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Conserved domains on  [gi|17508733|ref|NP_491539|]
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Spindle-defective protein 5 [Caenorhabditis elegans]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
699-1021 1.02e-10

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [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
SMC_prok_B super family cl37069
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]


The actual alignment was detected with superfamily member TIGR02168:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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