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Conserved domains on  [gi|158517902|ref|NP_113771|]
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structural maintenance of chromosomes protein 3 [Rattus norvegicus]

Protein Classification

chromosome segregation protein SMC( domain architecture ID 12035156)

chromosome segregation protein SMC is an ATPase required for chromosome condensation and partitioning

Gene Ontology:  GO:0003682|GO:0005524|GO:0016887|GO:0051301|GO:0007076|GO:0003677

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-1197 3.51e-126

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


:

Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 417.45  E-value: 3.51e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463    1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463   80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 399
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   400 KSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR-EENA 478
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkETQL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   479 EQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRL 558
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   559 FYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSMEV 638
Cdd:pfam02463  560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADEDD 619

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   639 STQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQM 718
Cdd:pfam02463  620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   719 QQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVD 798
Cdd:pfam02463  700 EIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   799 ALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINK--RVKDT 876
Cdd:pfam02463  779 EREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   877 MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHdtKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK 956
Cdd:pfam02463  850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES--KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   957 --------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 1028
Cdd:pfam02463  928 eillkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1029 IQLTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGE 1108
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKG 1071

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1109 MREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYG 1188
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVG 1151

                         1210
                   ....*....|
gi 158517902  1189 VKF-RNKVSH 1197
Cdd:pfam02463 1152 VTMvENGVST 1161
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-1197 3.51e-126

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 417.45  E-value: 3.51e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463    1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463   80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 399
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   400 KSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR-EENA 478
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkETQL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   479 EQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRL 558
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   559 FYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSMEV 638
Cdd:pfam02463  560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADEDD 619

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   639 STQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQM 718
Cdd:pfam02463  620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   719 QQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVD 798
Cdd:pfam02463  700 EIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   799 ALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINK--RVKDT 876
Cdd:pfam02463  779 EREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   877 MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHdtKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK 956
Cdd:pfam02463  850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES--KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   957 --------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 1028
Cdd:pfam02463  928 eillkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1029 IQLTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGE 1108
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKG 1071

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1109 MREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYG 1188
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVG 1151

                         1210
                   ....*....|
gi 158517902  1189 VKF-RNKVSH 1197
Cdd:pfam02463 1152 VTMvENGVST 1161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-1192 2.01e-102

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: 351.68  E-value: 2.01e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEG-TGPRVISAFVE 79
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGkNGQSGNEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    80 IIFDNSDNRLPiDKEEVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLK 157
Cdd:TIGR02169   80 VTFKNDDGKFP-DELEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRA 237
Cdd:TIGR02169  158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   238 KLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM--------KEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKEREL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARL------AQATQERTDLY--AKQGR 381
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkeFAETRDELKDYreKLEKL 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   382 GSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNK 461
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   462 KDELQSERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvldhfrrkginqhvqnGYHGIVMNNF 540
Cdd:TIGR02169  478 YDRVEKELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQLG 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   541 ECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNP 617
Cdd:TIGR02169  532 SVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDP 610

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   618 RFDKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLN 697
Cdd:TIGR02169  611 KYEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   698 E--NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRE 775
Cdd:TIGR02169  689 ElsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   776 SLKAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRE 852
Cdd:TIGR02169  769 ELEEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRID 844

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   853 TEGGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 932
Cdd:TIGR02169  845 LKEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   933 LKKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 1011
Cdd:TIGR02169  923 KAKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1012 KSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvD 1091
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD-----------------------------D 1052

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1092 QFTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1171
Cdd:TIGR02169 1053 PFAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFI 1131

                         1210      1220
                   ....*....|....*....|.
gi 158517902  1172 TTTFRPELLESADKFYGVKFR 1192
Cdd:TIGR02169 1132 VVSLRSPMIEYADRAIGVTMR 1152
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 3-158 6.32e-95

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 303.80  E-value: 6.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03272     1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902   83 DNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 158
Cdd:cd03272    81 DNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-1189 1.07e-72

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 262.57  E-value: 1.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---SdeFSHLRPEQRLALLHEGTGPR--VIS 75
Cdd:COG1196     1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSRkpLGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   76 AFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQ 154
Cdd:COG1196    78 AEVSLTFDNSDGTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  155 RLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNE 234
Cdd:COG1196   157 RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTdlyAKQGRGSQFTSKEERdkw 394
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLE--- 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR 474
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  475 EENAEQQALAAKREDLEKKQQLLRAATgkailngidSINKVLDHFRRKGINQHV---QNGYHGIVMNNFECEPAFYTCVE 551
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLL---------EAEADYEGFLEGVKAALLlagLRGLAGAVAVLIGVEAAYEAALE 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  552 VTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFDKAFKHVFGK 629
Cdd:COG1196   542 AALAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGD 620

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  630 TLICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenlrrnierinn 709
Cdd:COG1196   621 TLLGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG------------------------------------------ 656

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  710 eidqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAELGTDLLSQL 789
Cdd:COG1196   657 ------SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELE 722

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  790 SLEDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-LTAtTSELEA 868
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnLLA-IEEYEE 792

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  869 INKRVKDTMARSEDLDNSIDKTEAGIKElqksmerwknmekehmdaINHDTKELekmtnrqgmllkkkeecmkkirelgs 948
Cdd:COG1196   793 LEERYDFLSEQREDLEEARETLEEAIEE------------------IDRETRER-------------------------- 828

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  949 lpqeafekyqtlslkqlfrkleqcntelkkyshvnkkaldqfvnFSEqkeklikrqeeldrgyksimelmnvlelrkyea 1028
Cdd:COG1196   829 --------------------------------------------FLE--------------------------------- 831

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1029 iqlTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF-TGVGIRVSFTGKqg 1107
Cdd:COG1196   832 ---TFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPLeTGIEIMAQPPGK-- 877

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1108 EMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQFITTTFRPELLESADK 1185
Cdd:COG1196   878 KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADR 955


                  ....
gi 158517902 1186 FYGV 1189
Cdd:COG1196   956 LYGV 959
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 530-642 3.45e-28

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 110.01  E-value: 3.45e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    530 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 601
Cdd:smart00968    1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 158517902    602 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 642
Cdd:smart00968   80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-503 1.50e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 85.12  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:PRK03918    1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   80 iiFDNSDNRL--PIDKEEVSLRRVIGAKKDqyfLDKKMVTKNDVMNLLESAGFsrSNPYYIvKQGKINQMATApDSQRLK 157
Cdd:PRK03918   79 --KNGRKYRIvrSFNRGESYLKYLDGSEVL---EEGDSSVREWVERLIPYHVF--LNAIYI-RQGEIDAILES-DESREK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAqyqkwdkmrraleytiynQELNE 234
Cdd:PRK03918  150 VVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVL------------------REINE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  235 TRAKLDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQd 314
Cdd:PRK03918  212 ISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGiarlaqatqertdlyakqgrgsqfTSKEERDKW 394
Cdd:PRK03918  287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------------------------EEKEERLEE 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDqainDKKRQIAAIHKDLEDTEAnKEKNLEQYNKLDQDLNevkarVEELDRKYYEVKNKKDELQSERNYLwr 474
Cdd:PRK03918  343 LKKKLKELE----KRLEELEERHELYEEAKA-KKEELERLKKRLTGLT-----PEKLEKELEELEKAKEEIEEEISKI-- 410

                         490       500
                  ....*....|....*....|....*....
gi 158517902  475 eeNAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:PRK03918  411 --TARIGELKKEIKELKKAIEELKKAKGK 437
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 281-504 8.19e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 44.05  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  281 ISAMKEEKEQLSAERqEQIKQRtklELKAKDLQDElAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP-KFNSVKEKEE 359
Cdd:NF012221 1534 VVATSESSQQADAVS-KHAKQD---DAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALETNGQAQR 1608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  360 RGIARLAQA-TQERTDLyaKQG----RGSQFTSKEERDKW--------IKKELKSLDQA-------INDKKRQIAAIHKD 419
Cdd:NF012221 1609 DAILEESRAvTKELTTL--AQGldalDSQATYAGESGDQWrnpfagglLDRVQEQLDDAkkisgkqLADAKQRHVDNQQK 1686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  420 LEDTEANKEKNLEQ--YNKLDQDLNEVKARVeeldrkyyEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLL 497
Cdd:NF012221 1687 VKDAVAKSEAGVAQgeQNQANAEQDIDDAKA--------DAEKRKDDALAKQN---EAQQAESDANAAANDAQSRGEQDA 1755


                  ....*..
gi 158517902  498 RAATGKA 504
Cdd:NF012221 1756 SAAENKA 1762
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 2-1197 3.51e-126

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 417.45  E-value: 3.51e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRdQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSD-EFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:pfam02463    1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGErSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    81 IFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLL 159
Cdd:pfam02463   80 TFDNEDHELPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   160 REVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKL 239
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   240 DELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGN 319
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKEL 399
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   400 KSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR-EENA 478
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLkETQL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   479 EQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRL 558
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   559 FYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVrdtaypetndaipmisklryNPRFDKAFKHVFGKTLICRSMEV 638
Cdd:pfam02463  560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV--------------------LEIDPILNLAQLDKATLEADEDD 619

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   639 STQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQM 718
Cdd:pfam02463  620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   719 QQIETQQRKFKASRDSILSEMKMlKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVD 798
Cdd:pfam02463  700 EIKKKEQREKEELKKLKLEAEEL-LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   799 ALNDEIRQLQQEnrqllneriKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINK--RVKDT 876
Cdd:pfam02463  779 EREKTEKLKVEE---------EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLE 849

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   877 MARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHdtKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEK 956
Cdd:pfam02463  850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES--KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   957 --------YQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEA 1028
Cdd:pfam02463  928 eillkyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1029 IQLTFKQVSKNFSEVFQKLVPggkatlvMKKGDVEGSQSQDEGEGSGEsergsgsqsSVPSVDQFTGVGIRVSFTGKQGE 1108
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVS-------INKGWNKVFFYLELGGSAEL---------RLEDPDDPFSGGIEISARPPGKG 1071

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1109 MREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYG 1188
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVG 1151

                         1210
                   ....*....|
gi 158517902  1189 VKF-RNKVSH 1197
Cdd:pfam02463 1152 VTMvENGVST 1161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-1192 2.01e-102

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: 351.68  E-value: 2.01e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEG-TGPRVISAFVE 79
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGkNGQSGNEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    80 IIFDNSDNRLPiDKEEVSLRRVIG--AKKDQYFLDKKMVTKNDVMNLLESAGFSrSNPYYIVKQGKINQMATAPDSQRLK 157
Cdd:TIGR02169   80 VTFKNDDGKFP-DELEVVRRLKVTddGKYSYYYLNGQRVRLSEIHDFLAAAGIY-PEGYNVVLQGDVTDFISMSPVERRK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRA 237
Cdd:TIGR02169  158 IIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   238 KLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAM--------KEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKEREL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARL------AQATQERTDLY--AKQGR 381
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkeFAETRDELKDYreKLEKL 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   382 GSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNK 461
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   462 KDELQSERNYLWRE-ENAEQQALAAKREdlekkqQLLRAATGKAILNGIDsinkvldhfrrkginqhvqnGYHGIVMNNF 540
Cdd:TIGR02169  478 YDRVEKELSKLQRElAEAEAQARASEER------VRGGRAVEEVLKASIQ--------------------GVHGTVAQLG 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   541 ECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNP 617
Cdd:TIGR02169  532 SVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDP 610

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   618 RFDKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLN 697
Cdd:TIGR02169  611 KYEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   698 E--NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRE 775
Cdd:TIGR02169  689 ElsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   776 SLKAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRE 852
Cdd:TIGR02169  769 ELEEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRID 844

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   853 TEGGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 932
Cdd:TIGR02169  845 LKEQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   933 LKKKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 1011
Cdd:TIGR02169  923 KAKLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1012 KSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLvPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvD 1091
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENPD-----------------------------D 1052

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1092 QFTGvGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1171
Cdd:TIGR02169 1053 PFAG-GLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFI 1131

                         1210      1220
                   ....*....|....*....|.
gi 158517902  1172 TTTFRPELLESADKFYGVKFR 1192
Cdd:TIGR02169 1132 VVSLRSPMIEYADRAIGVTMR 1152
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 3-158 6.32e-95

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 303.80  E-value: 6.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03272     1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902   83 DNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKL 158
Cdd:cd03272    81 DNSDNRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-1198 3.01e-93

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: 325.47  E-value: 3.01e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     2 YIKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSdefshlrpEQRLALLHEGTGPRVI------- 74
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLG--------EQSAKALRGGKMEDVIfngsetr 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    75 ----SAFVEIIFDNSDNRLP-IDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRSNpYYIVKQGKINQMA 148
Cdd:TIGR02168   72 kplsLAEVELVFDNSDGLLPgADYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEII 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   149 TAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIY 228
Cdd:TIGR02168  151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   229 NQELNETRAKLDELSAKREtsgEKSRQLRDAQQDARDKMEDIErqvrELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:TIGR02168  231 VLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANEISRLEQQ 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsk 388
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL------------- 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyEVKNKKDELQSE 468
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEE 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   469 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA--ILNGIDSINKVLDHFRRKGI-------NQHVQNGYHGIVMNN 539
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELaqLQARLDSLERLQENLEGFSEgvkallkNQSGLSGILGVLSEL 528

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   540 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 614
Cdd:TIGR02168  529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   615 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 683
Cdd:TIGR02168  608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   684 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 756
Cdd:TIGR02168  688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   757 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 836
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   837 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 914
Cdd:TIGR02168  844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   915 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 991
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   992 NFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqDEG 1071
Cdd:TIGR02168  997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPE-------DLL 1069

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1072 EgsgesergsgsqssvpsvdqfTGVGIRVSFTGKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDA 1151
Cdd:TIGR02168 1070 E---------------------AGIEIFAQPPGKK--NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDD 1126

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|....*...
gi 158517902  1152 QHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNK-VSHI 1198
Cdd:TIGR02168 1127 ANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKI 1174
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-1189 1.07e-72

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 262.57  E-value: 1.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVL---SdeFSHLRPEQRLALLHEGTGPR--VIS 75
Cdd:COG1196     1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSRkpLGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   76 AFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKD-QYFLDKKMVTKNDVMNLLESAGFSRsNPYYIVKQGKINQMATAPDSQ 154
Cdd:COG1196    78 AEVSLTFDNSDGTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGP-ESYSIIGQGMIDRIIEAKPEE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  155 RLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNE 234
Cdd:COG1196   157 RRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  235 TRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQD 314
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTdlyAKQGRGSQFTSKEERdkw 394
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLE--- 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWR 474
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  475 EENAEQQALAAKREDLEKKQQLLRAATgkailngidSINKVLDHFRRKGINQHV---QNGYHGIVMNNFECEPAFYTCVE 551
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLL---------EAEADYEGFLEGVKAALLlagLRGLAGAVAVLIGVEAAYEAALE 541

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  552 VTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFDKAFKHVFGK 629
Cdd:COG1196   542 AALAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGD 620

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  630 TLICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenlrrnierinn 709
Cdd:COG1196   621 TLLGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG------------------------------------------ 656

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  710 eidqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAELGTDLLSQL 789
Cdd:COG1196   657 ------SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELE 722

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  790 SLEDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-LTAtTSELEA 868
Cdd:COG1196   723 EEALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnLLA-IEEYEE 792

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  869 INKRVKDTMARSEDLDNSIDKTEAGIKElqksmerwknmekehmdaINHDTKELekmtnrqgmllkkkeecmkkirelgs 948
Cdd:COG1196   793 LEERYDFLSEQREDLEEARETLEEAIEE------------------IDRETRER-------------------------- 828

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  949 lpqeafekyqtlslkqlfrkleqcntelkkyshvnkkaldqfvnFSEqkeklikrqeeldrgyksimelmnvlelrkyea 1028
Cdd:COG1196   829 --------------------------------------------FLE--------------------------------- 831

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1029 iqlTFKQVSKNFSEVFQKLVPGGKATLVMKKGDvegsqsqdegegsgesergsgsqssvpsvDQF-TGVGIRVSFTGKqg 1107
Cdd:COG1196   832 ---TFDAVNENFQELFPRLFGGGEAELLLTDPD-----------------------------DPLeTGIEIMAQPPGK-- 877

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1108 EMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQ--HRkaVSDMIMELAVHAQFITTTFRPELLESADK 1185
Cdd:COG1196   878 KLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFIVITHNKRTMEAADR 955


                  ....
gi 158517902 1186 FYGV 1189
Cdd:COG1196   956 LYGV 959
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 1105-1199 3.71e-57

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 197.87  E-value: 3.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1105 KQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1184
Cdd:cd03272   149 KQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVAD 228

                          90
                  ....*....|....*
gi 158517902 1185 KFYGVKFRNKVSHID 1199
Cdd:cd03272   229 KFYGVKFRNKVSTID 243
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 1062-1197 7.56e-38

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 140.14  E-value: 7.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1062 VEGSQSQDEGEGSGESERGSGSQSSVPSVDqftgVGI----RVSFTgKQGEMREMqqLSGGQKSLVALALIFAIQKCDPA 1137
Cdd:cd03239    45 VLGGKAAKLRRGSLLFLAGGGVKAGINSAS----VEItfdkSYFLV-LQGKVEQI--LSGGEKSLSALALIFALQEIKPS 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902 1138 PFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFRNKVSH 1197
Cdd:cd03239   118 PFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVHGVST 178
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 3-85 1.00e-30

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 119.72  E-value: 1.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIF 82
Cdd:cd03239     1 IKQITLKNFKSYRDETVV-GGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79


                  ...
gi 158517902   83 DNS 85
Cdd:cd03239    80 DKS 82
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 530-642 3.45e-28

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 110.01  E-value: 3.45e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    530 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYP 601
Cdd:smart00968    1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 158517902    602 ETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 642
Cdd:smart00968   80 EPGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 1114-1193 2.71e-27

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 108.99  E-value: 2.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1114 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLESADKFYGVKFR 1192
Cdd:cd03227    77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIKKV 156


                  .
gi 158517902 1193 N 1193
Cdd:cd03227   157 I 157
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1-144 5.77e-24

