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Conserved domains on  [gi|14318514|ref|NP_116647|]
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cohesin subunit SMC1 [Saccharomyces cerevisiae S288C]

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

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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 ...
 4-1209 0e+00

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: 595.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      4 LVGLELSNFKSYrGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSN-HLRSNILKDLIYRGvlndensddydne 82
Cdd:pfam02463    2 LKRIEIEGFKSY-AKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIHSK------------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     83 gaASSNPQSAYVKAFYQKGNKL-------VELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVE 155
Cdd:pfam02463   68 --SGAFVNSAEVEITFDNEDHElpidkeeVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIE 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    156 QIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQK 235
Cdd:pfam02463  146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    236 FQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLI 315
Cdd:pfam02463  226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    316 KVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKY 395
Cdd:pfam02463  306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    396 LTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQ 475
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    476 SDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKN 555
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    556 FDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEpeyekamqyvcgdsiicntl 635
Cdd:pfam02463  546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    636 niakdlkwkkgirgklvtiegALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVEN 715
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    716 SVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSK 795
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    796 IGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIG 875
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    876 SIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISS 955
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    956 ETTIDDLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVI 1035
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1036 NNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYH 1115
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1116 ATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISLKNTMF 1195
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....
gi 14318514   1196 EKSDALVGVYRQQQ 1209
Cdd:pfam02463 1144 EKADKLVGVTMVEN 1157
 
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 ...
 4-1209 0e+00

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: 595.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      4 LVGLELSNFKSYrGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSN-HLRSNILKDLIYRGvlndensddydne 82
Cdd:pfam02463    2 LKRIEIEGFKSY-AKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIHSK------------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     83 gaASSNPQSAYVKAFYQKGNKL-------VELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVE 155
Cdd:pfam02463   68 --SGAFVNSAEVEITFDNEDHElpidkeeVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIE 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    156 QIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQK 235
Cdd:pfam02463  146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    236 FQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLI 315
Cdd:pfam02463  226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    316 KVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKY 395
Cdd:pfam02463  306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    396 LTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQ 475
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    476 SDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKN 555
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    556 FDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEpeyekamqyvcgdsiicntl 635
Cdd:pfam02463  546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    636 niakdlkwkkgirgklvtiegALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVEN 715
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    716 SVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSK 795
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    796 IGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIG 875
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    876 SIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISS 955
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    956 ETTIDDLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVI 1035
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1036 NNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYH 1115
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1116 ATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISLKNTMF 1195
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....
gi 14318514   1196 EKSDALVGVYRQQQ 1209
Cdd:pfam02463 1144 EKADKLVGVTMVEN 1157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-1220 7.06e-113

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: 380.95  E-value: 7.06e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      7 LELSNFKSYRGVTKVGFGEsNFTSIIGPNGSGKSNMMDAISFVLGVRSNH-LRSNILKDLIYRGvlndensddyDNEGAA 85
Cdd:TIGR02169    5 IELENFKSFGKKKVIPFSK-GFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNG----------KNGQSG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     86 SSNPQSAYVKAFYQKGNKLVELMRIISRNGD---TSYKIDGKTVSYKDYSIFLENENILIKAKNFlVFQGDVEQIAAQSP 162
Cdd:TIGR02169   74 NEAYVTVTFKNDDGKFPDELEVVRRLKVTDDgkySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSP 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    163 VELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALWQL 242
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEK 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    243 YHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDK-EKLVSDLRLIKVPQQA 321
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    322 AGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNclheKYLTEGGS 401
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF----AETRDELK 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    402 ILEEKIAVLNNDKREIQEELERFNKRAdiskrritEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESA 481
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEEL--------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    482 NNQEYDLN---FKLRETLVKIDD-LSANQRETMK-----------ERKLRENIAMLKRFFPGVKGLVHDLCHpKKEKYGL 546
Cdd:TIGR02169  461 AADLSKYEqelYDLKEEYDRVEKeLSKLQRELAEaeaqaraseerVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYAT 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    547 AVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYI-LSINAIDYEPEYEKAMQYV 625
Cdd:TIGR02169  540 AIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgFAVDLVEFDPKYEPAFKYV 619

