
Cdd:smart00240 10 CDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
597-754 |
5.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 597 SQSQDLQAQMNASRETQKSLR---------------QEHLAEKEKLAEKLE-----------QEEKLKAKIQQLTEEKAA 650
Cdd:COG4913 631 ERLEALEAELDALQERREALQrlaeyswdeidvasaEREIAELEAELERLDassddlaaleeQLEELEAELEELEEELDE 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 651 LEESIGQeksrseeaLEKAQARVRELENHLASQKEALENSVAQEkrkMREMLEaERRKAQDLENqltQQKEISENntyek 730
Cdd:COG4913 711 LKGEIGR--------LEKELEQAEEELDELQDRLEAAEDLARLE---LRALLE-ERFAAALGDA---VERELREN----- 770
|
170 180
....*....|....*....|....
gi 1907156419 731 lkMRDTLEKEKRKIQDLENRLTKQ 754
Cdd:COG4913 771 --LEERIDALRARLNRAEEELERA 792
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
561-869 |
5.39e-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: 44.01 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 561 EETEQLLGDLDIELSDSDKgfslCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK 640
Cdd:pfam01576 71 QELEEILHELESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 641 IQQLTEEKAALEESIGQEKSRSEEALEKAQArVRELENHLASQKEALENSVAQEKrKMREMLEAERRK----AQDLENQL 716
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKlegeSTDLQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 717 T-QQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTtesqRAET 795
Cdd:pfam01576 225 AeLQAQIAE--------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN----KAEK 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 796 LALKLKEtlaELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ----HSQTIVSLEERLCQ 869
Cdd:pfam01576 293 QRRDLGE---ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQ 367
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
589-794 |
5.95e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEK 668
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 669 -------AQARVRELENHLASQKEA-------LENSVAQEKRKMREmleaERRKAQDLENQLtqqkEISENNTYEKLKMR 734
Cdd:pfam17380 465 lrqqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIE----EERKRKLLEKEM----EERQKAIYEEERRR 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 735 DTlEKEKRKIQDLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAE 794
Cdd:pfam17380 537 EA-EEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREMMRQIVESEKARAE 590
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
597-854 |
6.17e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 597 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 676
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 677 ENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKE 756
Cdd:COG4372 153 KE-LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 757 EIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 836
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
250
....*....|....*...
gi 1907156419 837 SQKHGFEEEISEYKEQIK 854
Cdd:COG4372 312 ALEDALLAALLELAKKLE 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
729-860 |
6.85e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 729 EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENvlnnKLKDALVMVEDAQQMK------TTESQRAETLALKLKE 802
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 803 TLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 860
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-1000 |
7.39e-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: 43.52 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 392 EQVQQLQEEVNRLRIENREKEYQLEALSsrcsvmKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNY 471
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 472 MGQNIISKTLREKNKLENFRNQVIKATFGKTKPFRDKPITDQQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVN 551
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 552 ILRVslswLEETEQLLGDLDIELSDSDKgFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKL 631
Cdd:TIGR02169 331 IDKL----LAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 632 EQEEKLKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnSVAQEKRKMRE---MLEAE 705
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS-KYEQELYDLKEeydRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 706 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE-----------------------------------------KRKI 744
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavaKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 745 QDLENR---------LTKQKEE-------------------IELKEQKENVLNNKLKDALVmVED--------------- 781
Cdd:TIGR02169 565 ELLKRRkagratflpLNKMRDErrdlsilsedgvigfavdlVEFDPKYEPAFKYVFGDTLV-VEDieaarrlmgkyrmvt 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 782 ---------------------AQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK----------- 829
Cdd:TIGR02169 644 legelfeksgamtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdasrkigeiek 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 830 ---ALQDERESQKHGFEE----------EISEYKEQIKQHSQTIVSLEERLCQ----VTQYYQKIEGEITTLKNNDTGPK 892
Cdd:TIGR02169 724 eieQLEQEEEKLKERLEEleedlssleqEIENVKSELKELEARIEELEEDLHKleeaLNDLEARLSHSRIPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 893 EEASQDLTAgpPLDSGDKEIACDHLIDDLLmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVR 972
Cdd:TIGR02169 804 EEEVSRIEA--RLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-ELEELEAALR 878
|
730 740
....*....|....*....|....*...
