|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
699-1021 |
1.02e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 699 SDIVEKLQNEVSELKNELEMARTR--DMRSPLNGSSGRLSDVQINTNRMFED-------LEVSEATLQKAKEENSTLKSQ 769
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEeeklkerLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 770 FAELEANLHQVNSKLGEVRCELNEALARVDGEQetrvkaenaLEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEF 849
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 850 LKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADycsTKMTE 929
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE---RKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 930 RKKEIELAKYREDFENAAivgLERISKEISELTKKTLKAKIIPSNISS---IQLVCDELCRRLS-------REREQQHEY 999
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAK---LEALEEELSEIEDPKGEDEEIPEEELSledVQAELQRVEEEIRalepvnmLAIQEYEEV 984
|
330 340
....*....|....*....|..
gi 17508733 1000 AKVMRDVNEKIEKLQLEKDALE 1021
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
694-1017 |
2.56e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 694 KFTSNSDIVEKLQNEVSELKNELEMARTR-----DMRSPLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKS 768
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEvkeleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 769 QFAELEA--NLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKS 846
Cdd:PRK03918 281 KVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 847 DEFLKSELSTALEEEKKSQNLA----DELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADY 922
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 923 CSTKMTERKKEIELAKYREDfenaaivgLERISKEISELTKKTLKAKIIPSNISSIqlvcdelcrrLSRERE--QQHEYA 1000
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAE--------LKRIEKELKEIEEKERKLRKELRELEKV----------LKKESEliKLKELA 502
|
330
....*....|....*..
gi 17508733 1001 KVMRDVNEKIEKLQLEK 1017
Cdd:PRK03918 503 EQLKELEEKLKKYNLEE 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
747-1021 |
1.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 747 EDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEE 826
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 827 NELKKtitdmgmRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHL 906
Cdd:COG1196 333 EELEE-------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 907 ETEMEKLSTSEIAAdycstkmteRKKEIELAKYREDFENAAIVGLERISKEISELTKKTLKAKiipsnissiqlvcdELC 986
Cdd:COG1196 406 EEAEEALLERLERL---------EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--------------ALL 462
|
250 260 270
....*....|....*....|....*....|....*
gi 17508733 987 RRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALE 1021
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-968 |
5.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 72 LKTKITILRGELQMYQRRYSEA---KEASQKRVKEVMDDYVDLKLGQENVQEKMEQYKLMEEDLLAMQSRIETSEDNFAR 148
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 149 QMKEFEAQKHAMEERIKELElsatdannTTVGSFRGTLDDIlkkndpdftltsgyeERKINDLEAKLLSEIDKVAELEDH 228
Cdd:TIGR02168 359 ELEELEAELEELESRLEELE--------EQLETLRSKVAQL---------------ELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 229 IQQLRQELDDQSARLADSENVRAQLEAATGQGILgaagnamvpnstfmigngRESQTRDqlnyiDDLETKLADAKKENDK 308
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEEL------------------EELQEEL-----ERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 309 ARQALVEYMNKCSKLEHEIRTMVknstfdssSMLLGGQTSDELKIQIGKVNGELNVLRAENRELrIRCDQltGGDGNLSI 388
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLE--------RLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE--GYEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 389 SLGQSrlMAGIATNDVDSIGQG------NETGGTSMRILpresqldDLEESKLPLMDTSSAVRNQQQFASMWEDFESVKD 462
Cdd:TIGR02168 542 ALGGR--LQAVVVENLNAAKKAiaflkqNELGRVTFLPL-------DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 463 SLQNNHNDTLEGSFnssMPPPGRDATQsfLSQKSFKNSPIVMQKPKSLHlhlKSHQSEGAGEQIQNNSFSTKTASPHVSQ 542
Cdd:TIGR02168 613 KLRKALSYLLGGVL---VVDDLDNALE--LAKKLRPGYRIVTLDGDLVR---PGGVITGGSAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 543 shipilhdmqqildssamflegqhdvavNVEQMQEKMSQIREALARLFERLkssaalfEEILErmgssdpNADKIKKMKL 622
Cdd:TIGR02168 685 ----------------------------KIEELEEKIAELEKALAELRKEL-------EELEE-------ELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 623 AFETSINDKLNVSAILEAAEKDLHNMSLNFSILEKSIVSQAAEASRRFTIAPDAEDVAsssllnasysplfkftsnSDIV 702
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA------------------EAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 703 EKLQNEVSELKNELEMARTRdmrspLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNS 782
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 783 KLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSdeflKSELSTALEE-E 861
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK----LAQLELRLEGlE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 862 KKSQNLADELSEElngWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAA--DYCSTKmtERKKeiELAKY 939
Cdd:TIGR02168 936 VRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieEYEELK--ERYD--FLTAQ 1008
|
890 900
....*....|....*....|....*....