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    626 CGDSIICNTLNIAKDLkwkkGIRGKLVTIEGALIHKAGLMTGG----ISGDANNRWDKEEYQ-------SLMSLKDKLLI 694
Cdd:TIGR02169  620 FGDTLVVEDIEAARRL----MGKYRMVTLEGELFEKSGAMTGGsrapRGGILFSRSEPAELQrlrerleGLKRELSSLQS 695

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    695 QIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQpKITELKKKLDDLENTK 774
Cdd:TIGR02169  696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS-ELKELEARIEELEEDL 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    775 DNLVKEKEALQNNIFKEFTSKIGftikeyenhsgELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLE 854
Cdd:TIGR02169  775 HKLEEALNDLEARLSHSRIPEIQ-----------AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    855 NAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELnssedilEDMNSNLQVLKRERDGIKEDIEKfd 934
Cdd:TIGR02169  844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER-------DELEAQLRELERKIEELEAQIEK-- 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    935 LERVTALKNCKISNINipiSSETTIDDLPISSTDNEAITISnsidinykgLPKKYKEnntdsaRKELEQKIHEVEEIlne 1014
Cdd:TIGR02169  915 KRKRLSELKAKLEALE---EELSEIEDPKGEDEEIPEEELS---------LEDVQAE------LQRVEEEIRALEPV--- 973

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1015 lqpNARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELtknpnsnvelAG 1094
Cdd:TIGR02169  974 ---NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL----------SG 1040

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1095 GNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAY 1174
Cdd:TIGR02169 1041 GTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKL 1120

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|....*.
gi 14318514   1175 IRRHRNpDLQFIVISLKNTMFEKSDALVGVyRQQQENSSKIITLDL 1220
Cdd:TIGR02169 1121 IREKAG-EAQFIVVSLRSPMIEYADRAIGV-TMRRNGESQVFGLKL 1164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-1225 3.37e-69

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 252.16  E-value: 3.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    3 RLVGLELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSN-HLRSNILKDLIYRG------------ 69
Cdd:COG1196    2 RLKRLELAGFKSFADPTTIPF-EPGITAIVGPNGSGKSNIVDAIRWVLGEQSAkSLRGGKMEDVIFAGsssrkplgraev 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   70 --VLndENSD-----DYDnegaassnpqsayvkafyqkgnkLVELMRIISRNGDTSYKIDGKTVSYKD------------ 130
Cdd:COG1196   81 slTF--DNSDgtlpiDYD-----------------------EVTITRRLYRSGESEYYINGKPCRLKDiqdlfldtglgp 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  131 --YSIflenenilikaknflVFQGDVEQIAAQSPVELSRMFEEVSGsiqykkeyeelkekieklsksatesI---KNRRR 205
Cdd:COG1196  136 esYSI---------------IGQGMIDRIIEAKPEERRAIIEEAAG-------------------------IskyKERKE 175

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  206 ------------------IHGELKTYKEGI----NKNEEYRKQLDKKNELQKFQALWQLYHLEQQKEELTDKLSALNSEI 263
Cdd:COG1196  176 eaerkleateenlerledILGELERQLEPLerqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  264 SSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQ 343
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  344 KTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKfklnendlktyncLHEKYLTEGGSILEEKIAVLNNDKREIQEELER 423
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLE-------------AEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  424 FNKRADISKRRIT-EELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQEYDLNFKLRETLVKIDDL 502
Cdd:COG1196  403 EELEEAEEALLERlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  503 SANQRETMKERKLRENI-------------AMLKRFFPGVKGLVHDLCHpKKEKYGLAVSTILGKNFDSVIVENLTVAQE 569
Cdd:COG1196  483 LEELAEAAARLLLLLEAeadyegflegvkaALLLAGLRGLAGAVAVLIG-VEAAYEAALEAALAAALQNIVVEDDEVAAA 561