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 102.38  E-value: 5.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:cd03273     1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKRGQAGITKASVT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   80 IIFDNSD-NRLPIDKE---EVSLRRVIG-AKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKI 144
Cdd:cd03273    81 IVFDNSDkSQSPIGFEnypEITVTRQIVlGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 1104-1196 1.31e-23

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 99.85  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1104 GKQgeMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1183
Cdd:cd03278   105 GKK--VQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAA 182

                          90
                  ....*....|....
gi 158517902 1184 DKFYGVKFRNK-VS 1196
Cdd:cd03278   183 DRLYGVTMQESgVS 196
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 530-643 1.97e-23

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 96.56  E-value: 1.97e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   530 NGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAI 607
Cdd:pfam06470    2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 158517902   608 PMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLA 643
Cdd:pfam06470   81 PLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1114-1199 3.35e-18

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 85.43  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1114 QLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRN 1193
Cdd:cd03273   166 ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTRFVD 245


                  ....*.
gi 158517902 1194 KVSHID 1199
Cdd:cd03273   246 GTSTVT 251
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 1110-1198 9.59e-17

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 81.08  E-value: 9.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAV-HAQFITTTFRPELLESADKFYG 1188
Cdd:cd03275   151 RDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADALVG 230

                          90
                  ....*....|...
gi 158517902 1189 VkFRNK---VSHI 1198
Cdd:cd03275   231 V-YRDQecnSSKV 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-503 1.50e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 85.12  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVL-SDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:PRK03918    1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFTRIGGSGTEIELKFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   80 iiFDNSDNRL--PIDKEEVSLRRVIGAKKDqyfLDKKMVTKNDVMNLLESAGFsrSNPYYIvKQGKINQMATApDSQRLK 157
Cdd:PRK03918   79 --KNGRKYRIvrSFNRGESYLKYLDGSEVL---EEGDSSVREWVERLIPYHVF--LNAIYI-RQGEIDAILES-DESREK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKY---IEERLHTLEEEKEELAqyqkwdkmrraleytiynQELNE 234
Cdd:PRK03918  150 VVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVL------------------REINE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  235 TRAKLDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQd 314
Cdd:PRK03918  212 ISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  315 ELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGiarlaqatqertdlyakqgrgsqfTSKEERDKW 394
Cdd:PRK03918  287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------------------------EEKEERLEE 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDqainDKKRQIAAIHKDLEDTEAnKEKNLEQYNKLDQDLNevkarVEELDRKYYEVKNKKDELQSERNYLwr 474
Cdd:PRK03918  343 LKKKLKELE----KRLEELEERHELYEEAKA-KKEELERLKKRLTGLT-----PEKLEKELEELEKAKEEIEEEISKI-- 410

                         490       500
                  ....*....|....*....|....*....
gi 158517902  475 eeNAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:PRK03918  411 --TARIGELKKEIKELKKAIEELKKAKGK 437
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 3-129 7.80e-16

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 78.38  E-value: 7.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVDPFSSkHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEG--TGPRVISAFVEI 80
Cdd:cd03275     1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRArvGKPDSNSAYVTA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 158517902   81 IFDNSDNrlpidkEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAG 129
Cdd:cd03275    80 VYEDDDG------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKIN 122
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 5-82 1.01e-15

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 75.86  E-value: 1.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902    5 QVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPeqrlallHEGTGPRVISAFVEIIF 82
Cdd:cd03227     1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR-------RSGVKAGCIVAAVSAEL 71
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1110-1189 2.80e-15

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 76.18  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGV 1189
Cdd:cd03274   123 KNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGI 202
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
3-205 1.31e-14

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 73.89  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHlRPEQRLALLHEGTGprviSAFVEIIF 82
Cdd:COG0419     2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE----EASVELEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   83 DNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVK-QGKINQMATAPDSQRLKLLRE 161
Cdd:COG0419    76 EHGGKR-----------------------------------------------YRIERrQGEFAEFLEAKPSERKEALKR 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158517902  162 VAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE 205
Cdd:COG0419   109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSG 152
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 1114-1190 4.26e-13

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 68.04  E-value: 4.26e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158517902 1114 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVH-AQFITTTFRPELLE-SADKFYGVK 1190
Cdd:cd00267    80 QLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLK 154
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 3-159 1.07e-12

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 68.26  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSH-LRPEQRLALLHEGTGPR--VISAFVE 79
Cdd:cd03278     1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAGSETRkpANFAEVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   80 IIFDNSDNRlpidkeevslrrvigakkdqyfldkkmvtkndvmnllesagfsrsnpYYIVKQGKINQMATAPD--SQRLK 157
Cdd:cd03278    80 LTFDNSDGR-----------------------------------------------YSIISQGDVSEIIEAPGkkVQRLS 112


                  ..
gi 158517902  158 LL 159
Cdd:cd03278   113 LL 114
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 1-89 1.37e-12

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 70.80  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFS-HLRPEQrlalLHEGTGPRVISAFVE 79
Cdd:COG3593     1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEED----FYLGDDPDLPEIEIE 74

                          90
                  ....*....|
gi 158517902   80 IIFDNSDNRL 89
Cdd:COG3593    75 LTFGSLLSRL 84
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 113-481 1.84e-12

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 71.69  E-value: 1.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   113 KKMVTKNDVMNLLESagFSRSNPYYIVKqgkINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL 192
Cdd:pfam17380  234 EKMERRKESFNLAED--VTTMTPEYTVR---YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEK 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   193 LKYIEERLHTLEEEKEELAQYQKwdkmrralEYTIYnqelnetrAKLDELSAKRETSGEKSRQlrdaqQDARDKMEDIER 272
Cdd:pfam17380  309 AREVERRRKLEEAEKARQAEMDR--------QAAIY--------AEQERMAMERERELERIRQ-----EERKRELERIRQ 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   273 QvrELKTKISAMKEeKEQLSAERQEQiKQRTKLELKAKDLQDELagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkFN 352
Cdd:pfam17380  368 E--EIAMEISRMRE-LERLQMERQQK-NERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEEARQRE--VR 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   353 SVKEKEERGIARLAQATQERTD----------------LYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAI 416
Cdd:pfam17380  439 RLEEERAREMERVRLEEQERQQqverlrqqeeerkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   417 HKDLED-----TEANKEKNLEQYNKLDQDLNEVKaRVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 481
Cdd:pfam17380  519 EKEMEErqkaiYEEERRREAEEERRKQQEMEERR-RIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
139-499 2.92e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.22  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  139 VKQGKINQMATAPDSQR------------LKLLREVAGT------RVYDERKEESISLMKETEGKREKinELlkyiEERL 200
Cdd:PRK02224  135 VRQGEVNKLINATPSDRqdmiddllqlgkLEEYRERASDarlgveRVLSDQRGSLDQLKAQIEEKEEK--DL----HERL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  201 HTLEeekeelaqyqkwdkmrraleytiynQELNETRAKLDELSAKRETSGEKSRQLR---DAQQDARDKMEDIERQVREL 277
Cdd:PRK02224  209 NGLE-------------------------SELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDL 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  278 KTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAEtepkfnsvkek 357
Cdd:PRK02224  264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE----------- 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  358 eergiARLAQatqertdlyakqgrgSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKL 437
Cdd:PRK02224  333 -----CRVAA---------------QAHNEEAES---LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  438 DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLwREENAEQQA-LAAKREDLEKKQQLLRA 499
Cdd:PRK02224  390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDEL-REREAELEAtLRTARERVEEAEALLEA 451
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1-495 1.22e-11

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 69.23  E-value: 1.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     1 MYIKQVIIQGFRSYRDQTIVDPFSSKHN-VIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVE 79
Cdd:TIGR00618    1 MKPLRLTLKNFGSYKGTHTIDFTALGPIfLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    80 IIFDNSDNRLPI---------DKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATA 150
Cdd:TIGR00618   81 FSLGTKIYRVHRtlrctrshrKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINE----LLKYIEERLHTLEEEKEELAQYQKwdkmrralEYT 226
Cdd:TIGR00618  161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLrsqlLTLCTPCMPDTYHERKQVLEKELK--------HLR 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQqdardkmedieRQVRELKTKISAMKEEKEQLSAERQ-----EQIKQ 301
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR-----------ARIEELRAQEAVLEETQERINRARKaaplaAHIKA 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---IEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK 378
Cdd:TIGR00618  302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   379 QGRGSQFTSKEERDKWIKKELKSLD----------QAINDKKRQIAAIHKDLedtEANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:TIGR00618  382 HTLQQQKTTLTQKLQSLCKELDILQreqatidtrtSAFRDLQGQLAHAKKQQ---ELQQRYAELCAAAITCTAQCEKLEK 458

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 158517902   449 EELDRKYYEVKNKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQ 495
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQET--RKKAVVLARLLELQEEP 503
PTZ00121 PTZ00121
MAEBL; Provisional
 169-494 1.73e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.01  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  169 DERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELN---ETRAKLDELSAK 245
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKK 1452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  246 RETSgEKSRQLRDAQQDARdKMEDIERQVRELKTKISAMKEEKEqlSAERQEQIKQRTKLELKAKDLQ--DELAGNSEQR 323
Cdd:PTZ00121 1453 AEEA-KKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKkaEEAKKADEAK 1528

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  324 KRLLKERQKLLEKIEEKQKelAETEPKFNSVKEKEERGIARLAQATQERTDLY---------AKQGRGSQFTSKEERDKW 394
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKK--ADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakkAEEARIEEVMKLYEEEKK 1606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ---DLNEVKARVEELDRKYYEVKNKKDELQSErny 471
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKA--- 1683

                         330       340
                  ....*....|....*....|...
gi 158517902  472 lwrEENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1684 ---EEDEKKAAEALKKEAEEAKK 1703
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 258-500 3.06e-11

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: 66.71  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  338 EEKQKELAetepkfnsvkekeERGIARLAQATQERTDLYAKQGRGSQFTskeerdkwikKELKSLDQAINDKKRQIAAIH 417
Cdd:COG4942   100 EAQKEELA-------------ELLRALYRLGRQPPLALLLSPEDFLDAV----------RRLQYLKYLAPARREQAEELR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  418 KDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKyyevKNKKDELQSErnyLWREENAEQQALAAKREDLEKKQQLL 497
Cdd:COG4942   157 ADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229


                  ...
gi 158517902  498 RAA 500
Cdd:COG4942   230 ARL 232
PTZ00121 PTZ00121
MAEBL; Provisional
 170-510 3.61e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  170 ERKEESISLMKETEGKReKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETS 249
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAK-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  250 GEKSRQLRDAQQ----DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ--RTKLELKAKDLQDELAGNSEQR 323
Cdd:PTZ00121 1533 AKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA 1612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  324 KRLLKERQKLLE-KIEEKQKELAETEPKfnsvKEKEERGIARLAQATQERTDLyakqgRGSQFTSKEERDKWIKKELKSL 402
Cdd:PTZ00121 1613 KKAEEAKIKAEElKKAEEEKKKVEQLKK----KEAEEKKKAEELKKAEEENKI-----KAAEEAKKAEEDKKKAEEAKKA 1683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  403 DQainDKKRQIAAIHKDLEdtEANK--------EKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELqsernylwR 474
Cdd:PTZ00121 1684 EE---DEKKAAEALKKEAE--EAKKaeelkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------K 1750

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 158517902  475 EENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 510
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-500 4.17e-11

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.10  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFshlrpEQRLALLHEGTGPRVISAFVEI 80
Cdd:COG4717     1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL-----EKEADELFKPQGRKPELNLKEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   81 ifdnsdnrlpidKEEVSLRRVIGAKKDQYfldkkmvtkndvmnllesagfsrsnpyyivkQGKINQMATApDSQRLKLLR 160
Cdd:COG4717    74 ------------KELEEELKEAEEKEEEY-------------------------------AELQEELEEL-EEELEELEA 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  161 EVAGTRVYDERKEESISLmKETEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALE------YTIYNQELN 233
Cdd:COG4717   110 ELEELREELEKLEKLLQL-LPLYQELEALEAELAELPERLEELEERLEELRELEeELEELEAELAelqeelEELLEQLSL 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  234 ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAmKEEKEQLSAERQ----------------- 296
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLllliaaallallglggs 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  297 ------------------------EQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKL-------LEKIEEKQKELA 345
Cdd:COG4717   268 llsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIE 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  346 ETEPKFNSVKEKEERgiARLAQATQERTDLYAKQGrgsqFTSKEERDKWIK--KELKSLDQAINDKKRQIAAIHKDLED- 422
Cdd:COG4717   348 ELQELLREAEELEEE--LQLEELEQEIAALLAEAG----VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEEl 421

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158517902  423 -TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYlwREENAEQQALAAKREDLEKKQQLLRAA 500
Cdd:COG4717   422 lEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKLA 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
168-503 4.37e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.40  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  168 YDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK03918  319 LEEEINGIEERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEK-------EQLSAERQEQIKQRTKLELkaKDLQDELAgNS 320
Cdd:PRK03918  395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAEL--KRIEKELK-EI 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  321 EQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEER----GIARLAQATQERTDLYAK----QGRGSQFTSKEERD 392
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKliklKGEIKSLKKELEKL 551

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  393 KWIKKELKSLDQAINDKKRQIAAIHKDLEdteankEKNLEQYNKLDQDLNEvkarVEELDRKYYEVKNKKDELQSERNYL 472
Cdd:PRK03918  552 EELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKE----LEPFYNEYLELKDAEKELEREEKEL 621

                         330       340       350
                  ....*....|....*....|....*....|.
gi 158517902  473 WREENaeqqALAAKREDLEKKQQLLRAATGK 503
Cdd:PRK03918  622 KKLEE----ELDKAFEELAETEKRLEELRKE 648
COG4637 COG4637
Predicted ATPase [General function prediction only];
3-181 1.63e-10

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 64.18  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTI-VDPFsskhNVIVGRNGSGKSNFFYAIQF---------------------VLSDEFSHLRPEQ 60
Cdd:COG4637     2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRFlsdaargglqdalarrggleeLLWRGPRTITEPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   61 RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRviGAKKDQYFLDKKMVTknDVMNLLESAGFSRSnpyyivk 140
Cdd:COG4637    78 RLELEFAEEDERDLRYELELGLPEPGGRPEVKEERLWLKR--GSGGRPFLDFRPKGR--AVGGEPERLDSPES------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 158517902  141 qgKINQMATAPDSQRLKLLRE-VAGTRVYDERkeesISLMKE 181
Cdd:COG4637   147 --LLSQLGDPERFPELRALREaLRSWRFYDFH----PAPLRQ 182
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1-151 2.52e-10

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 61.54  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTG-PRVISAFVE 79
Cdd:cd03274     1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158517902   80 IIFdnsdnrlpidkeevslrrvigakkdQYFLDKKmvtkndvmnLLESAGFSRSNPYYIVKQGKINQMATAP 151
Cdd:cd03274    81 VHF-------------------------QEIIDKP---------LLKSKGIDLDHNRFLILQGEVEQIAQMP 118
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-903 4.36e-10

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 64.17  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  262 DARDKMEDIERQVRELkTKISAMKEEKEQLSAERQEQIKQRTKLELKAkdlqdelagnSEQRKRLLKERqkllekIEEKQ 341
Cdd:COG4913   239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWF----------AQRRLELLEAE------LEELR 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  342 KELAETEpkfnsvkEKEERGIARLAQATQERTDLYAKQgRGSQFTSKEErdkwIKKELKSLDQAINDKKRQIAAIHKDLE 421
Cdd:COG4913   302 AELARLE-------AELERLEARLDALREELDELEAQI-RGNGGDRLEQ----LEREIERLERELEERERRRARLEALLA 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  422 D----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERnylwREENAEQQALAAKREDLEKKQQLL 497
Cdd:COG4913   370 AlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARLLAL 445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  498 RAATGKAIlnGIDSIN--------KVLDHFRRkginqhvqngyhgivmnnfeCEPAfytcVEVTAGNRLFYHIVDS---D 566
Cdd:COG4913   446 RDALAEAL--GLDEAElpfvgeliEVRPEEER--------------------WRGA----IERVLGGFALTLLVPPehyA 499

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  567 EVSTKIlmefNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPmiSKLRYNPrfdkafkHVFGktlicrsMEVSTQLARAF 646
Cdd:COG4913   500 AALRWV----NRLHLRGRLVYERVRTGLPDPERPRLDPDSLA--GKLDFKP-------HPFR-------AWLEAELGRRF 559

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  647 TMDC-------------ITLEGdQVSHRGALtgGYYDTRK---SRLELQKDVRKAEeelgeleaklnENLRRNIERINNE 710
Cdd:COG4913   560 DYVCvdspeelrrhpraITRAG-QVKGNGTR--HEKDDRRrirSRYVLGFDNRAKL-----------AALEAELAELEEE 625

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  711 IDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESLKAelgtdllsqls 790
Cdd:COG4913   626 LAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERLDA----------- 682

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  791 leDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGTVLTATTSELEAIN 870
Cdd:COG4913   683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAAEDLARLELRALLE 752

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 158517902  871 KRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 903
Cdd:COG4913   753 ERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
182-467 5.23e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.91  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  182 TEGKREKINELlkyiEERLHTLEEEKEELAQyqkwdKMRRAleytiynQELNETRAKLDELSAKRETSGEKsrqlrdaqq 261
Cdd:PRK02224  470 IEEDRERVEEL----EAELEDLEEEVEEVEE-----RLERA-------EDLVEAEDRIERLEERREDLEEL--------- 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  262 dardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgNSEQRKRLLKERQKLLEKIEEKQ 341
Cdd:PRK02224  525 -----IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLERIRTLL 598

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  342 KELAETEPKFNSVKEKEErgiARLAQATQERTDLYAKQGRGSQFTSK--EERDKWIKKELKSLDQAI---NDKKRQIAAI 416
Cdd:PRK02224  599 AAIADAEDEIERLREKRE---ALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLeqvEEKLDELREE 675

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 158517902  417 HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVknkkDELQS 467
Cdd:PRK02224  676 RDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEA----EELES 722
AAA_23 pfam13476
AAA domain;
6-191 6.14e-10