gi 17508733 940 REDFeNAAIVGLERISKEISELTKKTLKA 968
Cdd:TIGR02168 1009 KEDL-TEAKETLEEAIEEIDREARERFKD 1036
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
550-1034 |
1.02e-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: 50.12 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 550 DMQQILDSSAMFLEGQHDVAVNVEQMQEKMsqiREALARLFERLKSSAALFEEILErmgSSDPNADKIKKMKLAFETSIN 629
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDL---RNQLQNTVHELEAAKCLKEDMLE---DSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 630 DklnVSAIL----EAAEKDLHNMSLNFSILEKSIVSQAAEASRRFtiapDAEdvasSSLLNASYSPLfkftsnSDIVEKL 705
Cdd:pfam15921 188 E---IRSILvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILREL----DTE----ISYLKGRIFPV------EDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 706 QNEvSELKNELEMARTRDMRSPL--------NGSSGRLSDVQINTNRMFEDLEVSEatlQKAKEENSTLKSQFAELEANL 777
Cdd:pfam15921 251 KSE-SQNKIELLLQQHQDRIEQLiseheveiTGLTEKASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 778 HQVNSKLGEVRCELNEalaRVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTA 857
Cdd:pfam15921 327 SQLRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 858 LEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSE-KSEMLERIVHLETEMEKLS-TSEIAADYCSTKMTERKKEIE 935
Cdd:pfam15921 404 WDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEkVSSLTAQLESTKEMLRKVVEE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 936 LAKYREDFENAaivglER-ISKEISELTKKTLKAKIIPSNISSIQLVCDELCRRLSR-EREQQHeyakvMRDVNEKIEKL 1013
Cdd:pfam15921 484 LTAKKMTLESS-----ERtVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlKNEGDH-----LRNVQTECEAL 553
|
490 500
....*....|....*....|.
gi 17508733 1014 QLEKDALEHELKMMSSNNENV 1034
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENM 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-256 |
1.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 71 ALKTKITILRGELQMYQRRYSEAKEASQKRVKEVMDDYVDLKLGQENVQEKMEQYKLMEEDLLAMQSRIETSEDNFARQM 150
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 151 KEFEAQKHAMEERIKELELSatdannttvgSFRGTLDDILKKNDPDFTLTSGYEERKINDLEAKLLSEI-DKVAELEDHI 229
Cdd:COG4942 97 AELEAQKEELAELLRALYRL----------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELrADLAELAALR 166
|
170 180
....*....|....*....|....*..
gi 17508733 230 QQLRQELDDQSARLADSENVRAQLEAA 256
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-375 |
7.27e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 81 GELQMYQRRYSEAKEAsqkrVKEVMDDyvdLKLGQENVQEKMEQYKlmEEDLLAMQSRIETSEDNFARQMKEFEAQKHAM 160
Cdd:PRK02224 162 GKLEEYRERASDARLG----VERVLSD---QRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 161 EERIKELELsatdanntTVGSFRGTLDDI--LKKNDPDFTLTSGYEERKINDLEAKLLSEIDKVAELEDH---------- 228
Cdd:PRK02224 233 RETRDEADE--------VLEEHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 229 -------IQQLRQELDDQSARLADS-ENVRAQLEAATGQgILGAAGNAmvpnstfmigNGRESQTRDQLNYIDDLETKLA 300
Cdd:PRK02224 305 ddadaeaVEARREELEDRDEELRDRlEECRVAAQAHNEE-AESLREDA----------DDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508733 301 DAKKENDKARQALVEymnkcskLEHEIRTMVKnsTFDSSSMLLGGQT--SDELKIQIGKVNGELNVLRAENRELRIR 375
Cdd:PRK02224 374 EAREAVEDRREEIEE-------LEEEIEELRE--RFGDAPVDLGNAEdfLEELREERDELREREAELEATLRTARER 441
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
699-1021 |
1.02e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 699 SDIVEKLQNEVSELKNELEMARTR--DMRSPLNGSSGRLSDVQINTNRMFED-------LEVSEATLQKAKEENSTLKSQ 769
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEeeklkerLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 770 FAELEANLHQVNSKLGEVRCELNEALARVDGEQetrvkaenaLEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEF 849
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 850 LKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADycsTKMTE 929
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE---RKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 930 RKKEIELAKYREDFENAAivgLERISKEISELTKKTLKAKIIPSNISS---IQLVCDELCRRLS-------REREQQHEY 999
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAK---LEALEEELSEIEDPKGEDEEIPEEELSledVQAELQRVEEEIRalepvnmLAIQEYEEV 984
|
330 340
....*....|....*....|..