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  570 CIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRG 649
Cdd:COG1196  562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  650 -----KLVTIEGALIHKAGLMTGGisgdannrwdkeeyqslmslkdklliqidelsnGQRSNSIRAREVENSVSLLNSDI 724
Cdd:COG1196  642 lagrlREVTLEGEGGSAGGSLTGG---------------------------------SRRELLAALLEAEAELEELAERL 688

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  725 ANLRTQVTQQKRSLDENRleikyhndliekeiqpkitelkkklddlentkdnlvkekealqnnifkeftskigftikeye 804
Cdd:COG1196  689 AEEELELEEALLAEEEEE-------------------------------------------------------------- 706

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  805 nhsgelmRQQSKELQQLQKQILTVENKLQfetdrlsttqrryekaQKDLENAQVEMKSLEEQEYAIEmkigsieskleeh 884
Cdd:COG1196  707 -------RELAEAEEERLEEELEEEALEE----------------QLEAEREELLEELLEEEELLEE------------- 750

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  885 knhldelqkkfvtkqselnssediledmnsnlqvlkrerDGIKEDIEKFDLErvtalknckisninipissettiddlpi 964
Cdd:COG1196  751 ---------------------------------------EALEELPEPPDLE---------------------------- 763

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  965 sstdneaitisnsidinykglpkkykenntdsarkELEQKIHEVEEILNELQP-NARALERYDEAEGRFEVINNETEQLK 1043
Cdd:COG1196  764 -----------------------------------ELERELERLEREIEALGPvNLLAIEEYEELEERYDFLSEQREDLE 808

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1044 AEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKnpnsnvelaGGNASLTIEDEDEPFNAGIKYHATPPLKRF 1123
Cdd:COG1196  809 EARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFG---------GGEAELLLTDPDDPLETGIEIMAQPPGKKL 879

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1124 KDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISL-KNTMfEKSDALV 1202
Cdd:COG1196  880 QRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSE-DTQFIVITHnKRTM-EAADRLY 957

                       1290      1300
                 ....*....|....*....|...
gi 14318514 1203 GVYrQQQENSSKIITLDLSNYAE 1225
Cdd:COG1196  958 GVT-MQEPGVSRVVSVDLEEAEE 979
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-162 4.64e-69

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: 232.08  E-value: 4.64e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    4 LVGLELSNFKSYRGVTKVGFGESnFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGVLNDENsddydneg 83
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPD-------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514   84 aassnPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSP 162
Cdd:cd03275   72 -----SNSAYVTAVYEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 527-641 6.47e-32

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: 120.80  E-value: 6.47e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     527 PGVKGLVHDLCHPKKeKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYI 606
Cdd:smart00968    1 PGVLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREALLP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 14318514     607 LS------INAIDYEPEYEKAMQYVCGDSIICNTLNIAKDL 641
Cdd:smart00968   80 EPgfvgpaIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
recF PRK00064
recombination protein F; Reviewed
 7-127 9.21e-09

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 58.63  E-value: 9.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     7 LELSNFKSYRGVTkVGFgESNFTSIIGPNGSGKSNMMDAISFV-LGvRSnhLRSNILKDLIYRGvlndensddydnegaa 85
Cdd:PRK00064    6 LSLTDFRNYEELD-LEL-SPGVNVLVGENGQGKTNLLEAIYLLaPG-RS--HRTARDKELIRFG---------------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 14318514    86 ssnPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVS 127
Cdd:PRK00064   65 ---AEAAVIHGRVEKGGRELPLGLEIDKKGGRKVRINGEPQR 103
 