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 59.82  E-value: 6.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     6 VIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLH---EGTGPRVISAFVEIIF 82
Cdd:pfam13476    1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKgdiRIGLEGKGKAYVEITF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    83 DNSDNR-LPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYI-VKQGKINQMATAPDSQRLKLLR 160
Cdd:pfam13476   79 ENNDGRyTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVfLGQEREEEFERKEKKERLEELE 158

                          170       180       190
                   ....*....|....*....|....*....|.
gi 158517902   161 EVAGTRVYDERKEESISLMKETEGKREKINE 191
Cdd:pfam13476  159 KALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
PTZ00121 PTZ00121
MAEBL; Provisional
 150-494 8.70e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  150 APDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE---KINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEY 225
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  226 TIYNQ-ELNETRAKLDELSA-----KRETSGEKSRQLRDAQQdARDKMEDIERQVRELKTKISAMKEEKEqlSAERQEQI 299
Cdd:PTZ00121 1354 AAADEaEAAEEKAEAAEKKKeeakkKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEK 1430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  300 KQRTKLELKAKDLQ--DELAGNSEQRKRLLKERQKLLEKIE-EKQKELAETEPKFNSVKEKEERGIARLAQATQ-ERTDL 375
Cdd:PTZ00121 1431 KKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaAEAKK 1510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  376 YAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD--- 452
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkae 1590

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 158517902  453 --RKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1591 eaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 180-387 9.64e-10

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 62.09  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  180 KETEGKREKINELLKYIEERLHTLEEEKEELA-QYQKWDKMRRALEYTI--YNQELNETRAKLDELSAKRETSGEK---- 252
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEleaq 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  253 ----SRQLRDAQQDAR----------DKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAG 318
Cdd:COG4942   103 keelAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  319 NSEQRKRL---LKERQKLLEKIE----EKQKELAEtepkfnsvKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG4942   183 LEEERAALealKAERQKLLARLEkelaELAAELAE--------LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-454 2.31e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 60.93  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  309 AKDLQDELAG-------NSEQR---------------------KRLLKERQKLLEKIEEKQKELAETEpkfnsvkekeer 360
Cdd:COG4942    99 LEAQKEELAEllralyrLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALR------------ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  361 giARLAQATQERTDLYAKQgrgsqftskeerdkwiKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQD 440
Cdd:COG4942   167 --AELEAERAELEALLAEL----------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228

                         250
                  ....*....|....
gi 158517902  441 LNEVKARVEELDRK 454
Cdd:COG4942   229 IARLEAEAAAAAER 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-517 2.40e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.98  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEE---EKEELAQyQKWDKMRRALEYtiyNQELNETRAK-------- 238
Cdd:PRK02224  234 ETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAE-EVRDLRERLEEL---EEERDDLLAEaglddada 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  239 ------LDELSAKRETSGEKSRQLRDAQQDA-------RDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL 305
Cdd:PRK02224  310 eavearREELEDRDEELRDRLEECRVAAQAHneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  306 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQAT-----QERTDlyakQG 380
Cdd:PRK02224  390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG----SP 465

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  381 RGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIhKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKN 460
Cdd:PRK02224  466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158517902  461 KKDELQSErnylwrEENAEQQAlAAKREDLEKKQQLLRAATGK--AILNGIDSINKVLD 517
Cdd:PRK02224  545 RAAELEAE------AEEKREAA-AEAEEEAEEAREEVAELNSKlaELKERIESLERIRT 596
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1-472 4.19e-09

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 61.07  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVdpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRPEQRLALLHEGTGPRVISAFVEI 80
Cdd:PRK01156    1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMIKKGKNNLEVELEFRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   81 IFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMvtkNDVMNLLESAGFSRSNPYYI----VKQGKINQMATAPDSQRL 156
Cdd:PRK01156   76 GGHVYQIRRSIERRGKGSRREAYIKKDGSIIAEGF---DDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  157 KLLREVAG----TRVYDERKEESISLMKETEGKREKINELLKYIEErlhtLEEEKEELAQYQKW------DKMRRALEYT 226
Cdd:PRK01156  153 KILDEILEinslERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKShsitlkEIERLSIEYN 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDardkMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE 306
Cdd:PRK01156  229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYK 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  307 lkakdlqdelaGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEErgiaRLAQATQERTDLYAKQGR-GSQF 385
Cdd:PRK01156  305 -----------NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS----RYDDLNNQILELEGYEMDyNSYL 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  386 TSKEERDKWIKKELKsldqainDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDEL 465
Cdd:PRK01156  370 KSIESLKKKIEEYSK-------NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL 442


                  ....*..
gi 158517902  466 QSERNYL 472
Cdd:PRK01156  443 SRNMEML 449
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 1101-1171 6.40e-09

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 57.22  E-value: 6.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517902 1101 SF-TGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFI 1171
Cdd:cd03276    95 SFlTSNKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAkkqPGRQFI 169
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
8-524 6.55e-09

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 60.13  E-value: 6.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    8 IQGFRSYRDQTIVDPFSSKhNVIVGRNGSGK---SNFFYAIQfvLSDEFSHLRPEQRLALLHEGTGPRVI---SAFVEII 81
Cdd:COG4694     8 LKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE--LGDTSSEVIAEFEIEAGGSAPNPSVRvfnRDFVEEN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   82 FDNSDNRLPI---DKEEVSLRRVIGAKKDQyfLDKKMVTKNDVMNLLESAgfsrsnpyyivkqgkinqmatapDSQRLKL 158
Cdd:COG4694    85 LRSGEEIKGIftlGEENIELEEEIEELEKE--IEDLKKELDKLEKELKEA-----------------------KKALEKL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  159 LREVAGTRVyderkeESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAK 238
Cdd:COG4694   140 LEDLAKSIK------DDLKKLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEA 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  239 LDELSAKRETSGEKsrQLRDAQQDardkmEDIERQVRELKTKISAMKEEK----EQ-LSAERQEQIKQRtklelkakdLQ 313
Cdd:COG4694   214 ETLLEKSAVSSAIE--ELAALIQN-----PGNSDWVEQGLAYHKEEEDDTcpfcQQeLAAERIEALEAY---------FD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  314 DELAGNSEQRKRLLKERQKLLEKIEEkqKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERD 392
Cdd:COG4694   278 DEYEKLLAALKDLLEELESAINALSA--LLLEILRTLLPSAKEDLKAALEALNALLETlLAALEEKIANPSTSIDLDDQE 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  393 KW--IKKELKSLDQAINDKKRQIAaihkDLEDTEANKEKNLEQY--NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSe 468
Cdd:COG4694   356 LLdeLNDLIAALNALIEEHNAKIA----NLKAEKEEARKKLEAHelAELKEDLSRYKAEVEELIEELKTIKALKKALED- 430

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  469 rnylwreenaeqqaLAAKREDLEKKQqllraatgKAILNGIDSINKVLDHFRRKGI 524
Cdd:COG4694   431 --------------LKTEISELEAEL--------SSVDEAADEINEELKALGFDEF 464
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
166-469 8.29e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKE----------ELAQYQKWDKMRRaleytiYNQELNET 235
Cdd:PRK03918  391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEE------YTAELKRI 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  236 RAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRT-KLELKAKDL 312
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEIKSL 544

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  313 QDELagnsEQRKRLLKERQKLLEKIEEKQKELAETEPK-----FNSVKEKEERgIARLAQATQERTDLyakQGRGSQFTS 387
Cdd:PRK03918  545 KKEL----EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEER-LKELEPFYNEYLEL---KDAEKELER 616

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  388 KEERDKWIKKELKSLDQAINDKKRQIAAIHKDLED-----TEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKK 462
Cdd:PRK03918  617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696


                  ....*..
gi 158517902  463 DELQSER 469
Cdd:PRK03918  697 EKLKEEL 703
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 1-336 1.21e-08

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 58.76  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPrvisafVEI 80
Cdd:pfam13175    1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKI------DKE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    81 IFDNSDNRLPIDKEEVSLrrvigakkdqYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKInqmATAPDSQRLKLLR 160
Cdd:pfam13175   73 DLNIFENISFSIDIEIDV----------EFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKG---ANKADLLLELKIS 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   161 EVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQE--LNETRAK 238
Cdd:pfam13175  140 DLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHEnvLENLQIK 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   239 LDELSAKRETSGEKSRQLRDA-----QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlelkaKDLQ 313
Cdd:pfam13175  220 KLLISADRNASDEDSEKINSLlgalkQRIFEEALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKID-----KLKD 294

                          330       340
                   ....*....|....*....|...
gi 158517902   314 DELAGNSEQRKRLLKERQKLLEK 336
Cdd:pfam13175  295 FGYPPFLNPEIEIKKDDEDLPLN 317
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 186-497 1.43e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 59.36  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   186 REKINELLKYIEERLHTLEEeKEELAQYQKwDKMRRALEyTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam15921  266 QDRIEQLISEHEVEITGLTE-KASSARSQA-NSIQSQLE-IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   266 KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER-------QKLLEKIE 338
Cdd:pfam15921  343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtgnsitiDHLRRELD 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   339 EKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK-QGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAaih 417
Cdd:pfam15921  423 DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS--- 499

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   418 kDLEDTEANKEKNLEQYNkldQDLNEVKARVEELDRKYYEVKNKKDEL---QSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam15921  500 -DLTASLQEKERAIEATN---AEITKLRSRVDLKLQELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMT 575


                   ...
gi 158517902   495 QLL 497
Cdd:pfam15921  576 QLV 578
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
261-520 2.30e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  261 QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKL---------ELKAKDLQDELAGNSEQRKRLLK--- 328
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAssd 685

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  329 ERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEER---DKWIKKELksLDQA 405
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAAL--GDAV 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  406 INDKKRQIAAIHKDLEDTEANKEKNLEqyNKLDQDLNEVKARVEELDrkyyevknkkDELQSERNYLWREENAEQQALAA 485
Cdd:COG4913   764 ERELRENLEERIDALRARLNRAEEELE--RAMRAFNREWPAETADLD----------ADLESLPEYLALLDRLEEDGLPE 831

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 158517902  486 KREDLekKQQLLRAATG-------------KAILNGIDSINKVLDHFR 520
Cdd:COG4913   832 YEERF--KELLNENSIEfvadllsklrraiREIKERIDPLNDSLKRIP 877
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 180-387 2.31e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.53  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  180 KETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEK-SRQLRD 258
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNE--EYNELQAELEAL--QAEIDKLQAEIAEAEAEIEERREElGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  259 AQQ------------------DARDKMEDIER-------QVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQ 313
Cdd:COG3883    95 LYRsggsvsyldvllgsesfsDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902  314 DELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS 387
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-65 2.82e-08

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 56.54  E-value: 2.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517902    1 MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALL 65
Cdd:COG3950     1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
PTZ00121 PTZ00121
MAEBL; Provisional
 150-450 4.51e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  150 APDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiyn 229
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----- 1657

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  230 qelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQ------VRELKTKISAMKEEKEQLSAERQE---QIK 300
Cdd:PTZ00121 1658 ----ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEEnkiKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  301 QRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKfnSVKEKEERGIARLAQATQERTDLYA--- 377
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFAnii 1811

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  378 ---KQGRGSQFTSKEERDKWIKKELKSLDQAIND----KKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEE 450
Cdd:PTZ00121 1812 eggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 186-456 4.96e-08

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 57.24  E-value: 4.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  186 REKINELLKYIEER--LHtLEEEKEELAQyqkwDKMRRALEYTIynqELNETRAKLDELSAKRETSGE-----KSRQLRD 258
Cdd:PRK05771   15 KSYKDEVLEALHELgvVH-IEDLKEELSN----ERLRKLRSLLT---KLSEALDKLRSYLPKLNPLREekkkvSVKSLEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  259 AQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERqEQIKQRTKLELKAKDLQDElaGNSEQRKRLLKERQKLLEKIE 338
Cdd:PRK05771   87 LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI-ERLEPWGNFDLDLSLLLGF--KYVSVFVGTVPEDKLEELKLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  339 EKQKELAETEPKFNSV-------KEKEERGIARLAQATQERTDLYAKQgrgsqfTSKEERDKwIKKELKSLDQAINDKKR 411
Cdd:PRK05771  164 SDVENVEYISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEG------TPSELIRE-IKEELEEIEKERESLLE 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 158517902  412 QIAAIHKDLEDTEankeknLEQYNKLDQDLNEVKARVEELDRKYY 456
Cdd:PRK05771  237 ELKELAKKYLEEL------LALYEYLEIELERAEALSKFLKTDKT 275
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 230-371 5.04e-08

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.32  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  230 QELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkEEKEQLSAERQEQIKQ-RTKLELK 308
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvRNNKEYE 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  309 AkdLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE 371
Cdd:COG1579    93 A--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
recF PRK00064
recombination protein F; Reviewed
 1-57 5.49e-08

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 56.32  E-value: 5.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158517902    1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvlsdeFSHLR 57
Cdd:PRK00064    1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAIYL-----LAPGR 50
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
170-461 9.56e-08

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.30  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALeytiyNQELNETRAKLDELSAKRETS 249
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE------KRDEL-----NAQVKELREEAQELREKRDEL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE--LAGNSEQRKRLL 327
Cdd:COG1340    70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEkeLVEKIKELEKEL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  328 KERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQERTDLYAKQgrgsqftsKEERDKwIKKELKSLDQAIN 407
Cdd:COG1340   150 EKAKKALEKNEKLKELRAELKELRKEAEEIHKK-IKELAEEAQELHEEMIEL--------YKEADE-LRKEADELHKEIV 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  408 DKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--ARVEELDRKYYEVKNK 461
Cdd:COG1340   220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKreKEKEELEEKAEEIFEK 275
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-374 1.07e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  186 REKInELLKYIEERLHTLEEEKEELAQyqkWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:COG4913   248 REQI-ELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  266 KMEDIERQVR--------ELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA------------------KDLQDELAGN 319
Cdd:COG4913   324 ELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaalraeaaallEALEEELEAL 403

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158517902  320 SEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTD 374
Cdd:COG4913   404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-459 1.23e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  186 REKINEL---LKYIEERLHTLEEEKEEL-AQYQKWDKMRRAL----EYTIYNQELNETRAKLDELSAKR---ETSGEKSR 254
Cdd:COG4913   609 RAKLAALeaeLAELEEELAEAEERLEALeAELDALQERREALqrlaEYSWDEIDVASAEREIAELEAELerlDASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  255 QLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQDELAGNSEQ--R 323
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaeDLARLELRALLEERFAAALGDAVERelR 768

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  324 KRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERG-----------IARLAQatQERTDLYAKQGR-GSQFTSKEER 391
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADldadleslpeyLALLDR--LEEDGLPEYEERfKELLNENSIE 846

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902  392 DkwiKKELKS-LDQAINDKKRQIAAIHKDLEDTEANKEKNL---------EQYNKLDQDLNEVKARVEELDRKYYEVK 459
Cdd:COG4913   847 F---VADLLSkLRRAIREIKERIDPLNDSLKRIPFGPGRYLrlearprpdPEVREFRQELRAVTSGASLFDEELSEAR 921
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
3-214 2.12e-07

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 54.28  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    3 IKQVIIQGFRSYRDQTIVDPFSSKH-----NVIVGRNGSGKSNFFYAIQFVLS-DEFSHLRPEQRLALLHEGTGPRVISA 76
Cdd:COG1106     2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFLRNlVLNSSQPGDKLVEPFLLDSESKNEPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   77 FVEIIFDNSDNRLPIdKEEVSLRRVIgaKKDQYFLdkkmvtkndvmnlleSAGFSRSNPYYIvkqgkinqmatapdsqrl 156
Cdd:COG1106    82 EFEILFLLDGVRYEY-GFELDKERII--SEWLYFL---------------STAAQLNVPLLS------------------ 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902  157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIE---ERLHTLEEEKEELAQYQ 214
Cdd:COG1106   126 PLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLKIADpgiEDIEVEEEEIEDLVERK 186
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 287-504 2.76e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.45  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  287 EKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERgIARLA 366
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREE-LGERA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  367 QATQER----------------TDLYAKQGRGSQFTskeERDKWIKKELKSLDQAINDKKRQIAaihKDLEDTEANKEKN 430
Cdd:COG3883    93 RALYRSggsvsyldvllgsesfSDFLDRLSALSKIA---DADADLLEELKADKAELEAKKAELE---AKLAELEALKAEL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902  431 LEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
183-375 3.04e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 54.64  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  183 EGKREKINELLKYIEERLHTLEEEKEE----LAQY-QKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKELEEaeaaLEEFrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  258 DAQQDARDKMEDIERQVRelktkISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAgnsEQRKRLLKERQKLLEKI 337
Cdd:COG3206   247 AQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA---ALRAQLQQEAQRILASL 318

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 158517902  338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDL 375
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 172-498 3.39e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 54.80  E-value: 3.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   172 KEESISLMKEtegKREKINELLKYIEERLHTLEEEKEELAQ--------YQKWDKMRRALEYTiyNQELNETrakLDELS 243
Cdd:pfam01576   10 KEEELQKVKE---RQQKAESELKELEKKHQQLCEEKNALQEqlqaetelCAEAEEMRARLAAR--KQELEEI---LHELE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRElktkisamkEEkeqlsAERQEQIKQRTKLELKAKDLQDELAGNSEQR 323
Cdd:pfam01576   82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE---------EE-----AARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   324 KRLLKERQKLLEKIEEKQKELAETEPK---FNSVKEKEERGIA----RLAQATQERTDLyAKQGRGSQFTSKEERDkwik 396
Cdd:pfam01576  148 SKLSKERKLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISdleeRLKKEEKGRQEL-EKAKRKLEGESTDLQE---- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   397 kELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdrkyyevknkKDELQSERNYlwrEE 476
Cdd:pfam01576  223 -QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISEL----------QEDLESERAA---RN 288

                          330       340
                   ....*....|....*....|..
gi 158517902   477 NAEQQalaakREDLEKKQQLLR 498
Cdd:pfam01576  289 KAEKQ-----RRDLGEELEALK 305
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
169-464 3.66e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  169 DERKEESISLMKETEGKREKINELLKYiEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELsakrET 248
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSL----KK 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:PRK03918  547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  329 ERQKLLEKIEEKQKELAETEPKFNSVKEKeergiarlaqATQERtdlyakqgrgsqFTSKEERDKWIKKELKSLDQAIND 408
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKK----------YSEEE------------YEELREEYLELSRELAGLRAELEE 684