gi 17508733 1000 AKVMRDVNEKIEKLQLEKDALE 1021
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
694-1017 |
2.56e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 694 KFTSNSDIVEKLQNEVSELKNELEMARTR-----DMRSPLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKS 768
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEvkeleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 769 QFAELEA--NLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKS 846
Cdd:PRK03918 281 KVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 847 DEFLKSELSTALEEEKKSQNLA----DELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADY 922
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 923 CSTKMTERKKEIELAKYREDfenaaivgLERISKEISELTKKTLKAKIIPSNISSIqlvcdelcrrLSRERE--QQHEYA 1000
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAE--------LKRIEKELKEIEEKERKLRKELRELEKV----------LKKESEliKLKELA 502
|
330
....*....|....*..
gi 17508733 1001 KVMRDVNEKIEKLQLEK 1017
Cdd:PRK03918 503 EQLKELEEKLKKYNLEE 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
747-1021 |
1.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 747 EDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEE 826
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 827 NELKKtitdmgmRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHL 906
Cdd:COG1196 333 EELEE-------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 907 ETEMEKLSTSEIAAdycstkmteRKKEIELAKYREDFENAAIVGLERISKEISELTKKTLKAKiipsnissiqlvcdELC 986
Cdd:COG1196 406 EEAEEALLERLERL---------EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--------------ALL 462
|
250 260 270
....*....|....*....|....*....|....*
gi 17508733 987 RRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALE 1021
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
734-1025 |
2.07e-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: 58.91 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 734 RLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCEL-------NEALARVDGEQETRV 806
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 807 KAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELStALEEEKKSQNL-ADELSEELNGWRMRTKEA 885
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-ELRAELTLLNEeAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 886 ENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADYCSTKMTERKKEIE--LAKYREDFENAAiVGLERISKEISELTK 963
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEeaLALLRSELEELS-EELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508733 964 KTLKAKiipSNISSIQLVCDELCRRLSREREQ-QHEYAKVMRDVNEKIEKLQLEKDALEHELK 1025
Cdd:TIGR02168 916 ELEELR---EKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
769-1024 |
3.28e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 769 QFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDE 848
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 849 FLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLST--SEIAADYCSTK 926
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 927 MTERKKEIELAKYREDFENAAiVGLERISKEISELTKKTLKAKIipsnissiqlvcDELCRRLSREREQQHEYAKVMRDV 1006
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLE-DRRERLQQEIEELLKKLEEAEL------------KELQAELEELEEELEELQEELERL 459
|
250
....*....|....*...
gi 17508733 1007 NEKIEKLQLEKDALEHEL 1024
Cdd:TIGR02168 460 EEALEELREELEEAEQAL 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
701-1023 |
1.19e-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: 56.23 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 701 IVEKLQNEVSELKNELEMA-RTRDMRSPLNGSSGRLSDVQINTNRmfEDLEVSEATLQKAKEENSTLKSQFAELEANLHQ 779
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAeRYQALLKEKREYEGYELLKEKEALE--RQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 780 VNSKLGEvrceLNEALARVDGEQETRVKAEnaLEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSE---LST 856
Cdd:TIGR02169 270 IEQLLEE----LNKKIKDLGEEEQLRVKEK--IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEieeLER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 857 ALEEEKKS----QNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEiaadycsTKMTERKK 932
Cdd:TIGR02169 344 EIEEERKRrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-------DRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 933 EIELAkyREDFENAAIVGLERISKEISELTKKTLKAKIIPSNISSIQLVCDELCRRLSREREQQHEYAKVMRDVNEKIEK 1012
Cdd:TIGR02169 417 RLSEE--LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330
....*....|.
gi 17508733 1013 LQLEKDALEHE 1023
Cdd:TIGR02169 495 AEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-1021 |
1.26e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 704 KLQNEVSELKNELEMARTRDMRsplngssGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSK 783
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELR-------EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 784 LGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKK 863
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 864 SQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSeiaadycstkMTERKKEIELAKYREdf 943
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE----------IEELLKKLEEAELKE-- 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17508733 944 enaAIVGLERISKEISELTKKTlkakiipsnissiqlvcDELCRRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALE 1021
Cdd:TIGR02168 438 ---LQAELEELEEELEELQEEL-----------------ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
572-920 |
1.46e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 572 VEQMQEKMSQIREALARLFERLKSSAALFEEILERMGS-SDPNADKIKKMKLAFETSINDKLNVSAILEAAEKDLHNMSL 650
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 651 NFSILEKSIVSQAAEASRRftiapDAEDVASSSLLNASYSPLFKFTSNSDIveKLQNEVSELKNELEMARtrdmrsplng 730
Cdd:TIGR02169 245 QLASLEEELEKLTEEISEL-----EKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEAEIASLE---------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 731 ssGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAEN 810
Cdd:TIGR02169 308 --RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 811 ALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVE 890
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350
....*....|....*....|....*....|
gi 17508733 891 HASSEKSEMLERIVHLETEMEKLStSEIAA 920
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQ-RELAE 494
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
700-913 |
4.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 700 DIVEKLQNEVSELKNELEMARTRDMRSPLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAK----------EENSTLKSQ 769
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 770 FAELEAN--------------LHQVNSKLGEVRCELNEALARV---DGEQET-----------RVKAENALEEARQLISS 821
Cdd:PRK02224 260 IEDLRETiaeterereelaeeVRDLRERLEELEEERDDLLAEAgldDADAEAvearreeledrDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 822 LKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMR-------TKEAENKVEHASS 894
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELRE 419
|
250
....*....|....*....