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 ...
 4-1209 0e+00

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: 595.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      4 LVGLELSNFKSYrGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSN-HLRSNILKDLIYRGvlndensddydne 82
Cdd:pfam02463    2 LKRIEIEGFKSY-AKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIHSK------------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     83 gaASSNPQSAYVKAFYQKGNKL-------VELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVE 155
Cdd:pfam02463   68 --SGAFVNSAEVEITFDNEDHElpidkeeVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIE 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    156 QIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQK 235
Cdd:pfam02463  146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    236 FQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLI 315
Cdd:pfam02463  226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    316 KVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKY 395
Cdd:pfam02463  306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    396 LTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQ 475
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    476 SDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKN 555
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    556 FDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEpeyekamqyvcgdsiicntl 635
Cdd:pfam02463  546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    636 niakdlkwkkgirgklvtiegALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVEN 715
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    716 SVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSK 795
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    796 IGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIG 875
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    876 SIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISS 955
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    956 ETTIDDLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVI 1035
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1036 NNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYH 1115
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1116 ATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISLKNTMF 1195
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....
gi 14318514   1196 EKSDALVGVYRQQQ 1209
Cdd:pfam02463 1144 EKADKLVGVTMVEN 1157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-1220 7.06e-113

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: 380.95  E-value: 7.06e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      7 LELSNFKSYRGVTKVGFGEsNFTSIIGPNGSGKSNMMDAISFVLGVRSNH-LRSNILKDLIYRGvlndensddyDNEGAA 85
Cdd:TIGR02169    5 IELENFKSFGKKKVIPFSK-GFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNG----------KNGQSG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     86 SSNPQSAYVKAFYQKGNKLVELMRIISRNGD---TSYKIDGKTVSYKDYSIFLENENILIKAKNFlVFQGDVEQIAAQSP 162
Cdd:TIGR02169   74 NEAYVTVTFKNDDGKFPDELEVVRRLKVTDDgkySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSP 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    163 VELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALWQL 242
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEK 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    243 YHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDK-EKLVSDLRLIKVPQQA 321
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    322 AGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNclheKYLTEGGS 401
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF----AETRDELK 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    402 ILEEKIAVLNNDKREIQEELERFNKRAdiskrritEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESA 481
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEEL--------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    482 NNQEYDLN---FKLRETLVKIDD-LSANQRETMK-----------ERKLRENIAMLKRFFPGVKGLVHDLCHpKKEKYGL 546
Cdd:TIGR02169  461 AADLSKYEqelYDLKEEYDRVEKeLSKLQRELAEaeaqaraseerVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYAT 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    547 AVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYI-LSINAIDYEPEYEKAMQYV 625
Cdd:TIGR02169  540 AIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgFAVDLVEFDPKYEPAFKYV 619

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    626 CGDSIICNTLNIAKDLkwkkGIRGKLVTIEGALIHKAGLMTGG----ISGDANNRWDKEEYQ-------SLMSLKDKLLI 694
Cdd:TIGR02169  620 FGDTLVVEDIEAARRL----MGKYRMVTLEGELFEKSGAMTGGsrapRGGILFSRSEPAELQrlrerleGLKRELSSLQS 695

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    695 QIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQpKITELKKKLDDLENTK 774
Cdd:TIGR02169  696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS-ELKELEARIEELEEDL 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    775 DNLVKEKEALQNNIFKEFTSKIGftikeyenhsgELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLE 854
Cdd:TIGR02169  775 HKLEEALNDLEARLSHSRIPEIQ-----------AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    855 NAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELnssedilEDMNSNLQVLKRERDGIKEDIEKfd 934
Cdd:TIGR02169  844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER-------DELEAQLRELERKIEELEAQIEK-- 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    935 LERVTALKNCKISNINipiSSETTIDDLPISSTDNEAITISnsidinykgLPKKYKEnntdsaRKELEQKIHEVEEIlne 1014
Cdd:TIGR02169  915 KRKRLSELKAKLEALE---EELSEIEDPKGEDEEIPEEELS---------LEDVQAE------LQRVEEEIRALEPV--- 973

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1015 lqpNARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELtknpnsnvelAG 1094
Cdd:TIGR02169  974 ---NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL----------SG 1040

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1095 GNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAY 1174
Cdd:TIGR02169 1041 GTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKL 1120

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|....*.
gi 14318514   1175 IRRHRNpDLQFIVISLKNTMFEKSDALVGVyRQQQENSSKIITLDL 1220
Cdd:TIGR02169 1121 IREKAG-EAQFIVVSLRSPMIEYADRAIGV-TMRRNGESQVFGLKL 1164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-1220 6.57e-104