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  409 KKRQIAAIHKDLEDTEANKEKnLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 464
Cdd:PRK03918  685 LEKRREEIKKTLEKLKEELEE-REKAKKELEKLEKALERVEELREKVKKYKALLKE 739
PTZ00121 PTZ00121
MAEBL; Provisional
 143-505 3.81e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  143 KINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRA 222
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  223 LEYtiynqELNETRAKLDELSAKRETSgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:PTZ00121 1293 DEA-----KKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  303 TKLELK---AKDLQDELAGNSEQRKR---LLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLY 376
Cdd:PTZ00121 1367 EAAEKKkeeAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  377 AKQGRGSQFTSKEERDKWIKKELKSLDQ-----------------AINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ 439
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeakkadeakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  440 DLNEVKARVEELDRKYYEVKnKKDELQSERNYLWREEnaEQQALAAKREDLEKKQQLLRAATGKAI 505
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKK-KADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKA 1589
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-453 4.45e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  170 ERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwdkmrraleytiynqelnETRAKLDELSAKRETS 249
Cdd:PRK02224  499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE----------------------ELRERAAELEAEAEEK 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  250 GEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLsAERQEQIKQRTKLELKAKDLQDElagNSEQRKRL--L 327
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-AAIADAEDEIERLREKREALAEL---NDERRERLaeK 632

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  328 KERQKLLE------KIEEKQKELAETEPKFNSVKEKeergiarLAQATQERTDLYAKQGRgsqftskeerdkwIKKELKS 401
Cdd:PRK02224  633 RERKRELEaefdeaRIEEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEIGA-------------VENELEE 692

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158517902  402 LDqAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNevKARVEELDR 453
Cdd:PRK02224  693 LE-ELRERREALENRVEALEALYDEAEELESMYGDLRAELR--QRNVETLER 741
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 166-457 5.44e-07

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 54.07  E-value: 5.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   166 RVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR-AKLDELSA 244
Cdd:pfam12128  657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALdAQLALLKA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   245 KREtsgeKSRQLRDAQQDA---------------RDKMEDIERQVRELKTKISAMKEEK-----------EQLSAERQEQ 298
Cdd:pfam12128  737 AIA----ARRSGAKAELKAletwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRqevlryfdwyqETWLQRRPRL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkekEERGIARL---AQATQERTDL 375
Cdd:pfam12128  813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC----EMSKLATLkedANSEQAQGSI 888

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   376 YAKQGRGSQFTSKEERDKW-IKKELKSLDQAINDKKRQIAAIH----KDLEDTEANKEKNLEQYNKLDQDLNEV-KARVE 449
Cdd:pfam12128  889 GERLAQLEDLKLKRDYLSEsVKKYVEHFKNVIADHSGSGLAETweslREEDHYQNDKGIRLLDYRKLVPYLEQWfDVRVP 968


                   ....*...
gi 158517902   450 ELDRKYYE 457
Cdd:pfam12128  969 QSIMVLRE 976
PTZ00121 PTZ00121
MAEBL; Provisional
 143-494 6.76e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKRE--------KINELLKYIEERLHTLEEEKEELAQY 213
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEaRKAEDAKKAEAARKAEEvrkaeelrKAEDARKAEAARKAEEERKAEEARKA 1220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  214 Q---KWDKMRRALEytiynqelnetrAKLDELSAKRetsGEKSRQLRDAQQDARDKMEDIERqvRELKTKISAMKEEKEQ 290
Cdd:PTZ00121 1221 EdakKAEAVKKAEE------------AKKDAEEAKK---AEEERNNEEIRKFEEARMAHFAR--RQAAIKAEEARKADEL 1283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  291 LSAERQEQIKQRTKLELKAKdlQDELAGNSEQRKRL--LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQA 368
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKAdeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  369 TQERTDlyAKQGRGSQFTSKEERDKWIKKELKSLDQAiNDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQdlnevKARV 448
Cdd:PTZ00121 1362 AEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-----KKKA 1433

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 158517902  449 EELDRKYYEvKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:PTZ00121 1434 DEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 146-412 9.74e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.20  E-value: 9.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   146 QMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKRE--KINELlkyieerlhtleeEKEELAQYQKWDKMRRAL 223
Cdd:pfam17380  332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEisRMREL-------------ERLQMERQQKNERVRQEL 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   224 EYTIYNQELNETRAKldelsaKRETSGEKSRQLRDAQQDARdkmediERQVRELKTKISAMKEEKEQLSAERQEQIKQRT 303
Cdd:pfam17380  399 EAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAREMERVRLEEQERQQQVERLR 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   304 KLELKAKDLQDELAGNSEQRKRLLKERQKLLEK---------IEEKQKEL---AETEPKFNSVKEKEERGIA----RLAQ 367
Cdd:pfam17380  467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkqamIEEERKRKlleKEMEERQKAIYEEERRREAeeerRKQQ 546

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 158517902   368 ATQERTDLyakQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQ 412
Cdd:pfam17380  547 EMEERRRI---QEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
289-510 9.97e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  289 EQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQA 368
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANK-EKNLEQYNKLDQDLNEVKAR 447
Cdd:COG4717   128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  448 VEELDRKYYEVKNKKDELQSErnylwREENAEQQALAAKREDLEKKQQLLRAATGKAILNGID 510
Cdd:COG4717   208 LAELEEELEEAQEELEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 179-357 1.01e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.46  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  179 MKETEGKREKINELLKYIEERLHTLEEEKEEL-AQYQKWDKMRRALEYTIY-------------NQELNETRAKLDELSA 244
Cdd:COG4942    64 IAALARRIRALEQELAALEAELAELEKEIAELrAELEAQKEELAELLRALYrlgrqpplalllsPEDFLDAVRRLQYLKY 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  245 KRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRK 324
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         170       180       190
                  ....*....|....*....|....*....|...
gi 158517902  325 RLlkerQKLLEKIEEKQKELAETEPKFNSVKEK 357
Cdd:COG4942   224 EL----EALIARLEAEAAAAAERTPAAGFAALK 252
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 181-343 1.16e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 52.65  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   181 ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkmRRALEYTIYNQELNETRAKLDELSAKRetsgekSRQLRDAQ 260
Cdd:pfam15709  349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQ----RRFEEIRLRKQRLEEERQRQEEEERKQ------RLQLQAAQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   261 QDARDKMEDIERQVRELKTKisamkeeKEQLSAERQEQIKQRTK-LELKAKDLQDELAGNSE------QRKRLLKERQKL 333
Cdd:pfam15709  419 ERARQQQEEFRRKLQELQRK-------KQQEEAERAEAEKQRQKeLEMQLAEEQKRLMEMAEeerleyQRQKQEAEEKAR 491

                          170
                   ....*....|
gi 158517902   334 LEKIEEKQKE 343
Cdd:pfam15709  492 LEAEERRQKE 501
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-47 1.50e-06

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 51.69  E-value: 1.50e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 158517902    2 YIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQF 47
Cdd:COG1195     1 RLKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEAIYL 44
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 267-359 1.65e-06

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 52.39  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  267 MEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE 346
Cdd:COG0542   413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDE---LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE 489

                          90
                  ....*....|...
gi 158517902  347 TEPKFNSVKEKEE 359
Cdd:COG0542   490 LEKELAELEEELA 502
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
 795-1213 2.57e-06

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 51.66  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   795 KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlrkrLDQVEQELNELRETEGGTVLTattSELEAINKRVK 874
Cdd:TIGR00634  161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEE-----LEEADLQPGEDEALEAEQQRL---SNLEKLRELSQ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   875 DTMAR-SEDLDNSIDKTEAGIKELQKSMErwknmekehmdaiNHDTKELEKMTNRQGMLLKKKEECMKKIRELGS----L 949
Cdd:TIGR00634  233 NALAAlRGDVDVQEGSLLEGLGEAQLALA-------------SVIDGSLRELAEQVGNALTEVEEATRELQNYLDelefD 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   950 PQEAFEKYQTLS-LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYksIMELMNVLELRKYEA 1028
Cdd:TIGR00634  300 PERLNEIEERLAqIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEEL--DKAAVALSLIRRKAA 377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1029 iqltfKQVSKNFSEVFQKLvpggkaTLVMKKGDVEGSQSQDEGEGSGESERGsgsqssvpsVDQftgvgIRVSFTGKQGE 1108
Cdd:TIGR00634  378 -----ERLAKRVEQELKAL------AMEKAEFTVEIKTSLPSGAKARAGAYG---------ADQ-----VEFLFSANTGE 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1109 mrEMQQL----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESAD 1184
Cdd:TIGR00634  433 --PVKPLakvaSGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHAD 510

                          410       420
                   ....*....|....*....|....*....
gi 158517902  1185 KFYGVKfrnKVShIDVITAEMAKDFVEDD 1213
Cdd:TIGR00634  511 AHFKVE---KEG-LDGRTATRVRPLSGEE 535
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 168-489 2.83e-06

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 51.88  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEE----KEELAQYQKWDKM--RRALEYTIYNQELNETRA--KL 239
Cdd:COG3096   352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEvdslKSQLADYQQALDVqqTRAIQYQQAVQALEKARAlcGL 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  240 DELSAKretsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA------------ERQEQIKQRTKLEL 307
Cdd:COG3096   432 PDLTPE---------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiagevERSQAWQTARELLR 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  308 KAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGrgsqfTS 387
Cdd:COG3096   503 RYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA-----EA 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  388 KEERdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQS 467
Cdd:COG3096   577 VEQR-----SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAA 651

                         330       340
                  ....*....|....*....|..
gi 158517902  468 ERNYLwrEENAEQQALAAKRED 489
Cdd:COG3096   652 RKQAL--ESQIERLSQPGGAED 671
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 3-58 3.10e-06

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 49.14  E-value: 3.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902    3 IKQVIIQGFRSYRDQTIVDpFSSKHNVIVGRNGSGKSNFFYAIQFVLsdeFSHLRP 58
Cdd:cd03240     1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL---TGELPP 52
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
230-494 3.21e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.29  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  230 QELNETRAKLDELSAKREtsgeksrQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRtklelka 309
Cdd:COG1340     1 SKTDELSSSLEELEEKIE-------ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERgIARLAQATQ-------ERTDLYAKQGRG 382
Cdd:COG1340    67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQtevlspeEEKELVEKIKEL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  383 SQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKK 462
Cdd:COG1340   146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225

                         250       260       270
                  ....*....|....*....|....*....|..
gi 158517902  463 DELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:COG1340   226 DELHEEIIELQKELRELRKELKKLRKKQRALK 257
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
699-1029 3.59e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  699 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 775
Cdd:PRK03918  169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  776 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 855
Cdd:PRK03918  242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  856 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 930
Cdd:PRK03918  318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  931 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 996
Cdd:PRK03918  396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474

                         330       340       350
                  ....*....|....*....|....*....|...
gi 158517902  997 KEKLIKRQEELDrgyksiMELMNVLELRKYEAI 1029
Cdd:PRK03918  475 ERKLRKELRELE------KVLKKESELIKLKEL 501
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 231-447 3.73e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  231 ELNETRAKLDELSAKRETSGEksrQLRDAQQDARDKMEDIER---QVRELKTKISAMKEE---KEQLSAERQEQIKQR-- 302
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNElqaELEALQAEIDKLQAEiaeAEAEIEERREELGERar 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  303 ---------TKLE--LKAKDLQDeLAGNSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKEERGIARLAQATQE 371
Cdd:COG3883    94 alyrsggsvSYLDvlLGSESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAELEALKAELEAA 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902  372 RTDLYAKQgrgsqfTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 447
Cdd:COG3883   170 KAELEAQQ------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 152-504 4.45e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.27  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   152 DSQRLKLLREVagtrvydERKEESISLMKETE--------GKREKINELLKYIEERlhTLEEEK-EELAQYQKWDKMRRA 222
Cdd:pfam15921  376 DDQLQKLLADL-------HKREKELSLEKEQNkrlwdrdtGNSITIDHLRRELDDR--NMEVQRlEALLKAMKSECQGQM 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   223 LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15921  447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA---SLQEKERAIEATNAEITKLR 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   303 TKLELKAKDLQdELAGNSEQRKRLLKERQKLLEKIEEKQKElaetepkfnsvkekeergIARLAQATQERTDLYAKQGR- 381
Cdd:pfam15921  524 SRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKV------------------IEILRQQIENMTQLVGQHGRt 584

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   382 -GSQFTSKEERDKWIK------KELKSLDQAINDKKRQIAAIHKDLE------------------DTEANKEKNLEQYNK 436
Cdd:pfam15921  585 aGAMQVEKAQLEKEINdrrlelQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlravkDIKQERDQLLNEVKT 664

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   437 LDQDLNEVKARVEELDRKY---------------YEVKNKKDELQSERNYLWREENAE----------QQALAAKR---E 488
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFrnkseemetttnklkMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAKRgqiD 744

                          410
                   ....*....|....*.
gi 158517902   489 DLEKKQQLLRAATGKA 504
Cdd:pfam15921  745 ALQSKIQFLEEAMTNA 760
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 178-492 5.05e-06

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: 50.79  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   178 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKwDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:TIGR04523  312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:TIGR04523  391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   338 EEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQgrgSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIH 417
Cdd:TIGR04523  471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV---KDLTKKISS---LKEKIEKLESEKKEKESKISDLE 544

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158517902   418 KDLE--DTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEK 492
Cdd:TIGR04523  545 DELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
PTZ00121 PTZ00121
MAEBL; Provisional
 143-470 5.08e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  143 KINQMATAPDSQRLKLLREVAGTRVYDE-RKEESISLMKETEGKREKINEllkyiEERLHTLEEEKEELAQYQKwdkmRR 221
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEE----AR 1593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  222 ALEYTIYNQELNETRAkldELSAKRETSGEKSRQLRDAQQDaRDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQ 301
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKA---EEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  302 RTKLELKAKDLQDELAGNSEQRKRLLKERQKLlEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyakqgr 381
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---------- 1738

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  382 gsqftskEERDKWIKKELKSLDQaindKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVeELDRKYYEVKNK 461
Cdd:PTZ00121 1739 -------AEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIFDN 1806


                  ....*....
gi 158517902  462 KDELQSERN 470
Cdd:PTZ00121 1807 FANIIEGGK 1815
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 669-987 5.67e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.82  E-value: 5.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   669 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 748
Cdd:TIGR00606  205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   749 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 821
Cdd:TIGR00606  285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   822 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 898
Cdd:TIGR00606  360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   899 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 968
Cdd:TIGR00606  440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519

                          330
                   ....*....|....*....
gi 158517902   969 LEQCNTELKKYSHVNKKAL 987
Cdd:TIGR00606  520 LDQEMEQLNHHTTTRTQME 538
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 181-350 6.40e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  181 ETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQ 260
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEA-----------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  261 QDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:COG1579    83 GNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162

                         170
                  ....*....|..
gi 158517902  339 EKQKELAETEPK 350
Cdd:COG1579   163 AEREELAAKIPP 174
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 1104-1185 1.25e-05

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 49.21  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  1104 GKQGEMremqqLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESA 1183
Cdd:TIGR02857  453 GEGGAG-----LSGGQAQRLALARAF----LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523


                   ..
gi 158517902  1184 DK 1185
Cdd:TIGR02857  524 DR 525
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 1100-1165 1.60e-05

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 47.21  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902 1100 VSFtgKQGEmrEMQQL-----SGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:cd03277   111 VKF--REGE--QLQELdphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETA 177
PRK01156 PRK01156
chromosome segregation protein; Provisional
 171-499 1.60e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.51  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEK---EELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK01156  347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSkniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  248 TSGEKSRQLRDAQQDARDKM------------------EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKA 309
Cdd:PRK01156  427 SLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK 506

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  310 KDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEK---------EERGIARL-AQATQERTDLYAKQ 379
Cdd:PRK01156  507 EYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledlDSKRTSWLnALAVISLIDIETNR 586

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  380 GRGSQFTSK----EER---------------DKWIKK---ELKSLDQAIN---DKKRQIAAIHKDLEDTE---ANKEKNL 431
Cdd:PRK01156  587 SRSNEIKKQlndlESRlqeieigfpddksyiDKSIREienEANNLNNKYNeiqENKILIEKLRGKIDNYKkqiAEIDSII 666

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902  432 EQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRA 499
Cdd:PRK01156  667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 168-468 2.04e-05

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: 48.86  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   168 YDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAleytiynqELNETRAKLDELSAKRE 247
Cdd:TIGR04523  382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII--------KNNSEIKDLTNQDSVKE 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   248 TSGEKSRQLRDAQQDardKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLL 327
Cdd:TIGR04523  454 LIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   328 KERQKLLEKIEEKQKELAE--TEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTS-KEERDKWIKKELKSLDQ 404
Cdd:TIGR04523  531 SEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqKEKEKKDLIKEIEEKEK 610

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902   405 aindkkrQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 468
Cdd:TIGR04523  611 -------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 183-482 2.06e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   183 EGKREKINELLKYIEERLHTLEEEKEELAQYQKwdkMRRALEYtiynqELNETRAKLDELSAKREtsgEKSRQLRDAQ-- 260
Cdd:pfam01576  738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVA---AKKKLEL-----DLKELEAQIDAANKGRE---EAVKQLKKLQaq 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   261 --------QDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:pfam01576  807 mkdlqrelEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   333 LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQE-RTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDK-K 410
Cdd:pfam01576  887 LEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfK 966

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   411 RQIAAIHKDLEDTEANKE---KNLEQYNKL----DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWRE-ENAEQQA 482
Cdd:pfam01576  967 SSIAALEAKIAQLEEQLEqesRERQAANKLvrrtEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQlEEAEEEA 1046
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 1105-1190 2.27e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.83  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1105 KQGE-----MREMQQLSGGQKSLVALALIFAIQK--CDPAPFYLFDEIDQALDAQHRKAVSDMIMELA---VHAQFITTT 1174
Cdd:cd03240   101 HQGEsnwplLDMRGRCSGGEKVLASLIIRLALAEtfGSNCGILALDEPTTNLDEENIEESLAEIIEERksqKNFQLIVIT 180