gi 17508733 895 EKSEMLERIVHLETEMEKL 913
Cdd:PRK02224 420 ERDELREREAELEATLRTA 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-968 |
5.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 72 LKTKITILRGELQMYQRRYSEA---KEASQKRVKEVMDDYVDLKLGQENVQEKMEQYKLMEEDLLAMQSRIETSEDNFAR 148
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 149 QMKEFEAQKHAMEERIKELElsatdannTTVGSFRGTLDDIlkkndpdftltsgyeERKINDLEAKLLSEIDKVAELEDH 228
Cdd:TIGR02168 359 ELEELEAELEELESRLEELE--------EQLETLRSKVAQL---------------ELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 229 IQQLRQELDDQSARLADSENVRAQLEAATGQGILgaagnamvpnstfmigngRESQTRDqlnyiDDLETKLADAKKENDK 308
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEEL------------------EELQEEL-----ERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 309 ARQALVEYMNKCSKLEHEIRTMVknstfdssSMLLGGQTSDELKIQIGKVNGELNVLRAENRELrIRCDQltGGDGNLSI 388
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLE--------RLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE--GYEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 389 SLGQSrlMAGIATNDVDSIGQG------NETGGTSMRILpresqldDLEESKLPLMDTSSAVRNQQQFASMWEDFESVKD 462
Cdd:TIGR02168 542 ALGGR--LQAVVVENLNAAKKAiaflkqNELGRVTFLPL-------DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 463 SLQNNHNDTLEGSFnssMPPPGRDATQsfLSQKSFKNSPIVMQKPKSLHlhlKSHQSEGAGEQIQNNSFSTKTASPHVSQ 542
Cdd:TIGR02168 613 KLRKALSYLLGGVL---VVDDLDNALE--LAKKLRPGYRIVTLDGDLVR---PGGVITGGSAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 543 shipilhdmqqildssamflegqhdvavNVEQMQEKMSQIREALARLFERLkssaalfEEILErmgssdpNADKIKKMKL 622
Cdd:TIGR02168 685 ----------------------------KIEELEEKIAELEKALAELRKEL-------EELEE-------ELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 623 AFETSINDKLNVSAILEAAEKDLHNMSLNFSILEKSIVSQAAEASRRFTIAPDAEDVAsssllnasysplfkftsnSDIV 702
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA------------------EAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 703 EKLQNEVSELKNELEMARTRdmrspLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNS 782
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 783 KLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSdeflKSELSTALEE-E 861
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK----LAQLELRLEGlE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 862 KKSQNLADELSEElngWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAA--DYCSTKmtERKKeiELAKY 939
Cdd:TIGR02168 936 VRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieEYEELK--ERYD--FLTAQ 1008
|
890 900
....*....|....*....|....*....
gi 17508733 940 REDFeNAAIVGLERISKEISELTKKTLKA 968
Cdd:TIGR02168 1009 KEDL-TEAKETLEEAIEEIDREARERFKD 1036
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
694-962 |
6.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 694 KFTSNSDIVEKLQNEVSELKN----ELEMART--RDMRSPLNGSSGRLSDVQINTNRMfEDLEVSEATLQKAKEEnstLK 767
Cdd:PRK03918 494 ELIKLKELAEQLKELEEKLKKynleELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDE---LE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 768 SQFAELEANLHQVNSKLGEvrcELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDmgmrLNEAKKSD 847
Cdd:PRK03918 570 EELAELLKELEELGFESVE---ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE----LAETEKRL 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 848 EFLKSELSTAL-----EEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSEIAADy 922
Cdd:PRK03918 643 EELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE- 721
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17508733 923 cstKMTERKKEIelAKYREDFENAAIVGLERISKEI-SELT 962
Cdd:PRK03918 722 ---RVEELREKV--KKYKALLKERALSKVGEIASEIfEELT 757
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
550-1034 |
1.02e-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: 50.12 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 550 DMQQILDSSAMFLEGQHDVAVNVEQMQEKMsqiREALARLFERLKSSAALFEEILErmgSSDPNADKIKKMKLAFETSIN 629
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDL---RNQLQNTVHELEAAKCLKEDMLE---DSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 630 DklnVSAIL----EAAEKDLHNMSLNFSILEKSIVSQAAEASRRFtiapDAEdvasSSLLNASYSPLfkftsnSDIVEKL 705
Cdd:pfam15921 188 E---IRSILvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILREL----DTE----ISYLKGRIFPV------EDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 706 QNEvSELKNELEMARTRDMRSPL--------NGSSGRLSDVQINTNRMFEDLEVSEatlQKAKEENSTLKSQFAELEANL 777
Cdd:pfam15921 251 KSE-SQNKIELLLQQHQDRIEQLiseheveiTGLTEKASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 778 HQVNSKLGEVRCELNEalaRVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTA 857
Cdd:pfam15921 327 SQLRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 858 LEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSE-KSEMLERIVHLETEMEKLS-TSEIAADYCSTKMTERKKEIE 935
Cdd:pfam15921 404 WDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEkVSSLTAQLESTKEMLRKVVEE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 936 LAKYREDFENAaivglER-ISKEISELTKKTLKAKIIPSNISSIQLVCDELCRRLSR-EREQQHeyakvMRDVNEKIEKL 1013
Cdd:pfam15921 484 LTAKKMTLESS-----ERtVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlKNEGDH-----LRNVQTECEAL 553
|
490 500
....*....|....*....|.