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: 356.29  E-value: 6.57e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      3 RLVGLELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRS-NHLRSNILKDLIYrgvlndensddydn 81
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTINF-DKGITGIVGPNGCGKSNIVDAIRWVLGEQSaKALRGGKMEDVIF-------------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     82 EGAASSNPQS-AYVK--------AFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKD-YSIFLENEniLIKAKNFLVFQ 151
Cdd:TIGR02168   66 NGSETRKPLSlAEVElvfdnsdgLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDiQDLFLDTG--LGKRSYSIIEQ 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    152 GDVEQIAAQSPVELSRMFEEVSGsIQYKKEYEELKEKIEKLSKSATESIK-NRRRIHGELKTYKEGINKNEEYRKQLDKK 230
Cdd:TIGR02168  144 GKISEIIEAKPEERRAIFEEAAG-ISKYKERRKETERKLERTRENLDRLEdILNELERQLKSLERQAEKAERYKELKAEL 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    231 NELQKFQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVS 310
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    311 DLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKtync 390
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE---- 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    391 lhEKYLTEGGSI--LEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGE----KLDTQLNDLRVSLNEKNALH 464
Cdd:TIGR02168  379 --EQLETLRSKVaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEEELEELQEEL 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    465 TERLHELKKLQSDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPkKEKY 544
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV-DEGY 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    545 GLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYI-----LSINAIDYEPEYE 619
Cdd:TIGR02168  536 EAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgVAKDLVKFDPKLR 615

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    620 KAMQYVCGDSIICNTLNIAKDLKWKKGIRGKLVTIEGALIHKAGLMTGGISGDANNRWDKE-EYQSLMSLKDKLLIQIDE 698
Cdd:TIGR02168  616 KALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRrEIEELEEKIEELEEKIAE 695

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    699 LSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIE------KEIQPKITELKKKLDDLEN 772
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIEELEERLEEAEE 775

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    773 TKDNLVKEKEALQNNI--FKEFTSKIGFTIKEyenhsgelmrqQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQ 850
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIeqLKEELKALREALDE-----------LRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    851 KDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDI 930
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    931 EKFDLeRVTALKNcKISNInipissettiddlpisstdneAITISNSIDINYKGLPKKYkeNNTDSARKELEQKIHEVEE 1010
Cdd:TIGR02168  925 AQLEL-RLEGLEV-RIDNL---------------------QERLSEEYSLTLEEAEALE--NKIEDDEEEARRRLKRLEN 979

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1011 ILNELQP-NARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELtknpnsn 1089
Cdd:TIGR02168  980 KIKELGPvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKL------- 1052

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1090 veLAGGNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQ 1169
Cdd:TIGR02168 1053 --FGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVE 1130

                         1210      1220      1230      1240      1250
                   ....*....|....*....|....*....|....*....|....*....|..
gi 14318514   1170 RIAAYIRRHRNpDLQFIVISL-KNTMfEKSDALVGVyRQQQENSSKIITLDL 1220
Cdd:TIGR02168 1131 RFANLLKEFSK-NTQFIVITHnKGTM-EVADQLYGV-TMQEKGVSKIVSVDL 1179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-1225 3.37e-69

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 252.16  E-value: 3.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    3 RLVGLELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSN-HLRSNILKDLIYRG------------ 69
Cdd:COG1196    2 RLKRLELAGFKSFADPTTIPF-EPGITAIVGPNGSGKSNIVDAIRWVLGEQSAkSLRGGKMEDVIFAGsssrkplgraev 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   70 --VLndENSD-----DYDnegaassnpqsayvkafyqkgnkLVELMRIISRNGDTSYKIDGKTVSYKD------------ 130
Cdd:COG1196   81 slTF--DNSDgtlpiDYD-----------------------EVTITRRLYRSGESEYYINGKPCRLKDiqdlfldtglgp 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  131 --YSIflenenilikaknflVFQGDVEQIAAQSPVELSRMFEEVSGsiqykkeyeelkekieklsksatesI---KNRRR 205
Cdd:COG1196  136 esYSI---------------IGQGMIDRIIEAKPEERRAIIEEAAG-------------------------IskyKERKE 175