                          90
                  ....*....|....*.
gi 158517902 1175 FRPELLESADKFYGVK 1190
Cdd:cd03240   181 HDEELVDAADHIYRVE 196
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 187-1006 2.42e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   187 EKINELLKYIEERLHtleeEKEELAQYQKWdkmrraleytIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDK 266
Cdd:pfam15921   81 EEYSHQVKDLQRRLN----ESNELHEKQKF----------YLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   267 MEDierQVRELKtkisAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDE----LAGNSEQRKRLLKER------------ 330
Cdd:pfam15921  147 LQN---TVHELE----AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsiLVDFEEASGKKIYEHdsmstmhfrslg 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   331 ---QKLLEKIEEK----QKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKK 397
Cdd:pfam15921  220 saiSKILRELDTEisylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEheveitGLTEKASSARSQANSIQS 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   398 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDlnevkaRVEELDRKYYEVKNKKDELQSERNYLWRE-- 475
Cdd:pfam15921  300 QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELTEARTERDQFSQEsg 373

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   476 --ENAEQQALA--AKRE---DLEKKQ--QLLRAATGKAIlngidsinkVLDHFRRK--GINQHVQNGYHGIVMNNFECEP 544
Cdd:pfam15921  374 nlDDQLQKLLAdlHKREkelSLEKEQnkRLWDRDTGNSI---------TIDHLRREldDRNMEVQRLEALLKAMKSECQG 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   545 AFYTCVEVTAG--------NRLFYHIVDSDEVSTKILMEFN--KMNLP-GEVTFLPLN-KLDVRDTAYPETNDAipmISK 612
Cdd:pfam15921  445 QMERQMAAIQGkneslekvSSLTAQLESTKEMLRKVVEELTakKMTLEsSERTVSDLTaSLQEKERAIEATNAE---ITK 521

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   613 LRynPRFDKAFKHvfgktlicrsmevstqlaraftMDCITLEGDQVSHrgaltggyYDTRKSRLELQkdvrkaeeelGEL 692
Cdd:pfam15921  522 LR--SRVDLKLQE----------------------LQHLKNEGDHLRN--------VQTECEALKLQ----------MAE 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   693 EAKLNENLRRNIERINNEIDQ---LMNQMQQIETQQRKFKASRDSILSEMKMLKEKrqqsektfmpKQRSLQSLEASlha 769
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDK----------KDAKIRELEAR--- 626

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   770 mestreslkaelgtdlLSQLSLEDQKRVDALNDEIR---QLQQENRQLLNE----RIKLEGIITRVETyLNENLRKRLDQ 842
Cdd:pfam15921  627 ----------------VSDLELEKVKLVNAGSERLRavkDIKQERDQLLNEvktsRNELNSLSEDYEV-LKRNFRNKSEE 689

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   843 VEQELNELRETeggtvLTATTSELEainkRVKDTMARSEDLDNSIDKTEAGikelqksMERWKNMEKEHMDAINHDTKEL 922
Cdd:pfam15921  690 METTTNKLKMQ-----LKSAQSELE----QTRNTLKSMEGSDGHAMKVAMG-------MQKQITAKRGQIDALQSKIQFL 753

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   923 EK-MTNRQGMLLKKKEECMKKIRELGSLpqeAFEKYQTLSLKQLFRKLEQcntELKKYSHVNKKALDQF-VNFSEQKEkL 1000
Cdd:pfam15921  754 EEaMTNANKEKHFLKEEKNKLSQELSTV---ATEKNKMAGELEVLRSQER---RLKEKVANMEVALDKAsLQFAECQD-I 826


                   ....*.
gi 158517902  1001 IKRQEE 1006
Cdd:pfam15921  827 IQRQEQ 832
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
242-447 2.87e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  242 LSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTK----------------ISAMKEEKEQLSAERQEQIKQRTKL 305
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAAL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  306 ELKAKDLQDELA--GNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQErtdlyAKQGRGS 383
Cdd:COG3206   246 RAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-----ILASLEA 320

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902  384 QFTSKEERDKWIKKELKSLDQAIndkkRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKAR 447
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 226-468 3.23e-05

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: 47.97  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   226 TIYNQELNETRAKLDELSAKRETSgekSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEkeqLSAERQEQikqrTKL 305
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKH----EEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   306 ELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELA-------ETEPKFNSVKEKEERGIARLAQATQERTDLYAK 378
Cdd:pfam07888  100 EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   379 qgrgsqFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT----------EANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:pfam07888  180 ------LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLtqklttahrkEAENEALLEELRSLQERLNASERKV 253

                          250       260
                   ....*....|....*....|
gi 158517902   449 EELDRKYYEVKNKKDELQSE 468
Cdd:pfam07888  254 EGLGEELSSMAAQRDRTQAE 273
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 200-495 3.24e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 3.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   200 LHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDIERQVRELKT 279
Cdd:TIGR00606  799 MELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSEKL 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   280 KISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEE 359
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVK 951

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   360 RGIAR---LAQATQERTDLYAKQ------GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKE-K 429
Cdd:TIGR00606  952 NIHGYmkdIENKIQDGKDDYLKQketelnTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENElK 1031

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902   430 NLEQYNK-LDQDLNEVkaRVEELDRKYYEVKNKKDELQSERNYLW-REENAEQQALAAKREDLEKKQQ 495
Cdd:TIGR00606 1032 EVEEELKqHLKEMGQM--QVLQMKQEHQKLEENIDLIKRNHVLALgRQKGYEKEIKHFKKELREPQFR 1097
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 316-504 3.47e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftskeerdkwi 395
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNL---------------------------------------EQYNK 436
Cdd:COG4942    75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylaparrEQAEE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902  437 LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG4942   155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
PRK12704 PRK12704
phosphodiesterase; Provisional
 180-370 3.76e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  180 KETEGKREKInelLKYIEERLHTLEEEKEeLAQYQKWDKMRRALEytiynQELNETRAKLDE-----------LSAKRET 248
Cdd:PRK12704   34 KEAEEEAKRI---LEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFE-----KELRERRNELQKlekrllqkeenLDRKLEL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR--TKLELKAKdlqdelagnseqrkrl 326
Cdd:PRK12704  105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIllEKVEEEAR---------------- 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158517902  327 lKERQKLLEKIEEKQKELAetepkfnsvkEKEERGIarLAQATQ 370
Cdd:PRK12704  169 -HEAAVLIKEIEEEAKEEA----------DKKAKEI--LAQAIQ 199
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 148-415 4.83e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.74  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  148 ATAPDSQRLKL-LREVAGTRVYDERK-----EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqKWDKMRR 221
Cdd:PRK10929   20 ATAPDEKQITQeLEQAKAAKTPAQAEivealQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--ERDEPRS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  222 A---LEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDA-------QQDARDKMEDIERQVRELKTKISAmkEEKEQL 291
Cdd:PRK10929   98 VppnMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSlsqlpqqQTEARRQLNEIERRLQTLGTPNTP--LAQAQL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  292 SAERQEQIKQRTKLElkakdlQDELAGNS-EQRKRLLKERQKLLEK-IEEKQKELAETEPKFNSVKEKEergiarlAQAT 369
Cdd:PRK10929  176 TALQAESAALKALVD------ELELAQLSaNNRQELARLRSELAKKrSQQLDAYLQALRNQLNSQRQRE-------AERA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158517902  370 QERTDLYAKQGRG------SQFTSKEERDKWIKKELKSLDQaINDKKRQIAA 415
Cdd:PRK10929  243 LESTELLAEQSGDlpksivAQFKINRELSQALNQQAQRMDL-IASQQRQAAS 293
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 698-1046 5.53e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.74  E-value: 5.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 777
Cdd:TIGR01612  934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   778 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 846
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   847 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 915
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   916 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 980
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902   981 HVNKKALDQFVNFSEQKEK--LIKRQEELDRGYKSIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQK 1046
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISH-DDDKDHHIISKKHDENISDIREK 1306
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 251-428 6.03e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  251 EKSRQlRDAQQDARDKMEDI----ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRL 326
Cdd:PRK09510   78 EEQRK-KKEQQQAEELQQKQaaeqERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  327 LKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK09510  157 AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236

                         170       180
                  ....*....|....*....|..
gi 158517902  407 NDKKrqiAAIHKDLEDTEANKE 428
Cdd:PRK09510  237 AAEK---AAAAKAAEKAAAAKA 255
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 182-496 6.11e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.53  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   182 TEGKREKINELLKYIEERLHTLEEEKEELAQYQ-KWDKMRRALEYTIynQELNETRAKLDELS-AKRETSGEKSRQLRDA 259
Cdd:pfam12128  599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANgELEKASREETFAR--TALKNARLDLRRLFdEKQSEKDKKNKALAER 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   260 QQDARDKMEDIERQVRELKTKISAMKEE-KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEkiE 338
Cdd:pfam12128  677 KDSANERLNSLEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE--T 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   339 EKQKELAETEPKFNSVKeKEERGI----ARLAQATQERTDLyAKQGRGSQFTSKEERDKwIKKELKSLDQAINDKKRQIA 414
Cdd:pfam12128  755 WYKRDLASLGVDPDVIA-KLKREIrtleRKIERIAVRRQEV-LRYFDWYQETWLQRRPR-LATQLSNIERAISELQQQLA 831

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   415 AIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam12128  832 RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911


                   ..
gi 158517902   495 QL 496
Cdd:pfam12128  912 YV 913
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 238-359 7.39e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  238 KLDELSAKREtsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKlELKA------KD 311
Cdd:PRK00409  517 KLNELIASLE---ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIK-EAKKeadeiiKE 592

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 158517902  312 L-QDELAGNSEQRKRLLKERQKLL-EKIEEKQKELAETEPKFNSVKEKEE 359
Cdd:PRK00409  593 LrQLQKGGYASVKAHELIEARKRLnKANEKKEKKKKKQKEKQEELKVGDE 642
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
254-470 9.39e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  254 RQLRDAQQDARDKMEDIERQVRELKTKISAmkeekeqlsAERQ-EQIKQRTK---LELKAKDLQDELAGNSEQRKRLLKE 329
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEE---------AEAAlEEFRQKNGlvdLSEEAKLLLQQLSELESQLAEARAE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  330 RQKLLEKIEEKQKELAETEPKFNSVKEKEE--RGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSLDQAIN 407
Cdd:COG3206   235 LAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL------SARYTPNHPDVIALRAQIAALRAQLQ 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902  408 DKKRQI-AAIHKDLEDTEANK---EKNLEQYNKLDQDLNEVKARVEELDRKY------YE-VKNKKDELQSERN 470
Cdd:COG3206   309 QEAQRIlASLEAELEALQAREaslQAQLAQLEARLAELPELEAELRRLEREVevarelYEsLLQRLEEARLAEA 382
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 1115-1187 1.48e-04

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 43.91  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902 1115 LSGGQKSLVALALIFaIQKcdpAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFY 1187
Cdd:cd03228    97 LSGGQRQRIAIARAL-LRD---PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 670-899 1.69e-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: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  670 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 749
Cdd:COG4942    45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  750 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 829
Cdd:COG4942   121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  830 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 899
Cdd:COG4942   185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 180-482 1.72e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.72  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  180 KETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETraKLDELSAKRETSGEKSRQLRDA 259
Cdd:COG5185   156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESE--TGNLGSESTLLEKAKEIINIEE 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTK-LELKAKDLQDELAgNSEQRKRLLKERQKLLEKIE 338
Cdd:COG5185   234 ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrLNENANNLIKQFE-NTKEKIAEYTKSIDIKKATE 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  339 EKQKELAETEP--KFNSVKEKEERGIARL-AQATQERTDLYAKQ-----GRGSQFTSKEERDKwiKKELKSLDQAINDKK 410
Cdd:COG5185   313 SLEEQLAAAEAeqELEESKRETETGIQNLtAEIEQGQESLTENLeaikeEIENIVGEVELSKS--SEELDSFKDTIESTK 390

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  411 RQIAAIHKDLEDTEANKEKNLEQYNKL-DQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 482
Cdd:COG5185   391 ESLDEIPQNQRGYAQEILATLEDTLKAaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
 1-100 1.75e-04

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 45.42  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902     1 MYIKQVIIQGFRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIqFVLSDEFSHlRPEQRLALLHEGTgPRvisAFVEI 80
Cdd:TIGR00611    1 MYLSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLIRFGA-EA---FVIEG 72

                           90       100
                   ....*....|....*....|
gi 158517902    81 IFDNSDNRLPIDKEEVSLRR 100
Cdd:TIGR00611   73 RVSKGDREVTIPLEGLLKKK 92
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
157-348 2.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  157 KLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETR 236
Cdd:PRK03918  529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  237 AKLDELSAKRetsgEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMK-----EEKEQLSAE----RQEQIKQRTKLEl 307
Cdd:PRK03918  609 DAEKELEREE----KELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEylelSRELAGLRAELE- 683

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158517902  308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETE 348
Cdd:PRK03918  684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 173-505 2.17e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   173 EESISLMKETEGKREKINELLkyiEERLH----TLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRET 248
Cdd:pfam01576  137 EEDILLLEDQNSKLSKERKLL---EERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   249 SGEKSrqlrdaqqDARDKMEDIERQVRELKTKISAMKEE-------KEQLSAERQEQIKQRTKLELKAKDLQDELAGNSE 321
Cdd:pfam01576  214 EGEST--------DLQEQIAELQAQIAELRAQLAKKEEElqaalarLEEETAQKNNALKKIRELEAQISELQEDLESERA 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   322 QRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKE---KEERGIARLAQATQERTDLYA------KQGRGSQFTSKEERD 392
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEaqlqemRQKHTQALEELTEQL 365

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   393 KWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSErnyl 472
Cdd:pfam01576  366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSE---- 441

                          330       340       350
                   ....*....|....*....|....*....|...
gi 158517902   473 wreenaeqqalaakredLEKKQQLLRAATGKAI 505
Cdd:pfam01576  442 -----------------LESVSSLLNEAEGKNI 457
PRK11281 PRK11281
mechanosensitive channel MscK;
173-470 2.17e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.67  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYN-----QELNETrakLDELSAKRE 247
Cdd:PRK11281   66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSlrqleSRLAQT---LDQLQNAQN 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  248 TSGEKSRQLRDAQ-QDARDKMEDIERQVR--ELKTKISAMKEEKEQLSAERQEQIK-QRTKLELKAKDLQDELAGNSEQR 323
Cdd:PRK11281  143 DLAEYNSQLVSLQtQPERAQAALYANSQRlqQIRNLLKGGKVGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTQLQ 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  324 KRLLKERQKLLEKIEEKQKELAETEpkfNSVKEKeergiaRLAQATQErtdlyAKQGRGSQFTSKEERDKWIKKELksld 403
Cdd:PRK11281  223 DLLQKQRDYLTARIQRLEHQLQLLQ---EAINSK------RLTLSEKT-----VQEAQSQDEAARIQANPLVAQEL---- 284

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902  404 qaindkkrqiaaihkdledtEANKeknleqynKLDQDLNEVKARVEELDRKYYEVKNKKDEL-QSERN 470
Cdd:PRK11281  285 --------------------EINL--------QLSQRLLKATEKLNTLTQQNLRVKNWLDRLtQSERN 324
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
 11-79 2.38e-04

ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213209 [Multi-domain]  Cd Length: 270  Bit Score: 44.21  E-value: 2.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158517902   11 FRSYRDQTIvdPFSSKHNVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRlALLHEGTGPRVISAFVE 79
Cdd:cd03242     9 FRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL-LATGKSHRTSRDK-ELIRWGAEEAKISAVLE 73
COG5022 COG5022
Myosin heavy chain [General function prediction only];
698-1019 2.42e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 775
Cdd:COG5022   810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  776 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 853
Cdd:COG5022   887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  854 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 920
Cdd:COG5022   963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  921 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 993
Cdd:COG5022  1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120

                         330       340
                  ....*....|....*....|....*.
gi 158517902  994 SEQKEKLIKRQEELDRGYKSIMELMN 1019
Cdd:COG5022  1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-517 2.53e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELK 308
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  309 AKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSK 388
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  389 EERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE 468
Cdd:COG4372   211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 158517902  469 RNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLD 517
Cdd:COG4372   291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 1110-1172 2.91e-04

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 43.61  E-value: 2.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQFIT 1172
Cdd:cd03225   130 RSPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKL--KAEGKT 186
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 173-495 3.10e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 44.68  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   173 EESISLMKETEGKREKINEL-----------LKYIEERlHTLEEEKEELAQYQKW-DKMR--------RALEYTIYNQEL 232
Cdd:pfam05622   28 EEKNSLQQENKKLQERLDQLesgddsgtpggKKYLLLQ-KQLEQLQEENFRLETArDDYRikceelekEVLELQHRNEEL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   233 ----NETRAKLDELSAKRETSgEKSRQLRDAQQDARDKME---DIERQVREL------------------------KTKI 281
Cdd:pfam05622  107 tslaEEAQALKDEMDILRESS-DKVKKLEATVETYKKKLEdlgDLRRQVKLLeernaeymqrtlqleeelkkanalRGQL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   282 SAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKqkelaetepKFNSVKEKEERG 361
Cdd:pfam05622  186 ETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL---------RCAQLQQAELSQ 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   362 IARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKsLDQAINDKKRqIAAIHKDLEDTEANKEKNLEQYNKLDQDL 441
Cdd:pfam05622  257 ADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR-LGQEGSYRER-LTELQQLLEDANRRKNELETQNRLANQRI 334

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   442 NEVKARVEELDRKYYEVKNKKDELQSERNYL------WREENAEQQALAAKREDLEKKQQ 495
Cdd:pfam05622  335 LELQQQVEELQKALQEQGSKAEDSSLLKQKLeehlekLHEAQSELQKKKEQIEELEPKQD 394
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 275-489 3.27e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.94  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  275 RELKTKISAMKEEKEQlsAERQeqiKQRTklelkakdlqdelagnsEQRK-RLlkERQKLlEKiEEKQKELAE--TEPKF 351
Cdd:PRK05035  432 RQAKAEIRAIEQEKKK--AEEA---KARF-----------------EARQaRL--EREKA-AR-EARHKKAAEarAAKDK 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  352 NSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKS---LDQAINDKKRQIAAihkDLEDTEANKE 428
Cdd:PRK05035  486 DAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAekqAAAAADPKKAAVAA---AIARAKAKKA 562