gi 17508733 1014 QLEKDALEHELKMMSSNNENV 1034
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENM 574
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
734-970 |
1.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 734 RLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKaenaLE 813
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 814 EARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKKSqnladELSEELNGWRMRTKEAENKVEhas 893
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA-----EEYIKLSEFYEEYLDELREIE--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 894 SEKSEMLERIVHLETEMEKLSTSEIAADYCSTKMTERKKEIE-LAKYREDFENA--AIVGLERISKEISELTKKTLKAKI 970
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeLEERHELYEEAkaKKEELERLKKRLTGLTPEKLEKEL 393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
771-953 |
1.13e-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: 48.00 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 771 AELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEENELKKTITDMGMRLNEAKKSDEFl 850
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 851 kSELSTALEEEKKSQNLADELSEELNgwrMRTKEAENKVEHASSEKSEMLERIVHLETEMEK-LSTSEIAADYCSTKMTE 929
Cdd:COG1579 92 -EALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELEELEAEREE 167
|
170 180 190
....*....|....*....|....*....|
gi 17508733 930 RKKEIE---LAKY---REDFENAAIVGLER 953
Cdd:COG1579 168 LAAKIPpelLALYeriRKRKNGLAVVPVEG 197
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
703-1026 |
3.26e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 703 EKLQNEVSELKNELEMART--RDMRSPLNGSSGRLSDVQINTNRMFEDLEVSEATLQKAKEENSTLKSQFAELEANLHQV 780
Cdd:PRK02224 359 EELREEAAELESELEEAREavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 781 NSKLGEVRcELNEA------------LARVDGEQETRVKAEN---ALEEARQLISSL--KHEENE-LKKTITDMGMRLNE 842
Cdd:PRK02224 439 RERVEEAE-ALLEAgkcpecgqpvegSPHVETIEEDRERVEEleaELEDLEEEVEEVeeRLERAEdLVEAEDRIERLEER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 843 AKKSDEFLKSELSTALEEEKKSQNL---ADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLST-SEI 918
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 919 AADycstkMTERKKEIElaKYREDFENAAIVGLERISK--EISElTKKTLKAKIIPSNISSIQlvcdelcrrlsREREQQ 996
Cdd:PRK02224 598 LAA-----IADAEDEIE--RLREKREALAELNDERRERlaEKRE-RKRELEAEFDEARIEEAR-----------EDKERA 658
|
330 340 350
....*....|....*....|....*....|
gi 17508733 997 HEYakvMRDVNEKIEKLQLEKDALEHELKM 1026
Cdd:PRK02224 659 EEY---LEQVEEKLDELREERDDLQAEIGA 685
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
839-1034 |
1.25e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 839 RLNEAKKSdefLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLStSEI 918
Cdd:TIGR02169 678 RLRERLEG---LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE-QEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 919 AADycSTKMTERKKEIE-----LAKYREDFEN---------------------AAIVGLERISKEI-SELTKKTLKAKII 971
Cdd:TIGR02169 754 ENV--KSELKELEARIEeleedLHKLEEALNDlearlshsripeiqaelskleEEVSRIEARLREIeQKLNRLTLEKEYL 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508733 972 PSNISSIQLVCDELCRRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALEHELKMMSSNNENV 1034
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
756-1040 |
1.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 756 LQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENA--LEEARQLISSLKHEENELKKTI 833
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 834 TDMGMRLNEAKKSDEFLKSELSTAL--EEEKKSQNLADELSEELNgwrmRTKEAENKVEHASSEKSEMLERIVHLETEME 911
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 912 KlstseiaadycstkmtERKKEIELAKYREDFENAAivglERISKEISELTKKTLKAKIIPSNISSIQLVCDELCRRLSR 991
Cdd:PTZ00121 1713 E----------------EKKKAEELKKAEEENKIKA----EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17508733 992 EREQQHeyAKVMRDVNEKIEKLQLE-----KDALEHELKMMSSNNENVPPVGTS 1040
Cdd:PTZ00121 1773 IRKEKE--AVIEEELDEEDEKRRMEvdkkiKDIFDNFANIIEGGKEGNLVINDS 1824
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
71-256 |
1.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 71 ALKTKITILRGELQMYQRRYSEAKEASQKRVKEVMDDYVDLKLGQENVQEKMEQYKLMEEDLLAMQSRIETSEDNFARQM 150
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 151 KEFEAQKHAMEERIKELELSatdannttvgSFRGTLDDILKKNDPDFTLTSGYEERKINDLEAKLLSEI-DKVAELEDHI 229
Cdd:COG4942 97 AELEAQKEELAELLRALYRL----------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELrADLAELAALR 166
|
170 180
....*....|....*....|....*..