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  206 ------------------IHGELKTYKEGI----NKNEEYRKQLDKKNELQKFQALWQLYHLEQQKEELTDKLSALNSEI 263
Cdd:COG1196  176 eaerkleateenlerledILGELERQLEPLerqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  264 SSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQ 343
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  344 KTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKfklnendlktyncLHEKYLTEGGSILEEKIAVLNNDKREIQEELER 423
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLE-------------AEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  424 FNKRADISKRRIT-EELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQEYDLNFKLRETLVKIDDL 502
Cdd:COG1196  403 EELEEAEEALLERlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  503 SANQRETMKERKLRENI-------------AMLKRFFPGVKGLVHDLCHpKKEKYGLAVSTILGKNFDSVIVENLTVAQE 569
Cdd:COG1196  483 LEELAEAAARLLLLLEAeadyegflegvkaALLLAGLRGLAGAVAVLIG-VEAAYEAALEAALAAALQNIVVEDDEVAAA 561

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  570 CIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRG 649
Cdd:COG1196  562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  650 -----KLVTIEGALIHKAGLMTGGisgdannrwdkeeyqslmslkdklliqidelsnGQRSNSIRAREVENSVSLLNSDI 724
Cdd:COG1196  642 lagrlREVTLEGEGGSAGGSLTGG---------------------------------SRRELLAALLEAEAELEELAERL 688

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  725 ANLRTQVTQQKRSLDENRleikyhndliekeiqpkitelkkklddlentkdnlvkekealqnnifkeftskigftikeye 804
Cdd:COG1196  689 AEEELELEEALLAEEEEE-------------------------------------------------------------- 706

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  805 nhsgelmRQQSKELQQLQKQILTVENKLQfetdrlsttqrryekaQKDLENAQVEMKSLEEQEYAIEmkigsieskleeh 884
Cdd:COG1196  707 -------RELAEAEEERLEEELEEEALEE----------------QLEAEREELLEELLEEEELLEE------------- 750

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  885 knhldelqkkfvtkqselnssediledmnsnlqvlkrerDGIKEDIEKFDLErvtalknckisninipissettiddlpi 964
Cdd:COG1196  751 ---------------------------------------EALEELPEPPDLE---------------------------- 763

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  965 sstdneaitisnsidinykglpkkykenntdsarkELEQKIHEVEEILNELQP-NARALERYDEAEGRFEVINNETEQLK 1043
Cdd:COG1196  764 -----------------------------------ELERELERLEREIEALGPvNLLAIEEYEELEERYDFLSEQREDLE 808

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1044 AEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKnpnsnvelaGGNASLTIEDEDEPFNAGIKYHATPPLKRF 1123
Cdd:COG1196  809 EARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFG---------GGEAELLLTDPDDPLETGIEIMAQPPGKKL 879

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1124 KDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISL-KNTMfEKSDALV 1202
Cdd:COG1196  880 QRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSE-DTQFIVITHnKRTM-EAADRLY 957

                       1290      1300
                 ....*....|....*....|...
gi 14318514 1203 GVYrQQQENSSKIITLDLSNYAE 1225
Cdd:COG1196  958 GVT-MQEPGVSRVVSVDLEEAEE 979
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-162 4.64e-69

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: 232.08  E-value: 4.64e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    4 LVGLELSNFKSYRGVTKVGFGESnFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGVLNDENsddydneg 83
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPD-------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514   84 aassnPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSP 162
Cdd:cd03275   72 -----SNSAYVTAVYEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 1117-1220 4.80e-65

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: 220.52  E-value: 4.80e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1117 TPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFE 1196
Cdd:cd03275  144 NPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFS 223

                         90       100
                 ....*....|....*....|....
gi 14318514 1197 KSDALVGVYRQQQENSSKIITLDL 1220
Cdd:cd03275  224 KADALVGVYRDQECNSSKVLTLDL 247
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 1127-1208 2.96e-35