gi 1907156419 973 QQSGELSMLKAKVAQttglMEKKDRELK 1000
Cdd:TIGR02169 879 DLESRLGDLKKERDE----LEAQLRELE 902
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
585-852 |
7.61e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 585 LIYLLEHYKKIMSQSQDlQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR--- 661
Cdd:COG5185 287 LIKQFENTKEKIAEYTK-SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEien 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 662 --SEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLE-NQLTQQKEISENNTYEKLKMRDT 736
Cdd:COG5185 366 ivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtlKAADRQiEELQRQIEQATSSNEEVSKLLNE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 737 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKlkdalvmvEDAQQmkttESQRAETLALKLKETLAELETTKTKMI- 815
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRSKK--------EDLNE----ELTQIESRVSTLKATLEKLRAKLERQLe 513
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907156419 816 LTDDRLKLQQQSMKALQDERE-SQKHGFEEEISEYKEQ 852
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARGyAHILALENLIPASELI 551
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
642-974 |
8.09e-04 |
|
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: 43.67 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 642 QQLTEEKAALEESIGQEKSRS---EEALEKAQARVRELENHLASQKEALENS----------VAQEKRKMREMLEAERRK 708
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQaaaEEQLVQANGELEKASREETFARTALKNArldlrrlfdeKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 709 AQDLENQLTQQKEISENntyeklKMRDTLEKEKRkiQDLENRLTKQKEEIELKEQKENVLnNKLKDALVMVEDAQ--QMK 786
Cdd:pfam12128 680 ANERLNSLEAQLKQLDK------KHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQL-ALLKAAIAARRSGAkaELK 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 787 TTESQRAETLA---------LKLKETLAELETTKTKmiLTDDRLKL------QQQSMKALQDERESQKHGFEEEISEYKE 851
Cdd:pfam12128 751 ALETWYKRDLAslgvdpdviAKLKREIRTLERKIER--IAVRRQEVlryfdwYQETWLQRRPRLATQLSNIERAISELQQ 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 852 QIKQHSQtivSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ--DLTAGPPLDSGDKEIA-CDHLIDDLLM----- 923
Cdd:pfam12128 829 QLARLIA---DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlaTLKEDANSEQAQGSIGeRLAQLEDLKLkrdyl 905
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 924 ---AQKEILSQQEIIMKLR-TDLGEAHSRMSDLRGELSEKQKMEL-ERQVALVRQQ 974
Cdd:pfam12128 906 sesVKKYVEHFKNVIADHSgSGLAETWESLREEDHYQNDKGIRLLdYRKLVPYLEQ 961
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
591-886 |
8.45e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 591 HYKKIMSQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQ 670
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEE-------LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 671 ARVRELE-------------NHLASQK--EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisennTYEKLKMR- 734
Cdd:pfam06160 153 KQLAEIEeefsqfeeltesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 735 ---DTLEKEKRkIQDLENRLTKQKEEI---ELKEQKENVLN-----NKLKDALVMVEDAQQ-----MKTTESQRAETLAl 798
Cdd:pfam06160 228 yalEHLNVDKE-IQQLEEQLEENLALLenlELDEAEEALEEieeriDQLYDLLEKEVDAKKyveknLPEIEDYLEHAEE- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 799 KLKETLAELETTKTKMILTDDRLKLQQQsmkaLQDERESQKHGFEeeisEYKEQIKQHSQTIVSLEERLCQVTQYYQKIE 878
Cdd:pfam06160 306 QNKELKEELERVQQSYTLNENELERVRG----LEKQLEELEKRYD----EIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
....*...
gi 1907156419 879 GEITTLKN 886
Cdd:pfam06160 378 EEQEEFKE 385
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
625-883 |
8.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 625 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaqEKRKMREMLEA 704
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 705 ERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQ 784
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 785 MKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLE 864
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*....
gi 1907156419 865 ERLCQVTQYYQKIEGEITT 883
Cdd:COG4372 273 TEEEELEIAALELEALEEA 291
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
286-719 |
8.54e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 286 LQAEVADLSQRLSETAAVAAARQSnrcdpKLQGVDEGDDLRQKEIESMKS-------QINALQKGYSQvLSQTLAERNTE 358
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTK-----QLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIEN-LQEQLRDKDKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 359 IESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRlriENREKEYQLEALSSRCSVMKEELRKEEAQKDR 438
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRER---EDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 439 REAQEKELK-LCRSQMQDMEKEVRKLREeLKKNymgqniISKTLREKNKLENfrnQVIKAtfgktkpfrdkpitdQQACM 517
Cdd:pfam10174 494 KESSLIDLKeHASSLASSGLKKDSKLKS-LEIA------VEQKKEECSKLEN---QLKKA---------------HNAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 518 rDSCSSIDLKKEVELL-QHLPLSPLVSGLQKTVVNILrvsLSWLEETEQLLGDLDIELSD------------SDKGFSLC 584
Cdd:pfam10174 549 -AVRTNPEINDRIRLLeQEVARYKEESGKAQAEVERL---LGILREVENEKNDKDKKIAElesltlrqmkeqNKKVANIK 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 585 LIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRS-E 663
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQlE 704
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 664 EALEKAQarvrelENHLA--SQKEA----LENSvAQEKRKMREMLEAERRKAQDLENQLTQQ 719
Cdd:pfam10174 705 EILEMKQ------EALLAaiSEKDAnialLELS-SSKKKKTQEEVMALKREKDRLVHQLKQQ 759
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
587-795 |
8.88e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 587 YLLEHYKKIMSQSQDLQAQMNASretqKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAL 666
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKEL----SSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 667 EKA--------QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQL-TQQKEISENNTYEKLKMRDTL 737
Cdd:pfam06008 103 EKVatlgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIqTWFQSPQEENKALANALRDSL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156419 738 EKEKRKIQDLENRLtkqkEEIELKEQKENVLNNKLKDALVMVEdaQQMKTTESQRAET 795
Cdd:pfam06008 183 AEYEAKLSDLRELL----REAAAKTRDANRLNLANQANLREFQ--RKKEEVSEQKNQL 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-804 |
9.17e-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: 43.18 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 286 LQAEVADLSQRLSEtaaVAAARQSNRcdpKLQGVDEGD----DLRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIES 361