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902  429 KNLEQYNKLDQDLNEVKARVEELDRKyyeVKNKKDELQSErnylwREENAEQQALAAKRED 489
Cdd:PRK05035  563 AQQAANAEAEEEVDPKKAAVAAAIAR---AKAKKAAQQAA-----SAEPEEQVAEVDPKKA 615
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 151-500 3.27e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   151 PDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQ 230
Cdd:TIGR00618  274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   231 ELNETRAKLDELSAKRETSGEKS--RQLRDAQQD----------ARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ 298
Cdd:TIGR00618  354 EIHIRDAHEVATSIREISCQQHTltQHIHTLQQQkttltqklqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   299 IKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIE---------EKQKELAETEPKFNSVKEKEERGI-ARLAQA 368
Cdd:TIGR00618  434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLcGSCIHP 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   369 TQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARV 448
Cdd:TIGR00618  514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 158517902   449 EELDRKYYEVKNKKDELQSERNYLWREENAEQ--QALAAKREDLEKKQQLLRAA 500
Cdd:TIGR00618  594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlQDVRLHLQQCSQELALKLTA 647
PRK12704 PRK12704
phosphodiesterase; Provisional
 253-428 3.68e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  253 SRQLRDAQQDARDKMEDIERQVrelktkiSAMKEEKEqLSAeRQEQIKQRTKLELKAKDLQDELAGNSE---QRKRLLKE 329
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKrllQKEENLDR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  330 RQKLLEKIEEK-QKELAETEPKFNSVKEKEERgIARLAQATQERTDlyakqgRGSQFTSKEerdkwIKKELksLDQAIND 408
Cdd:PRK12704  101 KLELLEKREEElEKKEKELEQKQQELEKKEEE-LEELIEEQLQELE------RISGLTAEE-----AKEIL--LEKVEEE 166

                         170       180
                  ....*....|....*....|...
gi 158517902  409 KKRQIAAIHKDLED---TEANKE 428
Cdd:PRK12704  167 ARHEAAVLIKEIEEeakEEADKK 189
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
742-903 3.86e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  742 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 819
Cdd:COG3206   166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  820 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 888
Cdd:COG3206   244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323

                         170
                  ....*....|....*
gi 158517902  889 KTEAGIKELQKSMER 903
Cdd:COG3206   324 ALQAREASLQAQLAQ 338
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
169-491 3.87e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  169 DERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkmrralEYTIYNQELNETRAKLDELSAKRET 248
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----------ELEQLEEELEELNEQLQAAQAELAQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  249 SGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLK 328
Cdd:COG4372    99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  329 E--RQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:COG4372   179 AeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  407 NDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAK 486
Cdd:COG4372   259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338


                  ....*
gi 158517902  487 REDLE 491
Cdd:COG4372   339 LADLL 343
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 28-115 4.14e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 43.92  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    28 NVIVGRNGSGKSNFFYAIQFvLSDEFSHLRPEQRLALLHEGTG----------PRVISAFVEIIFDNSDNR----LPIDK 93
Cdd:pfam13304    2 NVLIGPNGSGKSNLLEALRF-LADFDALVIGLTDERSRNGGIGgipsllngidPKEPIEFEISEFLEDGVRyrygLDLER 80

                           90       100
                   ....*....|....*....|....
gi 158517902    94 EEVS--LRRVIGAKKDQYFLDKKM 115
Cdd:pfam13304   81 EDVEekLSSKPTLLEKRLLLREDS 104
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 1110-1171 4.77e-04

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 43.51  E-value: 4.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158517902 1110 REMQQLSGGQKSLVALAlIFAIQKCDpapFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFI 1171
Cdd:cd03236   135 RNIDQLSGGELQRVAIA-AALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 165-495 5.22e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   165 TRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAqyqkwDKMRRAleytiyNQELNETRAKLDELSA 244
Cdd:TIGR00606  704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKV------NRDIQRLKNDIEEQET 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   245 KRETSGEKSRQLRDAQQDArDKMEDIERQVRELKTKIsamkeekEQLSAERQEqikqrTKLELKAKDLQDELAGNSEQRK 324
Cdd:TIGR00606  773 LLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKI-------AQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELD 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiARLAQATQERTDLyakqgrgsqftskEERDKWIKKELKSLDQ 404
Cdd:TIGR00606  840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK----LQIGTNLQRRQQF-------------EEQLVELSTEVQSLIR 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   405 AINDKKRQIAAIHKDLEDTEANKEKNL---EQYNKLDQDlnEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQ 481
Cdd:TIGR00606  903 EIKDAKEQDSPLETFLEKDQQEKEELIsskETSNKKAQD--KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN 980

                          330
                   ....*....|....
gi 158517902   482 ALAAKREDLEKKQQ 495
Cdd:TIGR00606  981 TVNAQLEECEKHQE 994
mukB PRK04863
chromosome partition protein MukB;
207-485 5.35e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  207 KEELAQYQKWDKMRRALEYTiyNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKM---EDIERQVRELKtKISA 283
Cdd:PRK04863  286 EEALELRRELYTSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLE-ELEE 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  284 MKEEKEQLSAERQEQIKQR----TKLELKAKDLQDELA----GNSEQRKRLLKERQ--KLLEKIEEkQKELAETEPKfnS 353
Cdd:PRK04863  363 RLEEQNEVVEEADEQQEENearaEAAEEEVDELKSQLAdyqqALDVQQTRAIQYQQavQALERAKQ-LCGLPDLTAD--N 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  354 VKEKEERGIARLAQATQERTDLYAK----QGRGSQFT-------------SKEERDKWIKKELKSL--DQAINDKKRQIA 414
Cdd:PRK04863  440 AEDWLEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEqayqlvrkiagevSRSEAWDVARELLRRLreQRHLAEQLQQLR 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  415 AIHKDLE---DTEANKEKNLEQYNK------------------LDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLW 473
Cdd:PRK04863  520 MRLSELEqrlRQQQRAERLLAEFCKrlgknlddedeleqlqeeLEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599

                         330
                  ....*....|..
gi 158517902  474 REENAEQQALAA 485
Cdd:PRK04863  600 ARAPAWLAAQDA 611
PRK12704 PRK12704
phosphodiesterase; Provisional
 234-379 5.60e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  234 ETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKakdlQ 313
Cdd:PRK12704   52 EAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK----Q 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902  314 DELAGNSEQRKRLLKERQKLLEKI-----EEKQKELAEtepkfnSVKEKEERGIARLAQATQERTDLYAKQ 379
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsgltaEEAKEILLE------KVEEEARHEAAVLIKEIEEEAKEEADK 188
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 111-464 6.11e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 44.27  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  111 LDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKIN 190
Cdd:PTZ00108 1026 LVITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEKVE 1105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  191 ELLKYIEERLhtleeekeelaqyQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDI 270
Cdd:PTZ00108 1106 KLNAELEKKE-------------KELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKP 1172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  271 ERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGNSEQRKRLLKERQKLLEKIEEKQKE 343
Cdd:PTZ00108 1173 KLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPdnkksnsSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  344 LAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKEERDkwikkELKSLDQAINDKKRQIAAIHKDL 420
Cdd:PTZ00108 1253 SSEDNDEFSSDDLSKEGKPKNApkrVSAVQYSPPPPSKRPDGESNGGSKPSS-----PTKKKVKKRLEGSLAALKKKKKS 1327

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 158517902  421 EDTEANKEKNLEQYNK-LDQDLNEVKAR---------VEELDRKYYEVKNKKDE 464
Cdd:PTZ00108 1328 EKKTARKKKSKTRVKQaSASQSSRLLRRprkkksdssSEDDDDSEVDDSEDEDD 1381
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1114-1185 7.26e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 43.15  E-value: 7.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158517902 1114 QLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1185
Cdd:PRK10851  136 QLSGGQKQRVALARALAVE----PQILLLDEPFGALDAQVRKELRRWLRQL--HEELkFTSVFvthdQEEAMEVADR 206
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 388-482 7.82e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 42.63  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  388 KEERDKWIKkELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELdRKYYEVKNKKDElQS 467
Cdd:cd07653   104 RQERKKHLS-EGSKLQQKLESSIKQLEKSKKAYEKAFKEAEKAKQKYEKADADMNLTKADVEKA-KANANLKTQAAE-EA 180

                          90
                  ....*....|....*..
gi 158517902  468 ERNY--LWREENAEQQA 482
Cdd:cd07653   181 KNEYaaQLQKFNKEQRQ 197
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 281-504 8.19e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 44.05  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  281 ISAMKEEKEQLSAERqEQIKQRtklELKAKDLQDElAGNSEQRKRLLKERQKLLEKIEEKQKELAETEP-KFNSVKEKEE 359
Cdd:NF012221 1534 VVATSESSQQADAVS-KHAKQD---DAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQnALETNGQAQR 1608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  360 RGIARLAQA-TQERTDLyaKQG----RGSQFTSKEERDKW--------IKKELKSLDQA-------INDKKRQIAAIHKD 419
Cdd:NF012221 1609 DAILEESRAvTKELTTL--AQGldalDSQATYAGESGDQWrnpfagglLDRVQEQLDDAkkisgkqLADAKQRHVDNQQK 1686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  420 LEDTEANKEKNLEQ--YNKLDQDLNEVKARVeeldrkyyEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLL 497
Cdd:NF012221 1687 VKDAVAKSEAGVAQgeQNQANAEQDIDDAKA--------DAEKRKDDALAKQN---EAQQAESDANAAANDAQSRGEQDA 1755


                  ....*..
gi 158517902  498 RAATGKA 504
Cdd:NF012221 1756 SAAENKA 1762
mukB PRK04863
chromosome partition protein MukB;
187-457 8.23e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  187 EKINELLKYIEERLHTLEEEkeELAQYQKWDKMRRALeytiynQELNETRAKLDELsaKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK04863  840 RQLNRRRVELERALADHESQ--EQQQRSQLEQAKEGL------SALNRLLPRLNLL--ADETLADRVEEIREQLDEAEEA 909

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  267 MEDIERQ---VRELKTKISAMKEEKEQLSAERQ--EQIKQRTKLELKAKDLQDELAGNS-----EQRKRLLKERQKLLEK 336
Cdd:PRK04863  910 KRFVQQHgnaLAQLEPIVSVLQSDPEQFEQLKQdyQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK 989

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  337 IEEKQKElAETEPkfNSVKEKEERGIARLAQATQERTDLyakqgrGSQFTSKEERDKWIKKELKSL---------DQAIN 407
Cdd:PRK04863  990 LRQRLEQ-AEQER--TRAREQLRQAQAQLAQYNQVLASL------KSSYDAKRQMLQELKQELQDLgvpadsgaeERARA 1060

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 158517902  408 DKKRqiaaIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYE 457
Cdd:PRK04863 1061 RRDE----LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHE 1106
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 395-503 8.81e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKD--ELQSERNYL 472
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyeALQKEIESL 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 158517902  473 WREENAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:COG1579   102 KRRISDLEDEILELMERIEELEEELAELEAE 132
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
171-342 9.12e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  171 RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKM-RRALEYTIYNQELNETRAKLDELSAK---- 245
Cdd:COG3206   203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgPDALPELLQSPVIQQLRAQLAELEAElael 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  246 RETSGEKS---RQLRDAQQDARDKMED-IERQVRELKTKISAMKEEKEQLSAERQE---QIKQRTKLELKAKDLQDELAG 318
Cdd:COG3206   283 SARYTPNHpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEV 362

                         170       180
                  ....*....|....*....|....
gi 158517902  319 NSEQRKRLLKERQKLleKIEEKQK 342
Cdd:COG3206   363 ARELYESLLQRLEEA--RLAEALT 384
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 717-889 1.04e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  717 QMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKR 796
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  797 VDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELEAINKRVKDT 876
Cdd:COG1579    91 YEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELAELEAELEEL 161

                         170
                  ....*....|...
gi 158517902  877 MARSEDLDNSIDK 889
Cdd:COG1579   162 EAEREELAAKIPP 174
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 232-469 1.06e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.17  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   232 LNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKE-------QLSAERQEQIKQRTK 304
Cdd:pfam05483  263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNK 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSvkEKEERgiarlaqatqertdlyakqgrgSQ 384
Cdd:pfam05483  343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS--ELEEM----------------------TK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   385 FTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLnEVKARVEELDRKYY--EVKNKK 462
Cdd:pfam05483  399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL-EIQLTAIKTSEEHYlkEVEDLK 477


                   ....*..
gi 158517902   463 DELQSER 469
Cdd:pfam05483  478 TELEKEK 484
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 180-1009 1.06e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   180 KETEGKREKINELLKYIEErLHTLEEEKEELAQYQKWDKMRRALeYTIYNQELNETRAKLdelsAKRETSGEKSRQLRDA 259
Cdd:TIGR00606  169 KALKQKFDEIFSATRYIKA-LETLRQVRQTQGQKVQEHQMELKY-LKQYKEKACEIRDQI----TSKEAQLESSREIVKS 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   260 QQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDL----QDELAGNSEQRKRLLKERQKLLE 335
Cdd:TIGR00606  243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELV 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   336 KIEEKQKELAETEPKFNSVKEKEERGIARL---AQATQERTDLYAKQGRGSQFTSKE---ERDKWIKKELKS----LDQA 405
Cdd:TIGR00606  323 DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqADRHQEHIRARDSLIQSLATRLELdgfERGPFSERQIKNfhtlVIER 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   406 INDKKRQIAAIHKDLEDTEANKEKNLEQY-NKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALA 484
Cdd:TIGR00606  403 QEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   485 AKReDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFEcepafytcvevtagnRLFYHIVD 564
Cdd:TIGR00606  483 AER-ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---------------MLTKDKMD 546

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   565 SDEVSTKILMEfNKMNLPGEVTFLPlNKLDVRDTAYPETNDAIPM---ISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQ 641
Cdd:TIGR00606  547 KDEQIRKIKSR-HSDELTSLLGYFP-NKKQLEDWLHSKSKEINQTrdrLAKLNKELASLEQNKNHINNELESKEEQLSSY 624

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   642 LARAF----------TMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEI 711
Cdd:TIGR00606  625 EDKLFdvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   712 DQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSL 791
Cdd:TIGR00606  705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   792 ED-QKRVDALNDEIRQLQQENRQLLNERIKLEGI-ITRVETYLN---ENLRKRLDQVEQELNELR-----ETEGGTVLTA 861
Cdd:TIGR00606  785 KVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNqekQEKQHELDTVVSKIELNRkliqdQQEQIQHLKS 864

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   862 TTSELEAINKRVKDTMARSEDLDnsiDKTEAGIKELQKSMERWKNMEKEhmdaINHDTKELEKMTNRQGMLLKKKEECMK 941
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRRQQFE---EQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEKDQQEKEELISSKETSNK 937

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902   942 KIRELGSLPQEAFeKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDR 1009
Cdd:TIGR00606  938 KAQDKVNDIKEKV-KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 173-499 1.06e-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: 43.47  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   173 EESISLMKETEGKREKINELlkyiEERLHTLEEEKEELAQYQKWDKMrralEYTIYNQELNETRAKLDELSAKRETSGEK 252
Cdd:TIGR04523  103 SDLSKINSEIKNDKEQKNKL----EVELNKLEKQKKENKKNIDKFLT----EIKKKEKELEKLNNKYNDLKKQKEELENE 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   253 SRQLRDAQQDARDKMEDIERQV-----------------RELKTKISAMKEEKEQLSaerqeqiKQRTKLELKAKDLQDE 315
Cdd:TIGR04523  175 LNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknKSLESQISELKKQNNQLK-------DNIEKKQQEINEKTTE 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   316 LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRgSQFTSKEERDKWI 395
Cdd:TIGR04523  248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-SELKNQEKKLEEI 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   396 KKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSE-RNYLWR 474
Cdd:TIGR04523  327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiQNQEKL 406

                          330       340
                   ....*....|....*....|....*..
gi 158517902   475 EENAEQQ--ALAAKREDLEKKQQLLRA 499
Cdd:TIGR04523  407 NQQKDEQikKLQQEKELLEKEIERLKE 433
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 229-357 1.07e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.40  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   229 NQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSA---ERQEQIKQRTKL 305
Cdd:pfam06008   53 AQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSsdlSRMLAEAQRMLG 132

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 158517902   306 ELKAKDLQDELAGNSEQrkrlLKERQKLLEKIEEKQKEL-AETEPKFNSVKEK 357
Cdd:pfam06008  133 EIRSRDFGTQLQNAEAE----LKAAQDLLSRIQTWFQSPqEENKALANALRDS 181
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 158-347 1.09e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.92  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   158 LLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKW-DKMRRALE------------ 224
Cdd:pfam06160  279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELERVRGLEKQlEELEKRYDeiverleekeva 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   225 YTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKIsamkeEKEQLSAERQEQIKQRTK 304
Cdd:pfam06160  359 YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV-----EKSNLPGLPESYLDYFFD 433

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 158517902   305 LELKAKDLQDELAG---NSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam06160  434 VSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
362-499 1.15e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  362 IARLAQATqerTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHK--DLEDTEANKEKNLEQYNKLDQ 439
Cdd:COG3206   150 AAAVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELES 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  440 DLNEVKARVEELDRKYYEVKNKKDELQSERNYLwrEENAEQQALAAKREDLEKKQQLLRA 499
Cdd:COG3206   227 QLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEAELAELSA 284
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 325-506 1.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  325 RLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLyakqgrgsqftsKEERDKwIKKELKSLDQ 404
Cdd:COG1579     7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL------------EKEIKR-LELEIEEVEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  405 AINDKKRQIAAI--HKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQA 482
Cdd:COG1579    74 RIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153