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: 132.43  E-value: 2.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1127 EYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYR 1206
Cdd:cd03239   93 QILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLF 172


                 ..
gi 14318514 1207 QQ 1208
Cdd:cd03239  173 VH 174
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 527-641 6.47e-32

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: 120.80  E-value: 6.47e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     527 PGVKGLVHDLCHPKKeKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYI 606
Cdd:smart00968    1 PGVLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREALLP 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 14318514     607 LS------INAIDYEPEYEKAMQYVCGDSIICNTLNIAKDL 641
Cdd:smart00968   80 EPgfvgpaIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 1119-1213 6.58e-30

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: 117.95  E-value: 6.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1119 PLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISLKNTMFEKS 1198
Cdd:cd03278  104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSK-ETQFIVITHRKGTMEAA 182

                         90
                 ....*....|....*
gi 14318514 1199 DALVGVYRQQQENSS 1213
Cdd:cd03278  183 DRLYGVTMQESGVSK 197
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1116-1207 1.44e-29

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: 117.40  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1116 ATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRhRNPDLQFIVISLKNTMF 1195
Cdd:cd03274  115 AQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKE-RTKNAQFIVISLRNNMF 193

                         90
                 ....*....|..
gi 14318514 1196 EKSDALVGVYRQ 1207
Cdd:cd03274  194 ELADRLVGIYKT 205
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 526-641 6.59e-27

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: 106.19  E-value: 6.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    526 FPGVKGLVHDLCHPKkEKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDY 605
Cdd:pfam06470    1 LKGVLGRLADLIEVD-EGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGA 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 14318514    606 ILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDL 641
Cdd:pfam06470   80 GPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALEL 115
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 4-105 2.54e-25

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: 103.93  E-value: 2.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    4 LVGLELSNFKSYRGVTKVGFGESnFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLiyrgvlndensddydNEG 83
Cdd:cd03239    1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---------------AGG 64

                         90       100
                 ....*....|....*....|..
gi 14318514   84 AASSNPQSAYVKAFYQKGNKLV 105
Cdd:cd03239   65 GVKAGINSASVEITFDKSYFLV 86
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 1129-1208 7.73e-25

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: 102.05  E-value: 7.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1129 LSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYRQQ 1208
Cdd:cd03227   78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 7-158 5.06e-20

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: 89.66  E-value: 5.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    7 LELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYrgvlndeNSDDYdnegaas 86
Cdd:cd03274    6 LVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIH-------NSAGH------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14318514   87 SNPQSAYVKAFYQKgnklvelmrIISRNgdtsykidgktvsykdysiFLENENILIKAKNFLVFQGDVEQIA 158
Cdd:cd03274   72 PNLDSCSVEVHFQE---------IIDKP-------------------LLKSKGIDLDHNRFLILQGEVEQIA 115
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1129-1208 5.51e-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: 85.04  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1129 LSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRnPDLQFIVISLKNTMFEKSDALVGVYRQQ 1208
Cdd:cd03273  167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHF-KGSQFIVVSLKEGMFNNANVLFRTRFVD 245
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 7-69 3.67e-17

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: 80.97  E-value: 3.67e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318514    7 LELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSNH-LRSNILKDLIYRG 69
Cdd:cd03278    4 LELKGFKSFADKTTIPF-PPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKsLRGEKMSDVIFAG 66
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 7-59 6.52e-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: 73.55  E-value: 6.52e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 14318514    7 LELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRS 59
Cdd:cd03227    2 IVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR 54
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 1124-1204 2.34e-14

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: 74.22  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1124 KDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNpDLQFIVISLKNTMFEKSDALVG 1203
Cdd:cd03272  154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSD-GAQFITTTFRPELLEVADKFYG 232


                 .
gi 14318514 1204 V 1204
Cdd:cd03272  233 V 233
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 9-166 6.38e-14