Cdd:pfam15921 379 LQKLLADLHKREKE---LSLEKEQNK---RLWDRDTGNsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 362 LKNEGENLKRDHAITSG------MVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEA-------LSSRCSVMKEE 428
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQlestkeMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtnaeitkLRSRVDLKLQE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 429 LRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnyMGQnIISKTLREKNKLenfrnQVIKATFgktkpfrDK 508
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN--MTQ-LVGQHGRTAGAM-----QVEKAQL-------EK 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 509 PITDQQACMrdscssidlkKEVELLQhlplsplvsglqktvvnilrvslswlEETEQLLGDLDIELSDSDkgfslcliyl 588
Cdd:pfam15921 598 EINDRRLEL----------QEFKILK--------------------------DKKDAKIRELEARVSDLE---------- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEkLAEKLEQEEKLKAKIQQLTEEkaaLEESIGQEKSRseeaLEK 668
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE-LNSLSEDYEVLKRNFRNKSEE---METTTNKLKMQ----LKS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 669 AQARVRELENHLASQkEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 748
Cdd:pfam15921 704 AQSELEQTRNTLKSM-EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA 782
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 749 NRLTKQKEEIELKEQKENVLNNKLKDALVMVED-----AQQMKTTESQRAETLALKLKETL 804
Cdd:pfam15921 783 TEKNKMAGELEVLRSQERRLKEKVANMEVALDKaslqfAECQDIIQRQEQESVRLKLQHTL 843
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
542-831 |
9.29e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 542 VSGLQKTVvnILRVSLSWLEETEQLLGDLDIELSDSD--KGFSLCLIYLLEHYKKIMSQS--QDLQAQMNASRETQKSLR 617
Cdd:COG5022 861 FSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISslKLVNLELESEIIELKKSLSSDliENLEFKTELIARLKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 618 QEHLAE--------KEKLAEKLEQEEKLKakiqQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLaSQKEALEN 689
Cdd:COG5022 939 NIDLEEgpsieyvkLPELNKLHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS-KQYGALQE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 690 SVAQEKRKMREMLEAerrkaqdlenqltqqkeiseNNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEeiELKEQKENVLN 769
Cdd:COG5022 1014 STKQLKELPVEVAEL--------------------QSASKIISSESTELSILKPLQKLKGLLLLENN--QLQARYKALKL 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 770 NKlKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDD---RLKLQQQSMKAL 831
Cdd:COG5022 1072 RR-ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAqmiKLNLLQEISKFL 1135
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
633-839 |
9.74e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 633 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQA-RVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQD 711
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 712 LENQLTQQ--------KEISENNTYEKLkmRDTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKdalvmvEDA 782
Cdd:COG3206 241 RLAALRAQlgsgpdalPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDViALRAQIAALRAQLQQ------EAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156419 783 QQMKTTESQRaETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQK 839
Cdd:COG3206 313 RILASLEAEL-EALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAR 364
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
615-885 |
1.01e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 615 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 685
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 686 ALENsvAQEkrkMREMLEAERRKAQ----DLENQLT--------QQKEISENN----TYEKLK------------MRDTL 737
Cdd:PRK04863 370 VVEE--ADE---QQEENEARAEAAEeevdELKSQLAdyqqaldvQQTRAIQYQqavqALERAKqlcglpdltadnAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 738 EKEKRKIQDLENRL--TKQKEEI--ELKEQKENVLN--NKLKDAlVMVEDAQQ-----MKTTESQRAETLALK-LKETLA 805
Cdd:PRK04863 445 EEFQAKEQEATEELlsLEQKLSVaqAAHSQFEQAYQlvRKIAGE-VSRSEAWDvarelLRRLREQRHLAEQLQqLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 806 ELEttktkmiltdDRLKLQQQSMKALQDerESQKHG--------FEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 877
Cdd:PRK04863 524 ELE----------QRLRQQQRAERLLAE--FCKRLGknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
....*...
gi 1907156419 878 EGEITTLK 885
Cdd:PRK04863 592 QARIQRLA 599
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
614-766 |
1.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 614 KSLRQEHLAEKEKLAEKLEQEEKLKA------KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEAL 687
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 688 EnsvaqekrKMREMLEAERRKAQDLENQLTQQKEisennTYEKL--KMRDTLEK-------EKRKI--QDLENRLTKQK- 755
Cdd:PRK12704 106 E--------KREEELEKKEKELEQKQQELEKKEE-----ELEELieEQLQELERisgltaeEAKEIllEKVEEEARHEAa 172
|
170
....*....|....
gi 1907156419 756 ---EEIElKEQKEN 766
Cdd:PRK12704 173 vliKEIE-EEAKEE 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
598-808 |
1.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 598 QSQDLQAQMnasRETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQ-EKSRSEEALEKA---- 669
Cdd:pfam01576 799 QLKKLQAQM---KDLQRELEEARASRDEILAQSKESEKKLKnleAELLQLQEDLAASERARRQaQQERDELADEIAsgas 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 670 -----QARVRELENHLASQKEALENS-------------VAQEKRKMREMLEAERRKAQDLENQlTQQKEISENNTYEKL 731
Cdd:pfam01576 876 gksalQDEKRRLEARIAQLEEELEEEqsntellndrlrkSTLQVEQLTTELAAERSTSQKSESA-RQQLERQNKELKAKL 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 732 KMRDTLEKEKRK--IQDLENRLTKQKEEIElKEQKENVLNN--------KLKDALVMVEDAQQMKTTESQRAETLALKLK 801
Cdd:pfam01576 955 QEMEGTVKSKFKssIAALEAKIAQLEEQLE-QESRERQAANklvrrtekKLKEVLLQVEDERRHADQYKDQAEKGNSRMK 1033
|
....*..
gi 1907156419 802 ETLAELE 808
Cdd:pfam01576 1034 QLKRQLE 1040
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
610-858 |
1.51e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 610 RETQKSLRQEHLAEKEKLAEKLE-QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRElenhlasQKEALE 688
Cdd:pfam15709 263 ASERGAFSSDSVVEDPWLSSKYDaEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKRE-------QEKASR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 689 NSVAQEKRKMReMLEAErRKAQDLENQLTQQKEISENNTyeklKMRDTLEKEKRKIQDlENRLTKQKEEIELKEQKENVL 768
Cdd:pfam15709 336 DRLRAERAEMR-RLEVE-RKRREQEEQRRLQQEQLERAE----KMREELELEQQRRFE-EIRLRKQRLEEERQRQEEEER 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 769 NNKLKDALV--------------MVEDAQQMKTTESQRAETLALKLKETLAEL-ETTKTKMILT-DDRLKLQQQSMKA-- 830
Cdd:pfam15709 409 KQRLQLQAAqerarqqqeefrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLaEEQKRLMEMAeEERLEYQRQKQEAee 488
|
250 260
....*....|....*....|....*....