                         170       180
                  ....*....|....*....|....
gi 158517902  483 LAAKREDLEKKQQLLRAATGKAIL 506
Cdd:COG1579   154 LEAELEELEAEREELAAKIPPELL 177
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 359-509 1.44e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 42.41  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   359 ERGIARLAQATQERTDLYAKQGR-----GSQFTSKEERDKwIKKELKSLDQAINDKKRQIAAIHKDLEDTEA-------N 426
Cdd:pfam00529   61 DSAEAQLAKAQAQVARLQAELDRlqaleSELAISRQDYDG-ATAQLRAAQAAVKAAQAQLAQAQIDLARRRVlapiggiS 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   427 KEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNylwREENAEQQALAAKREDLEKKQQLLRAATGKAIL 506
Cdd:pfam00529  140 RESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR---SELSGAQLQIAEAEAELKLAKLDLERTEIRAPV 216


                   ...
gi 158517902   507 NGI 509
Cdd:pfam00529  217 DGT 219
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 700-1032 1.48e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   700 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 779
Cdd:pfam15921  262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   780 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 856
Cdd:pfam15921  338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   857 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 936
Cdd:pfam15921  412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   937 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGY 1011
Cdd:pfam15921  475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554

                          330       340
                   ....*....|....*....|.
gi 158517902  1012 KSIMELMNVLELRKYEAIQLT 1032
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMT 575
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 227-352 1.56e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 41.07  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   227 IYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQ--IKQRTK 304
Cdd:pfam06391   58 TNGIDVEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEKAKQelIDELMT 137

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 158517902   305 LELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFN 352
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFG 185
PRK00106 PRK00106
ribonuclease Y;
284-465 1.68e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 42.55  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  284 MKEEKEQ-----LSAErQEQIKQRTKLELKAkdlqdELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKE 358
Cdd:PRK00106   26 MKSAKEAaeltlLNAE-QEAVNLRGKAERDA-----EHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  359 ERGIARLAQ--ATQERTDlyakqgrgSQFTSKEerdkwikKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNK 436
Cdd:PRK00106  100 KQIESRLTEraTSLDRKD--------ENLSSKE-------KTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAA 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 158517902  437 LDQD--------------LNEVKARVEELDRkyyEVKNKKDEL 465
Cdd:PRK00106  165 LSQAeareiilaetenklTHEIATRIREAER---EVKDRSDKM 204
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 373-504 1.73e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  373 TDLYAKQGRGSQFTSKEERdkwIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELD 452
Cdd:COG3883    16 PQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902  453 RKYYEVKNKKDEL------QSERNYLWR----------------EENAEQQALAAKREDLEKKQQLLRAATGKA 504
Cdd:COG3883    93 RALYRSGGSVSYLdvllgsESFSDFLDRlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAEL 166
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 173-429 1.95e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQyqkwdkMRRALEYTI--YNQELNETRAKLDELSAKRETSG 250
Cdd:pfam05483  506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN------LRDELESVReeFIQKGDEVKCKLDKSEENARSIE 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:pfam05483  580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   331 QK-----------LLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAK--QGRGSQFTSKEERDKWIKK 397
Cdd:pfam05483  660 QKeiedkkiseekLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKiiEERDSELGLYKNKEQEQSS 739

                          250       260       270
                   ....*....|....*....|....*....|..
gi 158517902   398 ELKSLDQAINDKKRQIAAIHKDLEDTEANKEK 429
Cdd:pfam05483  740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 153-493 2.02e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   153 SQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEL-----LKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTI 227
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   228 YNQELNETRAKLDELSAKRETSgeksRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLEL 307
Cdd:TIGR00618  516 ARQDIDNPGPLTRRMQRGEQTY----AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   308 KAKDLQDELAGNSEQRKRLLKERQKLLEKIEEK-----------------QKELAETEPKFNSVKEKEERGIARLAQATQ 370
Cdd:TIGR00618  592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqdlqdvrlhlqqcsqelALKLTALHALQLTLTQERVREHALSIRVLP 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   371 ERT------DLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNE- 443
Cdd:TIGR00618  672 KELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHq 751

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   444 ----VKARVEELDRKYYEV------KNKKDELQSERNYLWREENAEQQALAAKREDLEKK 493
Cdd:TIGR00618  752 artvLKARTEAHFNNNEEVtaalqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 186-491 2.06e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 41.98  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   186 REKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRAlEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD 265
Cdd:pfam19220   26 KADFSQLIEPIEAILRELPQAKSRLLELEALLAQERA-AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEA 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   266 KMEDIERQVRELKTKISA----MKEEKEQLSAERQEQIKQRTKLELKAKDLQD---ELAGNSEQRKRLLKERQKLLEKIE 338
Cdd:pfam19220  105 AKEELRIELRDKTAQAEAlerqLAAETEQNRALEEENKALREEAQAAEKALQRaegELATARERLALLEQENRRLQALSE 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   339 EKQKELAETEPKfnsVKEKEERGIARLAQATQERTDLYAKQ-GRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIH 417
Cdd:pfam19220  185 EQAAELAELTRR---LAELETQLDATRARLRALEGQLAAEQaERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATE 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   418 KDLEDTEANKEKNLEQYNKLDQDLNE-------VKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDL 490
Cdd:pfam19220  262 QLLAEARNQLRDRDEAIRAAERRLKEasierdtLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAL 341


                   .
gi 158517902   491 E 491
Cdd:pfam19220  342 E 342
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
703-948 2.14e-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: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  703 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 782
Cdd:COG4913   226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  783 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 862
Cdd:COG4913   290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  863 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 942
Cdd:COG4913   353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427


                  ....*.
gi 158517902  943 IRELGS 948
Cdd:COG4913   428 IASLER 433
PTZ00121 PTZ00121
MAEBL; Provisional
 222-495 2.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  222 ALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARD--KMEDIERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  300 KQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLE--KIEEKQKelAETEPKFNSVKEKEErgiARLAQATQErtdlyA 377
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDarKAEAARK--AEEERKAEEARKAED---AKKAEAVKK-----A 1232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  378 KQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQ-DLNEVKARVEELDRKYY 456
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAE 1312

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 158517902  457 EvKNKKDELQSernylwREENAEQQALAAKREDLEKKQQ 495
Cdd:PTZ00121 1313 E-AKKADEAKK------KAEEAKKKADAAKKKAEEAKKA 1344
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 697-945 2.51e-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: 41.93  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   697 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 776
Cdd:TIGR04523  386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   777 LKAELGTDLLS----QLSLEDQKR--------VDALNDEIRQLQQENRQL------LNERI-KLEGIITRVETYL----- 832
Cdd:TIGR04523  466 LETQLKVLSRSinkiKQNLEQKQKelkskekeLKKLNEEKKELEEKVKDLtkkissLKEKIeKLESEKKEKESKIsdled 545

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   833 ----------NENLRKRLDQVEQELNELRETEggTVLTATTSELEainKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 902
Cdd:TIGR04523  546 elnkddfelkKENLEKEIDEKNKEIEELKQTQ--KSLKKKQEEKQ---ELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 158517902   903 rwkNMEKEHMDaINHDTKELEKMTNRQGMLLKKKEECMKKIRE 945
Cdd:TIGR04523  621 ---KAKKENEK-LSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
PTZ00121 PTZ00121
MAEBL; Provisional
 185-504 2.54e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  185 KREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDAR 264
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  265 DKMEDIERQVRELKtKISAmkeekeqlsAERQEQIKQRTKLElKAKDlqdelAGNSEQRKRLLKERqklleKIEEKQKel 344
Cdd:PTZ00121 1163 ARKAEEARKAEDAK-KAEA---------ARKAEEVRKAEELR-KAED-----ARKAEAARKAEEER-----KAEEARK-- 1219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  345 AETEPKFNSVKEKEE--RGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKElksldqaindKKRQIAAIHKDLED 422
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE----------EARKADELKKAEEK 1289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  423 TEANKEKNLEQYNKLDQ--DLNEVKARVEELDRKYYEVKNKKDELQSernylwREENAEQQALAAKREDlEKKQQLLRAA 500
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEakKKAEEAKKADEAKKKAEEAKKKADAAKK------KAEEAKKAAEAAKAEA-EAAADEAEAA 1362


                  ....
gi 158517902  501 TGKA 504
Cdd:PTZ00121 1363 EEKA 1366
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 183-503 2.84e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   183 EGKREKINELLKyiEERLHTLE-EEKEELAQYQKWDKMRRALEYTiynQELNETRAKLDELSAKRETSGEKSRQLRDAQQ 261
Cdd:pfam01576  600 EKKQKKFDQMLA--EEKAISARyAEERDRAEAEAREKETRALSLA---RALEEALEAKEELERTNKQLRAEMEDLVSSKD 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   262 DARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLE-----LKA---KDLQDELAGNSEQRKRLLKERQKL 333
Cdd:pfam01576  675 DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqaLKAqfeRDLQARDEQGEEKRRQLVKQVREL 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   334 LEKIEEKQK--------------ELAETEPKFNSVKEKEERGIARLAQATQERTDLY-----AKQGRGSQFTSKEERDKW 394
Cdd:pfam01576  755 EAELEDERKqraqavaakkklelDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQreleeARASRDEILAQSKESEKK 834

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   395 IKKELKSLDQAIND------KKRQIAAIHKDLEDTEAN--KEKNLEQYNK---------LDQDLNEVKARVEELDRKY-- 455
Cdd:pfam01576  835 LKNLEAELLQLQEDlaaserARRQAQQERDELADEIASgaSGKSALQDEKrrleariaqLEEELEEEQSNTELLNDRLrk 914

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 158517902   456 --YEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGK 503
Cdd:pfam01576  915 stLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSK 964
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 179-531 2.93e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   179 MKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiynQELNETRAKLDELSAKRETSGEKSRQLRD 258
Cdd:TIGR00606  600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK-----EEIEKSSKQRAMLAGATAVYSQFITQLTD 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   259 --------AQQDARDKMEdIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKER 330
Cdd:TIGR00606  675 enqsccpvCQRVFQTEAE-LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   331 QKLLEKIEEKQKELAETEPKFNSVKEKEERG---------IARLAQATQERTDLYAKQGRGSQFTSkeerdkwIKKELKS 401
Cdd:TIGR00606  754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtiMERFQMELKDVERKIAQQAAKLQGSD-------LDRTVQQ 826

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   402 LDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVK--------------ARVEELDRKYYEVKNKKDELQS 467
Cdd:TIGR00606  827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKseklqigtnlqrrqQFEEQLVELSTEVQSLIREIKD 906

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158517902   468 ERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKailngIDSINKVLD--HFRRKGINQHVQNG 531
Cdd:TIGR00606  907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDK-----VNDIKEKVKniHGYMKDIENKIQDG 967
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 1114-1185 2.93e-03

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 40.79  E-value: 2.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158517902 1114 QLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMELavHAQF-ITTTF----RPELLESADK 1185
Cdd:cd03296   136 QLSGGQRQRVALARALAV---EPK-VLLLDEPFGALDAKVRKELRRWLRRL--HDELhVTTVFvthdQEEALEVADR 206
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1110-1186 3.28e-03

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 40.15  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDQALDAQHRKAVSDMIMElavHAQ----FITTTFRPELLESADK 1185
Cdd:COG4133   127 LPVRQLSAGQKRRVALARLLLS----PAPLWLLDEPFTALDAAGVALLAELIAA---HLArggaVLLTTHQPLELAAARV 199


                  .
gi 158517902 1186 F 1186
Cdd:COG4133   200 L 200
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 735-969 3.38e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   735 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 810
Cdd:pfam17380  277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   811 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAInkRVKDTMARS 880
Cdd:pfam17380  357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQI--RAEQEEARQ 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   881 EDLDNSIDKTEAGIKEL-QKSMERWKNMEKEHMDAINHDTKELEKmtNRQGMLLKKKEECMKKIRElgslpQEAFEKYQT 959
Cdd:pfam17380  435 REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLEL--EKEKRDRKRAEEQRRKILE-----KELEERKQA 507

                          250
                   ....*....|
gi 158517902   960 LSLKQLFRKL 969
Cdd:pfam17380  508 MIEEERKRKL 517
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 1113-1185 3.42e-03

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 41.74  E-value: 3.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517902 1113 QQLSGGQKSLVALA--LIfaiqkCDPaPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADK 1185
Cdd:COG2274   610 SNLSGGQRQRLAIAraLL-----RNP-RILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-499 3.50e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  169 DERKEESISLMKETEGKREKINE---LLKYIEERLHTLEEEKEELAQ-YQKW-DKMRRALEYTIYNQELNETRAKLDELS 243
Cdd:COG3096   281 RELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQdYQAAsDHLNLVQTALRQQEKIERYQEDLEELT 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  244 AKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisamkeekeQLsAERQEqikqrtklelkAKDLQDELAGNSEQR 323
Cdd:COG3096   361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS----------QL-ADYQQ-----------ALDVQQTRAIQYQQA 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  324 KRLLKERQKLLekieekqkELAETEPKfnSVKEKEERGIARLAQATQERTDLYAK----QGRGSQF-------------T 386
Cdd:COG3096   419 VQALEKARALC--------GLPDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKlsvaDAARRQFekayelvckiageV 488

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  387 SKEERDKWIKKELKSL--DQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDE 464
Cdd:COG3096   489 ERSQAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 158517902  465 LQSERnylwREENAEQQALAAKREDLEKKQQLLRA 499
Cdd:COG3096   569 LEEQA----AEAVEQRSELRQQLEQLRARIKELAA 599
PRK12704 PRK12704
phosphodiesterase; Provisional
 278-482 3.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  278 KTKISAMKEEKEQLSAERQEQIKQRTKLELkakdlqdelagnSEQRKRLLKERQKLLEKIEEKQKELAETEpkfNSVKEK 357
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL------------LEAKEEIHKLRNEFEKELRERRNELQKLE---KRLLQK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  358 EErgiarlaqatqertdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKL 437
Cdd:PRK12704   95 EE------------------------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158517902  438 DQDlnEVKARVeeldrkyyeVKNKKDELQSERNYLWR--EENAEQQA 482
Cdd:PRK12704  151 TAE--EAKEIL---------LEKVEEEARHEAAVLIKeiEEEAKEEA 186
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1110-1164 3.68e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 40.74  E-value: 3.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIqkcDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1164
Cdd:PRK13632  138 KEPQNLSGGQKQRVAIASVLAL---NPE-IIIFDESTSMLDPKGKREIKKIMVDL 188
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
270-414 3.78e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  270 IERQVRELKTKISAMKEEKEQLSAERQEQikQRTKLELKAKDLQDELagnseqrKRLLKERQKLLEKIEEKQKELAETEP 349
Cdd:COG2433   378 IEEALEELIEKELPEEEPEAEREKEHEER--ELTEEEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIERLER 448

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158517902  350 KFNSVKEKEERGIARlaqatqERtdlyakqgrgsQFTSKEERDKWIKKELKSLDQAINDKKRQIA 414
Cdd:COG2433   449 ELSEARSEERREIRK------DR-----------EISRLDREIERLERELEEERERIEELKRKLE 496
COG5022 COG5022
Myosin heavy chain [General function prediction only];
171-360 3.86e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  171 RKEESISLMKETEGKREKINELLKYIEERlhtlEEEKEELAQYQKWDKMrraleytiynQELNETRAKLDELSAKRETSG 250
Cdd:COG5022   912 KKSLSSDLIENLEFKTELIARLKKLLNNI----DLEEGPSIEYVKLPEL----------NKLHEVESKLKETSEEYEDLL 977

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  251 EKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQE---------QIKQRTKLELKAKDLQdELAGNSE 321
Cdd:COG5022   978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaelqsaskIISSESTELSILKPLQ-KLKGLLL 1056

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158517902  322 QRKRLLKER------QKLLEKIEEKQKELAE-TEPKFNSVKEKEER 360
Cdd:COG5022  1057 LENNQLQARykalklRRENSLLDDKQLYQLEsTENLLKTINVKDLE 1102
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 1115-1187 4.04e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 40.15  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902 1115 LSGGQKSLVALALifAI-QKCDpapFYLFDEIDQALDAQhrkaVSDMIME------LAVHAQFITTTFRPELLESADKFY 1187
Cdd:cd03250   128 LSGGQKQRISLAR--AVySDAD---IYLLDDPLSAVDAH----VGRHIFEncilglLLNNKTRILVTHQLQLLPHADQIV 198
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 275-516 4.50e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 41.30  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   275 RELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELA-----GNSEQRKRLLKERQKLLEKIEEKQKELaetEP 349
Cdd:pfam18971  559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAeakstGNYDEVKKAQKDLEKSLRKREHLEKEV---EK 635

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   350 KFNSVKEKEERGIARlAQATQERTDLYAKQGRGSqftSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDT--EANK 427
Cdd:pfam18971  636 KLESKSGNKNKMEAK-AQANSQKDEIFALINKEA---NRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSfdEFKN 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   428 EKNlEQYNKLDQDLNEVKARVEELDRKyYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQllRAATGKAILN 507
Cdd:pfam18971  712 GKN-KDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVK--DVIINQKVTD 787


                   ....*....
gi 158517902   508 GIDSINKVL 516
Cdd:pfam18971  788 KVDNLNQAV 796
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 698-1047 4.62e-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: 41.16  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   698 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTresl 777
Cdd:TIGR04523  183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ---- 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   778 kaelgtdlLSQLSLEDQKRVDALNDEIRQLQQENRQLlneriklegiitrvetylnENLRKRLDQVEQELNELRETEGGT 857
Cdd:TIGR04523  255 --------LNQLKDEQNKIKKQLSEKQKELEQNNKKI-------------------KELEKQLNQLKSEISDLNNQKEQD 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   858 VLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKE 937
Cdd:TIGR04523  308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   938 ECMKKIRELGSLPQEAFEKYQTL-----SLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKrqeELDRGYK 1012
Cdd:TIGR04523  388 NLESQINDLESKIQNQEKLNQQKdeqikKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRE 464

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 158517902  1013 SIMELMNVLElRKYEAIQLTFKQVSKNFSEVFQKL 1047
Cdd:TIGR04523  465 SLETQLKVLS-RSINKIKQNLEQKQKELKSKEKEL 498
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 268-433 5.04e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.76  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   268 EDIERQVrELKTKISAMKEEKEQLSAERQEQIKQrtklELKAKdlQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAET 347
Cdd:pfam05262  188 EDNEKGV-NFRRDMTDLKERESQEDAKRAQQLKE----ELDKK--QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   348 EPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKrqiAAIHKDLEDTEANK 427
Cdd:pfam05262  261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKE---LEAQKKREPVAEDL 337