gi 17508733 230 QQLRQELDDQSARLADSENVRAQLEAA 256
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
579-921 |
3.01e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 579 MSQIREALARLFERLKSSAALFEEILERMGSSDPNADKIKKMKLAFETSINDKLNVSAILEAAEKDLHNMSLNFSILEKS 658
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 659 IVSQAAEASRrftiapdaedvasssllnasysplfkftsnsdivekLQNEVSELKNELEMARTRDMRspLNGSSGRLSDV 738
Cdd:pfam07888 201 LAQRDTQVLQ------------------------------------LQDTITTLTQKLTTAHRKEAE--NEALLEELRSL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 739 QintnrmfEDLEVSEATLQKAKEENSTLKSQFAELEANLHQV-------NSKLGEVRCELNEALARVDGEQETrvkAENA 811
Cdd:pfam07888 243 Q-------ERLNASERKVEGLGEELSSMAAQRDRTQAELHQArlqaaqlTLQLADASLALREGRARWAQERET---LQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 812 LEEARQLISSLKHEENELKKtitdmgmRLNEAKKSDEFLKSELStalEEEKKSQNLADELSEELNGWRMRTKEAENKVEH 891
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEE-------RLQEERMEREKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
330 340 350
....*....|....*....|....*....|
gi 17508733 892 ASSEKSEMLERIVHLETEMEKLSTSEIAAD 921
Cdd:pfam07888 383 LQAEKQELLEYIRQLEQRLETVADAKWSEA 412
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-375 |
7.27e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 81 GELQMYQRRYSEAKEAsqkrVKEVMDDyvdLKLGQENVQEKMEQYKlmEEDLLAMQSRIETSEDNFARQMKEFEAQKHAM 160
Cdd:PRK02224 162 GKLEEYRERASDARLG----VERVLSD---QRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 161 EERIKELELsatdanntTVGSFRGTLDDI--LKKNDPDFTLTSGYEERKINDLEAKLLSEIDKVAELEDH---------- 228
Cdd:PRK02224 233 RETRDEADE--------VLEEHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 229 -------IQQLRQELDDQSARLADS-ENVRAQLEAATGQgILGAAGNAmvpnstfmigNGRESQTRDQLNYIDDLETKLA 300
Cdd:PRK02224 305 ddadaeaVEARREELEDRDEELRDRlEECRVAAQAHNEE-AESLREDA----------DDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508733 301 DAKKENDKARQALVEymnkcskLEHEIRTMVKnsTFDSSSMLLGGQT--SDELKIQIGKVNGELNVLRAENRELRIR 375
Cdd:PRK02224 374 EAREAVEDRREEIEE-------LEEEIEELRE--RFGDAPVDLGNAEdfLEELREERDELREREAELEATLRTARER 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
771-1039 |
7.73e-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: 43.90 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 771 AELEANLHQVNSKLGEVRCELNEALARVDgEQETRVK--------AENALEEARQLISSLKHEENELKKTITDMGMRLNE 842
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELR-RIENRLDelsqelsdASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 843 AKKSDEFLKSELSTALEEEKKSQNLADELSEELNGW-----RMRTKEAENKVEHASSEKSEMLERIVHLETEMEKLSTSE 917
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 918 iaaDYCSTKMTERKKEIELAKYREDFENAAIVGLE-RISKEISELTKKTLKAKIIPSNISSIQLVCDELCRRLS--RERE 994
Cdd:TIGR02169 829 ---EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRelERKI 905
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17508733 995 QQHEYA-----KVMRDVNEKIEKLQLEKDALEHELKMMSSNNENVPPVGT 1039
Cdd:TIGR02169 906 EELEAQiekkrKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
753-1025 |
8.20e-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: 43.90 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 753 EATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEAL-------ARVDGEQETRVKAENALEEARQLI----SS 821
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYEGYELLKEKEALERQKEAIerqlAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 822 LKHEENELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKKS-QNLADELSEELNGWRMRTKEAENKVEHASSEKSEML 900
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 901 ERIVHLETEMEKLSTsEIAadycsTKMTERKKEIELAKYREDFENAAIVGLERISKEISELTKKTLKAKI----IPSNIS 976
Cdd:TIGR02169 329 AEIDKLLAEIEELER-EIE-----EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREklekLKREIN 402
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17508733 977 SIQLVCDELCRRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALEHELK 1025
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
783-1021 |
1.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 783 KLGEVRCELNEALARVDGEQETRVKAENALEEARQLIS------SLKHEENELKKTITDmgmRLNEAKKSDEFLKSELst 856
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKL-- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 857 aLEEEKKSQNLADELsEELNGWRMRTKEAENKVEHASSEKSEMLERIVHL------ETEMEKLSTSEIAADYCSTKMTER 930
Cdd:PRK03918 535 -IKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveELEERLKELEPFYNEYLELKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 931 KKEI---ELAKYREDFEnAAIVGLERISKEISELTKK--TLKAKIIPSNISSIQLVCDELCRRLSREREQQHEYAKVMRD 1005
Cdd:PRK03918 613 ELEReekELKKLEEELD-KAFEELAETEKRLEELRKEleELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
250
....*....|....*.