gi 1907156419 831 -LQDERESQKHGFEEEISEYKEQIKQHSQ 858
Cdd:pfam15709 489 kARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
588-889 |
1.65e-03 |
|
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: 42.73 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMSQSQDLQAQMNASRE-TQKSLRQEHLAEKEKLAEKL-----------EQEEKLKAKIQQLTEEKAALE--- 652
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKIENIvtkidkkkniyDEIKKLLNEIAEIEKDKTSLEevk 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 653 ---------------ESIGQEKSRSEEALEKAQARVRELENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLT 717
Cdd:TIGR01612 1214 ginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 718 QQK-------------EISENNtYEKLKMRD---TLEKEKRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDAL 776
Cdd:TIGR01612 1293 SKKhdenisdirekslKIIEDF-SEESDINDikkELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYT 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 777 VMVEDAQQMKTTESQRAETLALKLKETLAeLETTKTKMILTDDRLKLQQqsmkALQDERESQKHGFEEE--ISEYKEQIK 854
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLDDKDIDE----CIKKIKELKNHILSEEsnIDTYFKNAD 1446
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907156419 855 QHSQTIVSL---EERLCQVTQYYQKIEgeittlKNNDT 889
Cdd:TIGR01612 1447 ENNENVLLLfknIEMADNKSQHILKIK------KDNAT 1478
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
73-131 |
1.70e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 39.14 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 73 IDNHHALIEFNEAEGTFVLQDFnSRNGTFVNE--CHIQNVAVKLIPGDILRFGSAGMTYEL 131
Cdd:cd22701 46 ISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRSGSLIQIGGVLFYFLL 105
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
62-130 |
1.75e-03 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 38.73 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156419 62 CTCRSDaeSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMTYE 130
Cdd:cd22673 31 CDIRIQ--LPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFRFE 95
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
582-715 |
1.75e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.57 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 582 SLCLIYLL---EHYKKIMSQSQDLQAQMNASRETQKslrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQE 658
Cdd:pfam06785 47 SLCLLLLLyywEDALKEKFEKSFLEEKEAKLTELDA---EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156419 659 KSRSEEALEKAQARVRELENHLAsQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 715
Cdd:pfam06785 124 QIQLQQISQDFAEFRLESEEQLA-EKQLLINEYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
593-1004 |
1.79e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNaSRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK---IQQLTEEKAALEESIGQEKSRSEEALEKA 669
Cdd:TIGR00618 307 QQAQRIHTELQSKMR-SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 670 QAR--VRELENHLASQKEALENSVAQ------EKRKMREMLeAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 741
Cdd:TIGR00618 386 QQKttLTQKLQSLCKELDILQREQATidtrtsAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 742 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALklketlaELETTKTKMILTDDRL 821
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID-------NPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 822 KLQQQSMKALQDERESQKhgfeEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKnnDTGPKEEASQDLTA 901
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSER----KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 902 GpplDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDlrgELSEKQKMELERQVALVRQQSGELSML 981
Cdd:TIGR00618 612 C---EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE---RVREHALSIRVLPKELLASRQLALQKM 685
|
410 420
....*....|....*....|...
gi 1907156419 982 KAKVAQTTGLMEKKDRELKVLRE 1004
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAQCQTLLRE 708
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
589-688 |
2.06e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.97 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE--EKLKAKIQQLTEEKAALEESIG---QEKSRSE 663
Cdd:pfam13166 357 LDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHlvEEFKSEIDEYKDKYAGLEKAINsleKEIKNLE 436
|
90 100
....*....|....*....|....*
gi 1907156419 664 EALEKAQARVRELENHLASQKEALE 688
Cdd:pfam13166 437 AEIKKLREEIKELEAQLRDHKPGAD 461
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
327-437 |
2.11e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 327 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEqVQQLQEEVNRLRI 406
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 1907156419 407 ENREKEYQLEALSSRCSVMKeELRKEEAQKD 437
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSGE 509
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
679-886 |
2.18e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 679 HLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 758
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 759 -ELKEQKENVLNNK-----LKDALVMVEDAQQMKTT--------ESQRAETLALKLKETLAELETTKTKM--ILTDDRLK 822
Cdd:PRK05771 110 sELENEIKELEQEIerlepWGNFDLDLSLLLGFKYVsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 823 LQQQsmkalqdERESQKHGFEE-EISEykeqIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 886
Cdd:PRK05771 190 SDEV-------EEELKKLGFERlELEE----EGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
593-711 |
2.21e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKlAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 672
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907156419 673 VRELENHLASQKEALENSVAQEKRKMREmlEAERRKAQD 711
Cdd:PRK09510 162 KAAAEAKKKAEAEAAKKAAAEAKKKAEA--EAAAKAAAE 198
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
59-123 |
2.26e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 38.88 E-value: 2.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 59 PGLCTCRSDAESADIDNHHALIEFNeAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 123
Cdd:cd22663 29 LGVTYQLVSTCPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
611-853 |
2.29e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 611 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ------EKSRSEEALEKAQARVRELENHLaSQK 684
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeenSSWEKEEKRDSRLGRYKEEETEI-REK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 685 EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQK---EISENNTYEKLK----MRDTLEKEK----RKIQDLENRLTK 753
Cdd:pfam02029 139 EYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFakeEVKDEKIKKEKKvkyeSKVFLDQKRghpeVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 754 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMK-------TTESQRAETLALKLKETLAELETTKTKMiltDDRLKLQQQ 826
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEelrrrrqEKESEEFEKLRQKQQEAELELEELKKKR---EERRKLLEE 295
|
250 260
....*....|....*....|....*..