                   ....*.
gi 158517902   428 EKNLEQ 433
Cdd:pfam05262  338 QKTKPQ 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 792-1006 5.19e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  792 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 871
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  872 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 947
Cdd:COG4942    98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158517902  948 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKEKLIKRQEE 1006
Cdd:COG4942   178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
PRK00106 PRK00106
ribonuclease Y;
215-406 5.36e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.01  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  215 KWDKMRRALEYTIYNQELN--------ETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVR----ELKTKIS 282
Cdd:PRK00106   25 KMKSAKEAAELTLLNAEQEavnlrgkaERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKserqELKQIES 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  283 AMKEEKEQLSAERQEQIKQRTKLELKAKDLQDelagnseqRKRLLKERQKLLEKIEEKQKELAEtepKFNSVKEKEERGI 362
Cdd:PRK00106  105 RLTERATSLDRKDENLSSKEKTLESKEQSLTD--------KSKHIDEREEQVEKLEEQKKAELE---RVAALSQAEAREI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158517902  363 ArLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAI 406
Cdd:PRK00106  174 I-LAETENKLTHEIATRIREAEREVKDRSDKMAKDLLAQAMQRL 216
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 155-373 5.37e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  155 RLKLLREVAGTRVYDE---RKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELaqyqkwDKMRRALEYtiynqe 231
Cdd:PRK05771   61 KLRSYLPKLNPLREEKkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL------EQEIERLEP------ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  232 LNETRAKLDELSAKRETSGEKSRqlRDAQQDARDKMEDIERQVRELKTK-------ISAMKEEKEQLSAERQEQIKQRTK 304
Cdd:PRK05771  129 WGNFDLDLSLLLGFKYVSVFVGT--VPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLE 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  305 LELKaKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAE----TEPKFNSVKEKEErgiARLAQATQERT 373
Cdd:PRK05771  207 LEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERAE---ALSKFLKTDKT 275
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 173-504 5.42e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   173 EESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALeytiyNQELNETRAKLdelsakretsgek 252
Cdd:TIGR00606  234 ESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD-----NSELELKMEKV------------- 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   253 srqLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQK 332
Cdd:TIGR00606  296 ---FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   333 LLEKIEEKQKE---LAETEPKfNSVKEKEERGIARLAQATQERTDLYAKQG-RGSQFTSKEERDKWIKKELKSLDQAIND 408
Cdd:TIGR00606  373 LATRLELDGFErgpFSERQIK-NFHTLVIERQEDEAKTAAQLCADLQSKERlKQEQADEIRDEKKGLGRTIELKKEILEK 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   409 KKRQIAAIHKDLEDTEANKEKNLEqynkLDQDLNEVKARVEELDRKYYEVKNKKDE--LQSERNYLWREENAEQQALAAK 486
Cdd:TIGR00606  452 KQEELKFVIKELQQLEGSSDRILE----LDQELRKAERELSKAEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQL 527

                          330
                   ....*....|....*...
gi 158517902   487 REDLEKKQQLLRAATGKA 504
Cdd:TIGR00606  528 NHHTTTRTQMEMLTKDKM 545
46 PHA02562
endonuclease subunit; Provisional
 167-364 5.44e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  167 VYDERKEESISLMKETEGKREKINELLKYIEERLHTLEE-------EKEELAQYQKWDKM-RRALEYTIYNQELNETRAK 238
Cdd:PHA02562  221 KYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakIKSKIEQFQKVIKMyEKGGVCPTCTQQISEGPDR 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  239 LDELSAKRETSGEKSRQLrdaqQDARDKMEDIERQVRELKTKISAMkeeKEQLSAERQeqikQRTKLELKAKDLQDELag 318
Cdd:PHA02562  301 ITKIKDKLKELQHSLEKL----DTAIDELEEIMDEFNEQSKKLLEL---KNKISTNKQ----SLITLVDKAKKVKAAI-- 367

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 158517902  319 nseqrKRLLKERQKLLEKIEEKQKELAET-EPKFNSVKEKEERGIAR 364
Cdd:PHA02562  368 -----EELQAEFVDNAEELAKLQDELDKIvKTKSELVKEKYHRGIVT 409
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 697-1007 5.48e-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: 41.16  E-value: 5.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   697 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILsemKMLKEKRQQSEKTfmpkQRSLQSLEASLHAMESTRES 776
Cdd:TIGR04523  227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK---KQLSEKQKELEQN----NKKIKELEKQLNQLKSEISD 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   777 LKAELGTDLLSQlsledqkrvdaLNDEIRQLQQENRQLLNERIKLEGIITRVETYLNeNLRKRLDQVEQELNELRETegg 856
Cdd:TIGR04523  300 LNNQKEQDWNKE-----------LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-QLKKELTNSESENSEKQRE--- 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   857 tvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSM----ERWKNMEKEHmDAINHDTKELEKMTNRQGM- 931
Cdd:TIGR04523  365 --LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK-ELLEKEIERLKETIIKNNSe 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   932 ---LLKKKEECMKKIRELGSLPQEAFEKYQTLS---------LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEK 999
Cdd:TIGR04523  442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521


                   ....*...
gi 158517902  1000 LIKRQEEL 1007
Cdd:TIGR04523  522 LKEKIEKL 529
DUF4175 pfam13779
Domain of unknown function (DUF4175);
254-335 5.90e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 40.74  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   254 RQLRDAQQDARDKMED------IERQVRELKtkiSAMKEEKEQLsAERQEQIKQRTK-------LELKAKDLQD------ 314
Cdd:pfam13779  489 RRLRAAQERLSEALERgasdeeIAKLMQELR---EALDDYMQAL-AEQAQQNPQDLQqpddpnaQEMTQQDLQRmldrie 564

                           90       100
                   ....*....|....*....|...
gi 158517902   315 ELA--GNSEQRKRLLKERQKLLE 335
Cdd:pfam13779  565 ELArsGRRAEAQQMLSQLQQMLE 587
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 1113-1165 6.04e-03

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 39.55  E-value: 6.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158517902 1113 QQLSGGQKSLVALALIFAIQKcdpaPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:cd03226   125 LSLSGGQKQRLAIAAALLSGK----DLLIFDEPTSGLDYKNMERVGELIRELA 173
PTZ00121 PTZ00121
MAEBL; Provisional
 139-463 6.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  139 VKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINEllKYIEERLHTLEEEKEELAQYQKWDK 218
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEA 1712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  219 mrraleytiynqelnETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRElKTKISAMKEEKEQLSAERQEQ 298
Cdd:PTZ00121 1713 ---------------EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKE 1776

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  299 IKQRTKLELKAKDLQDELagnseQRKRLLKERQKLLEKIEEKQKelaETEPKFNSVKEKEERGIARLAQATQ---ERTDL 375
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM-----EVDKKIKDIFDNFANIIEGGK---EGNLVINDSKEMEDSAIKEVADSKNmqlEEADA 1848

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  376 YAKQGRGSQFTSKE----ERDKWIKKELKSLDQAINDKKRQIAAIHK-DLEDTEAN---KEKNLEQ-YNKLDQDlnEVKA 446
Cdd:PTZ00121 1849 FEKHKFNKNNENGEdgnkEADFNKEKDLKEDDEEEIEEADEIEKIDKdDIEREIPNnnmAGKNNDIiDDKLDKD--EYIK 1926

                         330
                  ....*....|....*..
gi 158517902  447 RVEELDRKYYEVKNKKD 463
Cdd:PTZ00121 1927 RDAEETREEIIKISKKD 1943
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1113-1164 6.12e-03

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 40.66  E-value: 6.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158517902 1113 QQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDQALDAQHRKAVSDMIMEL 1164
Cdd:COG1123   141 HQLSGGQRQRVAIAMALA---LDPD-LLIADEPTTALDVTTQAEILDLLREL 188
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 178-500 6.23e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 6.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   178 LMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIynqELNETRAKLDELSAKRETSGEKSRQLR 257
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI---EEREQKRQEEYEEKLQEREQMDEIVER 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   258 DAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKI 337
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   338 EEKQKELAETepkfnsvKEKEERGIARLAQATQERtdlyakqgrgsqftskeerdKWIKKELksldQAINDKKRQIAAIH 417
Cdd:pfam13868  190 RAQQEKAQDE-------KAERDELRAKLYQEEQER--------------------KERQKER----EEAEKKARQRQELQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   418 KDLEDTEANKEKNLEQYNKLDQDLNE-VKARVEELDRKYYEVKNKKDELQSE--RNYLWREENAEQQALAAKREDLEKKQ 494
Cdd:pfam13868  239 QAREEQIELKERRLAEEAEREEEEFErMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIEEREEQRAAEREEELEEGE 318


                   ....*.
gi 158517902   495 QLLRAA 500
Cdd:pfam13868  319 RLREEE 324
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 191-299 6.53e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  191 ELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEytiYNQELNETRAKLDELSAKretsGEKSRQLRDAQQDARDKMEDI 270
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEASFERLAE---LRDELAELEEELEALKAR----WEAEKELIEEIQELKEELEQR 483

                          90       100
                  ....*....|....*....|....*....
gi 158517902  271 ERQVRELKTKISAMKEEKEQLSAERQEQI 299
Cdd:COG0542   484 YGKIPELEKELAELEEELAELAPLLREEV 512
PRK12705 PRK12705
hypothetical protein; Provisional
 192-370 6.66e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  192 LLKYIEERLHTLEEEKEELAQYQK-WDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQL--RDAQQDAR-DKM 267
Cdd:PRK12705   21 LVVLLKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqKEEQLDARaEKL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  268 EDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLElkakdlqdelagNSEQRKRLLKERQKLLEkiEEKQKELAET 347
Cdd:PRK12705  101 DNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT------------PEQARKLLLKLLDAELE--EEKAQRVKKI 166

                         170       180
                  ....*....|....*....|...
gi 158517902  348 EPKFNSVKEKEERGIarLAQATQ 370
Cdd:PRK12705  167 EEEADLEAERKAQNI--LAQAMQ 187
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 233-496 6.77e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   233 NETRAKLDELSAKRETSGEKSRQLRDAQQDARD----------KMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQR 302
Cdd:pfam15905   52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRAlvqergeqdkRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   303 TKLELKAKDLQDELAGNSEQRK--RLLKERQKLLEKIEEKQKELAEtepkfnsvkekEERGIARLAQATQerTDLYAKQG 380
Cdd:pfam15905  132 LELTRVNELLKAKFSEDGTQKKmsSLSMELMKLRNKLEAKMKEVMA-----------KQEGMEGKLQVTQ--KNLEHSKG 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   381 RGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTE---ANKEKNLEQYNKLDQDL-NEVKARVEELDRKYY 456
Cdd:pfam15905  199 KVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKldiAQLEELLKEKNDEIESLkQSLEEKEQELSKQIK 278

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 158517902   457 EVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQL 496
Cdd:pfam15905  279 DLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTL 318
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 1112-1161 6.90e-03

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 38.20  E-value: 6.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 158517902 1112 MQQLSGGQKSLVALALIFaIQKCDpapFYLFDEIDQALDAQHRKAVSDMI 1161
Cdd:cd03221    68 FEQLSGGEKMRLALAKLL-LENPN---LLLLDEPTNHLDLESIEALEEAL 113
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1110-1165 7.01e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 40.56  E-value: 7.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158517902 1110 REMQQLSGG--QKSLVALALIfaiqkcDPAPFYLFDEIDQALDAQHRKAVSDMIMELA 1165
Cdd:PRK13409  208 RDISELSGGelQRVAIAAALL------RDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
mukB PRK04863
chromosome partition protein MukB;
173-500 7.46e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  173 EESISLMKE---TEGKREKINELLKYIEERLHTLEEEKEELAQ-YQKW-DKMRRALEYTIYNQELNETRAKLDELSAKRE 247
Cdd:PRK04863  286 EEALELRRElytSRRQLAAEQYRLVEMARELAELNEAESDLEQdYQAAsDHLNLVQTALRQQEKIERYQADLEELEERLE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  248 TSGEKSRQLRDAQQDARDKMEDIERQVRELKTkisamkeekeQLSAERQeqikqrtklelkAKDLQDELAGNSEQRKRLL 327
Cdd:PRK04863  366 EQNEVVEEADEQQEENEARAEAAEEEVDELKS----------QLADYQQ------------ALDVQQTRAIQYQQAVQAL 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  328 KERQKLLekieekqkELAETEPKfnSVKEKEERGIARLAQATQERTDLYAK----QGRGSQFT-------------SKEE 390
Cdd:PRK04863  424 ERAKQLC--------GLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKlsvaQAAHSQFEqayqlvrkiagevSRSE 493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  391 RDKWIKKELKSL--DQAINDKKRQIAAIHKDLE---DTEANKEKNLEQYNK-----------LDQDLNEVKARVEELDrk 454
Cdd:PRK04863  494 AWDVARELLRRLreQRHLAEQLQQLRMRLSELEqrlRQQQRAERLLAEFCKrlgknlddedeLEQLQEELEARLESLS-- 571

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 158517902  455 yyEVKNKKDELQSernylwrEENAEQQALAAKREDLEKKQQLLRAA 500
Cdd:PRK04863  572 --ESVSEARERRM-------ALRQQLEQLQARIQRLAARAPAWLAA 608
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
670-884 7.91e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  670 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 748
Cdd:COG3206   172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  749 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 821
Cdd:COG3206   252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158517902  822 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 884
Cdd:COG3206   323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 834-1025 7.94e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  834 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 913
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  914 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 992
Cdd:COG4942   105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175

                         170       180       190
                  ....*....|....*....|....*....|...
gi 158517902  993 FSEQKEKLIKRQEELDRGYKSIMELMNVLELRK 1025
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 247-345 8.00e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 39.03  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   247 ETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKD-------LQDELAGN 319
Cdd:pfam06785   79 ELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEqlaekqlLINEYQQT 158

                           90       100
                   ....*....|....*....|....*.
gi 158517902   320 SEQRKRLLKERQKLLEKIEEKQKELA 345
Cdd:pfam06785  159 IEEQRSVLEKRQDQIENLESKVRDLN 184
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 154-385 8.02e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   154 QRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQ------------------YQK 215
Cdd:TIGR00618  643 LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtllrelethieeydreFNE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   216 WDKMRRALEYTI------YNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIErqvRELKTKISAMkEEKE 289
Cdd:TIGR00618  723 IENASSSLGSDLaaredaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA---AEIQFFNRLR-EEDT 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902   290 QLSAERQEQIKQRTKLELKAKDLQDE-LAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEergiarlAQA 368
Cdd:TIGR00618  799 HLLKTLEAEIGQEIPSDEDILNLQCEtLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ-------AKI 871

                          250
                   ....*....|....*..
gi 158517902   369 TQERTDLYAKQGRGSQF 385
Cdd:TIGR00618  872 IQLSDKLNGINQIKIQF 888
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 733-820 8.30e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 8.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902    733 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 812
Cdd:smart00935    7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86


                    ....*...
gi 158517902    813 QLLNERIK 820
Cdd:smart00935   87 KRQQEELQ 94
PRK11637 PRK11637
AmiB activator; Provisional
 206-467 8.46e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.06  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  206 EKEELAQYQKwdKMRRALeytiynqelnetrakLDELSAKRETSGEKSRQLRDAQqdarDKMEDIERQVRELKTKISAMK 285
Cdd:PRK11637   58 AKEKSVRQQQ--QQRASL---------------LAQLKKQEEAISQASRKLRETQ----NTLNQLNKQIDELNASIAKLE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  286 EEK--------EQL-SAERQeqiKQRTKLELKakdlqdeLAGNSEQRK-RLL-------KERQKLLEKIEEKQKELAETE 348
Cdd:PRK11637  117 QQQaaqerllaAQLdAAFRQ---GEHTGLQLI-------LSGEESQRGeRILayfgylnQARQETIAELKQTREELAAQK 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  349 pkfnsvKEKEERgiarlaqATQERTDLYAKQGRGSQFT-SKEERdkwiKKELKSLDQAINDKKRQIAAIHKD---LEDTE 424
Cdd:PRK11637  187 ------AELEEK-------QSQQKTLLYEQQAQQQKLEqARNER----KKTLTGLESSLQKDQQQLSELRANesrLRDSI 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 158517902  425 ANKEKnleqynkldqdlnEVKARVEELDRKYYEVKNKKDELQS 467
Cdd:PRK11637  250 ARAER-------------EAKARAEREAREAARVRDKQKQAKR 279
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 193-297 8.56e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.05  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  193 LKYIEERLHTLEE------EKEELAQYQKWDKMRRALEytiynqelnetrAKLDELSAKRETSGEKSRQLRDAQQDARDK 266
Cdd:PRK05431    4 IKLIRENPEAVKEalakrgFPLDVDELLELDEERRELQ------------TELEELQAERNALSKEIGQAKRKGEDAEAL 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 158517902  267 MEdierQVRELKTKISAMKEEKEQLSAERQE 297
Cdd:PRK05431   72 IA----EVKELKEEIKALEAELDELEAELEE 98
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 1110-1172 8.75e-03

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 39.24  E-value: 8.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158517902 1110 REMQQLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDQALDAQHRKAVSDMIMELavHAQFIT 1172
Cdd:COG1122   130 RPPHELSGGQKQRVAIAGVLAME-----PEVLvLDEPTAGLDPRGRRELLELLKRL--NKEGKT 186
PRK12704 PRK12704
phosphodiesterase; Provisional
 395-505 9.77e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158517902  395 IKKELKSLDQAINDKKRQIAAIHKDLEdTEAnKEKNLEQYNKLDQDLNEVKARVEELDRKyyeVKNKKDELQSERNYLWR 474
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAIKKEAL-LEA-KEEIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEK 107

                          90       100       110
                  ....*....|....*....|....*....|....
gi 158517902  475 EEN---AEQQALAAKREDLEKKQQLLRAATGKAI 505
Cdd:PRK12704  108 REEeleKKEKELEQKQQELEKKEEELEELIEEQL 141
 
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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