gi 17508733 1006 VNEKIEKLQLEKDALE 1021
Cdd:PRK03918 692 IKKTLEKLKEELEERE 707
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
765-1025 |
1.22e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 765 TLKSQFAELEANLHqvnsKLGEVrcELNEALARVDGEQETRVKAEnaLEEARQLISSLKHEENELKkTITDMGMRLNEaK 844
Cdd:PRK05771 13 TLKSYKDEVLEALH----ELGVV--HIEDLKEELSNERLRKLRSL--LTKLSEALDKLRSYLPKLN-PLREEKKKVSV-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 845 KSDEFLKSELSTALEEEKKsqnlADELSEELNgwrmrtkEAENKVEHASSEKSEmLERIVHLETEMEKLSTSEI------ 918
Cdd:PRK05771 83 SLEELIKDVEEELEKIEKE----IKELEEEIS-------ELENEIKELEQEIER-LEPWGNFDLDLSLLLGFKYvsvfvg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 919 ---AADYCSTKMTERKKEIELAKYREDFENAAIVGLERISKEISELTKKT-LKAKIIPSNISSIQLVcdelcrrlsrere 994
Cdd:PRK05771 151 tvpEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLgFERLELEEEGTPSELI------------- 217
|
250 260 270
....*....|....*....|....*....|.
gi 17508733 995 qqheyakvmRDVNEKIEKLQLEKDALEHELK 1025
Cdd:PRK05771 218 ---------REIKEELEEIEKERESLLEELK 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-319 |
1.79e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 147 ARQMKEFEAQKHAMEERIKELELSATDANN--TTVGSFRGTLDDILKKNDPDftLTSGYEERKINDLEAK---LLSEIDK 221
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAelDALQERREALQRLAEYSWDE--IDVASAEREIAELEAElerLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 222 VAELEDHIQQLRQELDDQSARLADSENVRAQLEAATGQ---------GILGAAGNAMVPNSTFMIGN--GRESQTRDQLN 290
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldelqDRLEAAEDLARLELRALLEErfAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 17508733 291 YIDDLETKLADAKKENDKARQALVEYMNK 319
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
757-1034 |
1.97e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 757 QKAKEENSTLKSQFAELEANLHQVN--SKLGEVRCELNEALARVDGEQETRVKAENalEEARQLISSLKHEENELKKTIT 834
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEklNQQKDEQIKKLQQEKELLEKEIERLKETI--IKNNSEIKDLTNQDSVKELIIK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 835 DMGMRLNEAKKS-DEFLKSELSTALEEEKKSQNLADELSeELNGWRMRTKEAENKVEHASSEKSEMLERIVHLETEMEKL 913
Cdd:TIGR04523 458 NLDNTRESLETQlKVLSRSINKIKQNLEQKQKELKSKEK-ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 914 stseiaadycSTKMTERKKEIELAKYREDFENAAIVGLErISKEISEL--TKKTLKAKiipsnISSIQLVCDELCRRLSR 991
Cdd:TIGR04523 537 ----------ESKISDLEDELNKDDFELKKENLEKEIDE-KNKEIEELkqTQKSLKKK-----QEEKQELIDQKEKEKKD 600
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17508733 992 EREQQHEYAKVMRDVNEKIEKLQLEKDALEHELKMMSSNNENV 1034
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
747-1027 |
2.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 747 EDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEE 826
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 827 NELKKtitdmgmRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHL 906
Cdd:COG4372 111 EELQE-------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 907 ETEMEKLSTSEIAADYCSTKMTERKKEIELAKYREDFENAAIVGLERISKEISELTKKTLKAKIIP-SNISSIQLVCDEL 985
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEeLLEEVILKEIEEL 263
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17508733 986 CRRLSREREQQHEYAKVMRDVNEKIEKLQLEKDALEHELKMM 1027
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
115-259 |
3.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 115 QENVQEKMEQYKLMEEDLLAMQSRIETSEDNFARQMKEFEAQKHAMEERIKELELSatdannttvGSFRGTLDDILKKND 194
Cdd:COG3883 43 QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS---------GGSVSYLDVLLGSES 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17508733 195 PDFTLTSGYEERKINDLEAKLLSEI-DKVAELEDHIQQLRQELDDQSARLADSENVRAQLEAATGQ 259
Cdd:COG3883 114 FSDFLDRLSALSKIADADADLLEELkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