gi 1907156419 827 SMKALQDERESQKHGFEEEISEYKEQI 853
Cdd:pfam02029 296 EEQRRKQEEAERKLREEEEKRRMKEEI 322
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
311-858 |
2.46e-03 |
|
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: 41.96 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 311 RCDPKLQGVDEGDDLRQKEIESMKSQINALQKgysqVLSQTLAERN------------TEIESLKNEGENLKRdhaiTSG 378
Cdd:TIGR01612 1126 KIDHHIKALEEIKKKSENYIDEIKAQINDLED----VADKAISNDDpeeiekkienivTKIDKKKNIYDEIKK----LLN 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 379 MVTSLQKDMSARnEQVQQLQ----EEVNRLRIENREKEYQlealSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQ 454
Cdd:TIGR01612 1198 EIAEIEKDKTSL-EEVKGINlsygKNLGKLFLEKIDEEKK----KSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 455 DMEKEVRKLREELKKNYmgqNIISKtlREKNKLENFRNQVIKATFGKtkpFRDKPITDQQACMRDSCSSIDlKKEVELLQ 534
Cdd:TIGR01612 1273 KAEMETFNISHDDDKDH---HIISK--KHDENISDIREKSLKIIEDF---SEESDINDIKKELQKNLLDAQ-KHNSDINL 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 535 HL-PLSPLVSGLQ-KTVVNILRVSLSWLEETEQLLGDLDIELSDS-------------------------DKGFSLCLIY 587
Cdd:TIGR01612 1344 YLnEIANIYNILKlNKIKKIIDEVKEYTKEIEENNKNIKDELDKSeklikkikddinleeckskiestldDKDIDECIKK 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMSQSQDLQAQMNASRETQKSL------------RQEHLAEKEK----------LAEKLEQEEKLKAKIQQLT 645
Cdd:TIGR01612 1424 IKELKNHILSEESNIDTYFKNADENNENVlllfkniemadnKSQHILKIKKdnatndhdfnINELKEHIDKSKGCKDEAD 1503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 646 EEKAALEesigqeksRSEEALEKAQARVRELENHLASQkeALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISEN 725
Cdd:TIGR01612 1504 KNAKAIE--------KNKELFEQYKKDVTELLNKYSAL--AIKNKFAKTKKDSEIII----KEIKDAHKKFILEAEKSEQ 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 726 ntyeklKMRDtLEKEKRKIQD-LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESqraetlaLKLKETL 804
Cdd:TIGR01612 1570 ------KIKE-IKKEKFRIEDdAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETES-------IEKKISS 1635
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 805 AELETTKTKMILTDDRLKLQQQSMKALQDER---ESQKHGFEE---EISEYKEQIKQHSQ 858
Cdd:TIGR01612 1636 FSIDSQDTELKENGDNLNSLQEFLESLKDQKkniEDKKKELDEldsEIEKIEIDVDQHKK 1695
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
273-774 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 273 EMESKYKDA--LIMNLQAEVADLsQRLSETAAVAAARQSNrcdpKLQGVDEGDDLRQKEIESMKSQINALQKGysqvlSQ 350
Cdd:pfam05557 94 EKESQLADAreVISCLKNELSEL-RRQIQRAELELQSTNS----ELEELQERLDLLKAKASEAEQLRQNLEKQ-----QS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 351 TLAERNTEIESLKNEGENLKRDHAITsgmvtslqKDMSARNEQVQQLQEEVNRLRIENRekeyQLEALSSRCSVMKEELR 430
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIV--------KNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKEEVE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 431 KEEAQKDRREAQEKELKlcrsqmqDMEKEVRKLREELKK-----NYMGQNIIS-KTLREKNKLENFRNQVIKA-TFGKTK 503
Cdd:pfam05557 232 DLKRKLEREEKYREEAA-------TLELEKEKLEQELQSwvklaQDTGLNLRSpEDLSRRIEQLQQREIVLKEeNSSLTS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 504 PFRDKPITDQQacMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKtvvnilRVSLSWLEET--EQLLGDLDIELSDSDKGF 581
Cdd:pfam05557 305 SARQLEKARRE--LEQELAQYLKKIEDLNKKLKRHKALVRRLQR------RVLLLTKERDgyRAILESYDKELTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 582 SlcliyLLEHYKKIMSQSQDLQAQmNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEE--SIGQEK 659
Cdd:pfam05557 377 Q-----LLERIEEAEDMTQKMQAH-NEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvdSLRRKL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 660 SRSEEALEKAQARVRELENHLASQKEALENSVAQEK---RKMREMLEAERRKAQDLEnQLTQqkeisENNTYEKLKMRDT 736
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRKNQLE-KLQA-----EIERLKRLLKKLE 524
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907156419 737 LEKEKRKIQDLENRLTKQKEEIELKEQKE--NVLNNKLKD 774
Cdd:pfam05557 525 DDLEQVLRLPETTSTMNFKEVLDLRKELEsaELKNQRLKE 564
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
591-972 |
2.71e-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: 41.63 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 591 HYKKIMSQSqDLQAQMNASRETQKSLRQEHLAEKEKL---AEKLEQEEKLKAKIQQLTEEKAALEE-SIGQEKS--RSEE 664
Cdd:pfam05483 60 HYQEGLKDS-DFENSEGLSRLYSKLYKEAEKIKKWKVsieAELKQKENKLQENRKIIEAQRKAIQElQFENEKVslKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 665 ALEKAQARVRE--LENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLKMRDTLE 738
Cdd:pfam05483 139 EIQENKDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 739 KEKRKIQDLENrltKQKEEIELKEQKENVL-------NNKLKDALVMVEDAQQMKTTESQRAETLALKLKETL------- 804
Cdd:pfam05483 219 EDHEKIQHLEE---EYKKEINDKEKQVSLLliqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIekkdhlt 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 805 AELETTKTKMILT-------DDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 877
Cdd:pfam05483 296 KELEDIKMSLQRSmstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 878 EGEITTLknndTGPKEEASQDLTAGPPLdSGDKEIACDHLiDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRgELS 957
Cdd:pfam05483 376 EDQLKII----TMELQKKSSELEEMTKF-KNNKEVELEEL-KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL-QAR 448
|
410
....*....|....*
gi 1907156419 958 EKQKMELERQVALVR 972
Cdd:pfam05483 449 EKEIHDLEIQLTAIK 463
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
615-716 |
2.87e-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: 41.86 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 615 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 685
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvQTALRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110
....*....|....*....|....*....|....*
gi 1907156419 686 ALENsvAQEKrkmREMLEAERRKAQD----LENQL 716
Cdd:COG3096 369 VVEE--AAEQ---LAEAEARLEAAEEevdsLKSQL 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
608-1012 |
2.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 608 ASRETQ-KSLRQEHlaekEKLAEKLEQEEKLKAKIQQLTEekaALEESIGQEKSRS-----EEALEKAQARVRELENHLA 681
Cdd:PRK04863 782 AAREKRiEQLRAER----EELAERYATLSFDVQKLQRLHQ---AFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALA 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 682 SQKEALensvaqekRKMREMLEAERRKAQDLeNQLTQQKEISENNTYEKLKM-----RDTLEKEKRKIQDLENRLTKQKE 756
Cdd:PRK04863 855 DHESQE--------QQQRSQLEQAKEGLSAL-NRLLPRLNLLADETLADRVEeireqLDEAEEAKRFVQQHGNALAQLEP 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 757 EIE-LKEQKENvlNNKLKDAlvmVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDrlklqqqsmKALQDE- 834
Cdd:PRK04863 926 IVSvLQSDPEQ--FEQLKQD---YQQAQQTQRDAKQQAFALT-EVVQRRAHFSYEDAAEMLAKN---------SDLNEKl 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 835 RESQKHGfEEEISEYKEQIKQHsqtivslEERLCQVTQYYQKIEGEITTLKNNdtgpKEEASQDLTA-GPPLDSGDKEia 913
Cdd:PRK04863 991 RQRLEQA-EQERTRAREQLRQA-------QAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDlGVPADSGAEE-- 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 914 cdhliddllmaqkeilsqqeiimKLRTDLGEAHSRMSDLRGelsekQKMELERQVALvrqQSGELSMLKAKVaqttglmE 993
Cdd:PRK04863 1057 -----------------------RARARRDELHARLSANRS-----RRNQLEKQLTF---CEAEMDNLTKKL-------R 1098
|
410
....*....|....*....
gi 1907156419 994 KKDRELKVLREALRCGKGS 1012
Cdd:PRK04863 1099 KLERDYHEMREQVVNAKAG 1117
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
76-129 |
3.32e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 37.75 E-value: 3.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 76 HHAliEFNEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTY 129
Cdd:cd22684 43 RHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
737-840 |
3.42e-03 |
|
Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.
Pssm-ID: 283549 [Multi-domain] Cd Length: 398 Bit Score: 40.99 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 737 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALklketlaELETTKTKMIL 816
Cdd:pfam05917 129 LEQEKKEAENAEDRANKNGIELEQEKQKTNKSGIELANNQIKAEQEQQKTEQEKQKAEKEAI-------ELEQEKQKTIK 201
|
90 100
....*....|....*....|....
gi 1907156419 817 TDDRLKLQQQSMKALQDERESQKH 840
Cdd:pfam05917 202 TQRDLIKEQKDFIKETEQNCQENH 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-497 |
3.42e-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: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 326 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 405
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 406 --IENREKEYQ------------------------------LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQM 453
Cdd:COG4942 97 aeLEAQKEELAellralyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907156419 454 QDMEKEVRKLREELKKNYMGQNIISKTLREKNKLENFRNQVIKA 497
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-493 |
3.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 286 LQAEVADLSQRLSETAAVAAARQsnrcdpklqgvDEGDDLRQKeiesmKSQINALQKGYSQVLSQTLAERntEIESLKNE 365
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALE-----------AELDALQER-----REALQRLAEYSWDEIDVASAER--EIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 366 GENLKRDhaitSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELrkEEAQKDRREAQEKE 445
Cdd:COG4913 677 LERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907156419 446 LKLcRSQMQDMEKEVRKLREELKKNYMGQNiiSKTLREKNKLENFRNQ 493
Cdd:COG4913 751 LEE-RFAAALGDAVERELRENLEERIDALR--ARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
301-497 |
3.76e-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: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 301 AAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMV 380
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 381 TSLQKDMSARNEQVQQL------------------QEEVNR-------LRIENREKEYQLEALSSRCSVMKEELRKEEAQ 435
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156419 436 KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMG-QNIISKTLREKNKLENFRNQVIKA 497
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEALIARLEAE 235
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
589-808 |
3.92e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKL------------AEKLEQEEKLKAKIQQLTEEKAALEESIG 656
Cdd:pfam13868 65 EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMdeiveriqeedqAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 657 QEKSRSEEALEKAQARVRELENHLAS---QKEALENSVAQEKRKMREMLEAERRKAQDLENQLtQQKEISENNTYEKLKM 733
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEreaEREEIEEEKEREIARLRAQQEKAQDEKAERDELR-AKLYQEEQERKERQKE 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156419 734 RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvMVEDAQQMKTTESQRAETLALKLKETLAELE 808
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER--MLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| NFACT_N |
pfam05833 |
NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of ... |
588-770 |
4.02e-03 |
|
NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of NFACT (NEMF, FbpA, Caliban, and Tae2) proteins from eukaryotes, archaea and bacteria. Many members of this family act in ribosome quality control (RQC), including RqcH, which are involved in the addition of a poly-Ala tail to defective translated proteins to tag them for degradation. This process is analogous to the ssrA/tmRNA bacterial system. However, some other NFACT family members, such as bacterial proteins FbpA in Listeria or PavA in Streptococcus, are exported (despite lack of a classical signal peptide) and behave as fibronectin-binding adhesins associated with virulence.