749-913 |
4.77e-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: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 749 LEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRcelnEALARVDGEQETRVKAEnaLEEARQLISSLKHEENE 828
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELE----AQIRGNGGDRLEQLERE--IERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 829 LKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKksqNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHLET 908
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
....*
gi 17508733 909 EMEKL 913
Cdd:COG4913 441 RLLAL 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-256 |
5.81e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 67 EENKALKTKITILRGELQMYQRRYSEAKEASQKRVKEVMDdyvdLKLGQENVQEKMEQYKLMEEDLLAMQSRIETSEDNF 146
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 147 ARQMKEFEAQKHAMEERIKELELSATDANNTTVGSFRGTLDdilkkndpdftltsgyEERKINDLEAKLLSEIDKVAELE 226
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----------------AEEELEELAEELLEALRAAAELA 399
|
170 180 190
....*....|....*....|....*....|
gi 17508733 227 DHIQQLRQELDDQSARLADSENVRAQLEAA 256
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
747-945 |
6.04e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.63 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 747 EDLEVSEATLQKAKEENSTLKSQFAELEANLHQVNSKLGEVRCELNEALARVDGEQETRVKAENALEEARQLISSLKHEE 826
Cdd:pfam00261 22 KKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 827 NELKKTITDMGMRLNEAKKSDEFLKSELSTALEEEKKSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEMLERIVHL 906
Cdd:pfam00261 102 KEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17508733 907 EtemEKLSTSEIAADYCSTKMTERKKEI-----ELAKYREDFEN 945
Cdd:pfam00261 182 T---EKLKEAETRAEFAERSVQKLEKEVdrledELEAEKEKYKA 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
747-917 |
6.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 747 EDLEVSEATLQKAKEENStlksQFAELEANLHQVNSKLGEVRCELNEALARVDG--EQETRVKAENALEEARQLISSLKH 824
Cdd:COG4717 71 KELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 825 EENELK---KTITDMGMRLNEAKKSDEFLKSELSTALEEEK-KSQNLADELSEELNGWRMRTKEAENKVEHASSEKSEML 900
Cdd:COG4717 147 RLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*..
gi 17508733 901 ERIVHLETEMEKLSTSE 917
Cdd:COG4717 227 EELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-255 |
7.72e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 67 EENKALKTKITILRGELQMYQRRYSEAK---EASQKRVKEVMDDYVDLKLGQENVQEKMEQyklMEEDLLAMQSRIEtse 143
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSqelSDASRKIGEIEKEIEQLEQEEEKLKERLEE---LEEDLSSLEQEIE--- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 144 dNFARQMKEFEAQKHAMEERIKELELSATD------------------ANNTTVGSFRGTLDDILKKNDpDFTLTSGYEE 205
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDlearlshsripeiqaelsKLEEEVSRIEARLREIEQKLN-RLTLEKEYLE 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17508733 206 RKINDLEAKLLSEIDKVAELEDHIQQLRQELDDQSARLADSENVRAQLEA 255
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
744-969 |
8.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 744 RMFEDLEVSEATlQKAKEENSTLKSQFAELEANLHQVNsKLGEVRCELNEA--LARVDGEQETRVKAENALEEARQLISS 821
Cdd:PTZ00121 1194 RKAEDARKAEAA-RKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508733 822 LKHEE----NELKKTitdmgmrlNEAKKSDEFLKSELSTALEEEKK---SQNLADELSEELNGWRMRTKEAENKVEHA-- 892
Cdd:PTZ00121 1272 IKAEEarkaDELKKA--------EEKKKADEAKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKKADAAKKKAEEAkk 1343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17508733 893 --SSEKSEMLERIVHLETEMEKLSTSEIAADYCSTKMTERKKEIELAKYREDFENAAivglERISKEISELTKKTLKAK 969
Cdd:PTZ00121 1344 aaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA----EEDKKKADELKKAAAAKK 1418
|
|
|