Pssm-ID: 428644 [Multi-domain] Cd Length: 451 Bit Score: 40.69 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMSQSQDLQAQMNASRETQKS------LRQEHLAEK--EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEK 659
Cdd:pfam05833 229 LYEAFQDLLNQLESGNFEPTLYYDDEPKdfsvlpLSHLGLEKEtfDSLSELLDEYYAEKAERDRVKQKRSDLEKVVQNEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 660 SRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMleaerrkaqDLENQLTQQKEI----------SEN-- 725
Cdd:pfam05833 309 EKLEKKLKKLEKELEEAENADEYRLygELLTANLYQIKKGMKEV---------ELPNYYDEGEPVtipldpakspSENaq 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907156419 726 ---NTYEKLKmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNN 770
Cdd:pfam05833 380 kyfKKYQKLK---------RAVEAVKEQIEETKEEIEYLESVETQLEN 418
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
598-778 |
4.09e-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: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 598 QSQDLQAQMNASRETQKSLRQ------------EHLA---EKEKLAEKLEQEEKLKAKIQQLTeekaaleesigQEKSRS 662
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLKQqifalsevvqrrPHFSyedAVGLLGENSDLNEKLRARLEQAE-----------EARREA 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 663 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLE--------AE---RRKAQDLENQLTQQKeiSENNTYEKl 731
Cdd:COG3096 1004 REQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEeraRIRRDELHEELSQNR--SRRSQLEK- 1080
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907156419 732 kmrdTLEKEKRKIQDLENRLTkqKEEIELKEQKENVLNNKLKDALVM 778
Cdd:COG3096 1081 ----QLTRCEAEMDSLQKRLR--KAERDYKQEREQVVQAKAGWCAVL 1121
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
588-764 |
4.74e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 588 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEH------LAEKEKLA------EKLEQEEKLKAKIQQLTEEKAALEESI 655
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELdllrfqLEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 656 GQEKSRSEEALEKAQARVRELENH---LASQKEALENS------VAQEKRKMREMLEAERRKAQDLENQLTQQKEISE-- 724
Cdd:COG0497 236 SGGEGGALDLLGQALRALERLAEYdpsLAELAERLESAlieleeAASELRRYLDSLEFDPERLEEVEERLALLRRLARky 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907156419 725 NNTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 764
Cdd:COG0497 316 GVTVEELlAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
621-834 |
4.97e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 621 LAEKEKLAEKLEQEEKLKAKIQQLTEEkaaLEESIGQEKSRSEEALEKaqarVRELENHLASQKEALENSvaqeKRKMRE 700
Cdd:cd22656 99 LIDDLADATDDEELEEAKKTIKALLDD---LLKEAKKYQDKAAKVVDK----LTDFENQTEKDQTALETL----EKALKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 701 MLEAE-----RRKAQDLENQLTQQKEIsenntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENV--LNNKL 772
Cdd:cd22656 168 LLTDEggaiaRKEIKDLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALRLIAdLTAADTDLdnLLALI 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156419 773 KDALVMVedaQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 834
Cdd:cd22656 242 GPAIPAL---EKLQGAWQAIATDLD-SLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEK 299
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
434-688 |
5.14e-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: 40.52 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 434 AQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniISKTLREKNKLENFRNQVIKATfgktkpfrDKPITDQ 513
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA-------LLKQLAALERRIAALARRIRAL--------EQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 514 QACMRDSCSSID-LKKEVELLQHLpLSPLVSGLQKtvvnilrvsLSWLEETEQLLGDLDIelSDSDKGFSLcLIYLLEHY 592
Cdd:COG4942 82 EAELAELEKEIAeLRAELEAQKEE-LAELLRALYR---------LGRQPPLALLLSPEDF--LDAVRRLQY-LKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKiqqlteeKAALEESIGQEKSRSEEALEKAQAR 672
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE-------RQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|....*.
gi 1907156419 673 VRELENHLASQKEALE 688
Cdd:COG4942 222 AEELEALIARLEAEAA 237
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
558-699 |
5.24e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 558 SWLEETEQLLGDLDIELSDSDKGFSlcliyLLEHYKKIMsqsqdlqAQMNASRETQKslrqehlaekeklaekleqeEKL 637
Cdd:pfam05911 716 SQLQESEQLIAELRSELASLKESNS-----LAETQLKCM-------AESYEDLETRL--------------------TEL 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 638 KAKIQQLTEEKAALEESIGQEKSRSEEALekaqARVRELENHL--ASQKEALENSVAQEKRKMR 699
Cdd:pfam05911 764 EAELNELRQKFEALEVELEEEKNCHEELE----AKCLELQEQLerNEKKESSNCDADQEDKKLQ 823
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
326-474 |
5.77e-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: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 326 RQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDHAITSGMV----------TSLQKDMSA 389
Cdd:pfam05667 333 REEELEELQEQLEDLESSIQELekeikkLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaeeniAKLQALVDA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 390 RNEQVQQLQEEVNRLRIENREKeyqLEALSSRCSvmkeelrkeeAQKDRREAQEKELKLCRSQMQDMEKEVRKlREELKK 469
Cdd:pfam05667 413 SAQRLVELAGQWEKHRVPLIEE---YRALKEAKS----------NKEDESQRKLEEIKELREKIKEVAEEAKQ-KEELYK 478
|
....*
gi 1907156419 470 NYMGQ 474
Cdd:pfam05667 479 QLVAE 483
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
253-469 |
5.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 253 QDKDEIILLLGR-EVNRLSDFEMESKYKDALimnlQAEVADLSQRLSETAA---VAAARQSNrcdpklqgVDEGDDLRQK 328
Cdd:PLN02939 138 QNAEKNILLLNQaRLQALEDLEKILTEKEAL----QGKINILEMRLSETDArikLAAQEKIH--------VEILEEQLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 329 EIESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DHAITSGMVTSLQKDMSARNEQVQQLQEEVnrlr 405
Cdd:PLN02939 206 LRNELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELESKF---- 280
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 406 IENREKEYQLEALSSRCsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKK 469
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKE 342
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
602-720 |
5.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 602 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR-SEEALEKAQARVRELENHL 680
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPaDSGAEERARARRDELHARL 1069
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907156419 681 A---SQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQK 720
Cdd:PRK04863 1070 SanrSRRNQLEKQLTFCEAEMDNLtkkLRKLERDYHEMREQVVNAK 1115
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
69-124 |
5.93e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 38.05 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156419 69 ESADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 124
Cdd:cd22695 61 DSRVLSRNHACLSCDPTTGKVYIRDLKSSNGTFVNGQKIRQNDVELKVGDEVDLGT 116
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
602-719 |
7.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 602 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESI--------GQEKSRSEEALEKAQARV 673
Cdd:PRK12705 61 LLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALsareleleELEKQLDNELYRVAGLTP 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907156419 674 RELENHLASQKEA-LENSVAQEKRKMREMLEAE-RRKAQDLENQLTQQ 719
Cdd:PRK12705 141 EQARKLLLKLLDAeLEEEKAQRVKKIEEEADLEaERKAQNILAQAMQR 188
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
55-197 |
8.60e-03 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 39.66 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 55 HAPPPG-LCTCRSDAESADI-----------------DNHHALIEFNEaeGTFVLQDFnSRNGTFVNECH---IQNVAVK 113
Cdd:TIGR03354 9 HQLTPGiAAQKTFGTNGGTIgrsedcdwvlpdperhvSGRHARIRYRD--GAYLLTDL-STNGVFLNGSGsplGRGNPVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 114 LIPGDILRFGSagmtYELVIENPSP------------VSCPWVRGP-APWPSPQPHL---------SSSPPDMPFhhgiQ 171
Cdd:TIGR03354 86 LEQGDRLRLGD----YEIRVSLGDPlvsrqasesradTSLPTAGGPpTPDPAPLAQLdplkaldqePLSAADLDD----L 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907156419 172 PATVQRSWSQGCP--------RPTMVP-----PAPHQRP 197
Cdd:TIGR03354 158 SAPLFPPLDARLPafaapidaEPTMVPpfvplPAPEPAP 196
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
593-823 |
8.63e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.02 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 593 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 672
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 673 VRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLT 752
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 753 KQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKL 823
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-1011 |
8.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 721 EISENNTYEKLKM----RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEdaqqmkttesqraetl 796
Cdd:PRK03918 161 ENAYKNLGEVIKEikrrIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE---------------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 797 alKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD---ERESQKHGFEEEISEYKEQ------IKQHSQTIVSLEERL 867
Cdd:PRK03918 225 --KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 868 CQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagppLDSGDKEIacdhliDDLLMAQKEILSQQEII---MKLRTDLGE 944
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKE-------LEEKEERL------EELKKKLKELEKRLEELeerHELYEEAKA 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156419 945 AHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRCGKG 1011
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
653-774 |
9.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 653 ESIGQEKSRSEEALEKAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ--KEISE 724
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEaeallkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEakKEADE 588
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907156419 725 --NNTYEKLKMRDTLEKEKrKIQDLENRLTKQKEEIE--LKEQKENVLNNKLKD 774
Cdd:PRK00409 589 iiKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEkkKKKQKEKQEELKVGD 641
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
396-760 |
9.38e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 40.03 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 396 QLQEEVNRLRIENREKEYQLEALSSrcSVMKEELRKEEAQKDRREAQEKELKLcRSQMQDMEKEVRKLREELKKnymgqn 475
Cdd:pfam14817 81 ELQKEIERLRAEISRLDKQLEAREL--ELSREEAERERALDEISDSRHRQLLL-EAYDQQCEEARKILAEDHQR------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 476 iISKTLREKNKLEnfRNQVIKATFGKTKPFRDKPITDQQACMRDSCSSIDLKkeVELLQHLPLSPL----VSGLQKTVVN 551
Cdd:pfam14817 152 -LQGQLQQLRDAA--RKAEKEVVFGDSKGSKSSVIALEPQVLRDVREACELR--AQFLQELLESSLkayeGSGIHMNRDQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 552 ILRVSLSWLEETEQLLGDLDIELsdsdkgfslcLIYLLEHY-KKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEK 630
Cdd:pfam14817 227 RRAVIQHWLSAVETLLTSHPPSH----------LLQALEHLaAREKTAIQEETESLDVRADAEA-LRFRYESNHLLDVSS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 631 lEQEEKLKAKIQQLTEEKAALEESI---GQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMRE----MLE 703
Cdd:pfam14817 296 -DESSDLPSVRQLLERQWAHVQQFLnelAETRSRCQQLQARLQGLKDEAELESLGIGDTSQNDSLLRQVLELElqaaGLA 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156419 704 AER----RKAQDLENQLTQQKEisenntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIEL 760
Cdd:pfam14817 375 ASRdtlrSECQQLNKLARERQE-----------ALRSLQKKWQRILDFRQLVSELQEQIRA 424
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
583-844 |
9.43e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 583 LCLIYLLEHYKKIMSQSQDLQaqmNASRETQKSLRQEHLAEKEKLAEK---LEQEEK-LKAKIQQLTEEKAALEEsigQE 658
Cdd:pfam12128 258 LRLSHLHFGYKSDETLIASRQ---EERQETSAELNQLLRTLDDQWKEKrdeLNGELSaADAAVAKDRSELEALED---QH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 659 KSRSEEALEKAQArvrELENhlasqkealENSVAQEKRKMREMLEAERRKAQDLENQltqqkeisenntYEKLKMRDTLE 738
Cdd:pfam12128 332 GAFLDADIETAAA---DQEQ---------LPSWQSELENLEERLKALTGKHQDVTAK------------YNRRRSKIKEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 739 KeKRKIQDLENRLTKQKEEIEL-KEQKENVLnNKLKDALVMVEDAQQMKTTESQraetlaLKLKETLAELETTKTKMILT 817
Cdd:pfam12128 388 N-NRDIAGIKDKLAKIREARDRqLAVAEDDL-QALESELREQLEAGKLEFNEEE------YRLKSRLGELKLRLNQATAT 459
|
250 260
....*....|....*....|....*..
gi 1907156419 818 DDRLKLQQQSMKALQDERESQKHGFEE 844
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAE 486
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
589-710 |
9.86e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156419 589 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKiQQLTEEKAALEESIGQEKSRS-EEALE 667
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKAR-AKAAKAQEKVNEALSGIDSDDaTSALE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907156419 668 KAQARVRELENHLASQKE-ALENSVAQEKRKMREMLEAERRKAQ 710
Cdd:COG1842 169 RMEEKIEEMEARAEAAAElAAGDSLDDELAELEADSEVEDELAA 212
|
|
| |