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: 73.10  E-value: 6.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    9 LSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRS-NHLRSNILKDLIYR----GVLNDENSDDYDNEG 83
Cdd:cd03273    8 LDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKrgqaGITKASVTIVFDNSD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   84 AASSNPQsayvkafyQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQ------I 157
Cdd:cd03273   88 KSQSPIG--------FENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKvlnmggV 159


                 ....*....
gi 14318514  158 AAQSPVELS 166
Cdd:cd03273  160 WKESLTELS 168
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
3-127 3.24e-10

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


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 63.25  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    3 RLVGLELSNFKSYRGVTkVGFGeSNFTSIIGPNGSGKSNMMDAISFVLGVRSnhLRSNILKDLIyrgvlndensddydNE 82
Cdd:COG1195    1 RLKRLSLTNFRNYESLE-LEFS-PGINVLVGPNGQGKTNLLEAIYLLATGRS--FRTARDAELI--------------RF 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 14318514   83 GAassnpQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVS 127
Cdd:COG1195   63 GA-----DGFRVRAEVERDGREVRLGLGLSRGGKKRVRINGKPVR 102
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 9-174 1.05e-09

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: 60.35  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    9 LSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGvlndensddydnegaASSN 88
Cdd:cd03272    6 IQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEG---------------SGPS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   89 PQSAYVK-AFYQKGNKL------VELMRIISRNGDtSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQS 161
Cdd:cd03272   71 VMSAYVEiIFDNSDNRFpidkeeVRLRRTIGLKKD-EYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMK 149

                        170
                 ....*....|...
gi 14318514  162 PVELSRMfEEVSG 174
Cdd:cd03272  150 QDEQQEM-QQLSG 161
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 1111-1189 2.05e-09

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: 57.64  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1111 GIKYHATPPLKRFKDMEY---LSGGEKTVAALALLFAINSyqpsPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIV 1187
Cdd:cd00267   60 GKDIAKLPLEELRRRIGYvpqLSGGQRQRVALARALLLNP----DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVII 135


                 ..
gi 14318514 1188 IS 1189
Cdd:cd00267  136 VT 137
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 755-932 6.02e-09

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: 58.01  E-value: 6.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  755 EIQPKITELKKKLDDLENTKDNLVKEKEALQNNIfKEFTSKIgftikeyenhsgelmRQQSKELQQLQKQILTVENKLQf 834
Cdd:COG1579   21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-EDLEKEI---------------KRLELEIEEVEARIKKYEEQLG- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  835 etdrLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELnssEDILEDMNS 914
Cdd:COG1579   84 ----NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEA 156

                        170
                 ....*....|....*...
gi 14318514  915 NLQVLKRERDGIKEDIEK 932
Cdd:COG1579  157 ELEELEAEREELAAKIPP 174
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
3-69 6.38e-09

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 57.33  E-value: 6.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318514    3 RLVGLELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHlRSNILKDLIYRG 69
Cdd:COG0419    1 KLLRLRLENFRSYRDTETIDF-DDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVG 65
recF PRK00064
recombination protein F; Reviewed
 7-127 9.21e-09

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 58.63  E-value: 9.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     7 LELSNFKSYRGVTkVGFgESNFTSIIGPNGSGKSNMMDAISFV-LGvRSnhLRSNILKDLIYRGvlndensddydnegaa 85
Cdd:PRK00064    6 LSLTDFRNYEELD-LEL-SPGVNVLVGENGQGKTNLLEAIYLLaPG-RS--HRTARDKELIRFG---------------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 14318514    86 ssnPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVS 127
Cdd:PRK00064   65 ---AEAAVIHGRVEKGGRELPLGLEIDKKGGRKVRINGEPQR 103
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3-446 1.56e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    3 RLVGLELSNFKSYRGVTKVGFGESNfTSIIGPNGSGKSNMMDAISFVL-----------------GVRSnhLRSnilkdl 65
Cdd:COG4913    2 RLQRLQLINWGTFDGVHTIDFDGRG-TLLTGDNGSGKSTLLDAIQTLLvpakrprfnkaandagkSDRT--LLS------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   66 iY-RGVLNDENSDDYDN-----EGAASSnpqsaYVKAFYQ--KGNKLVELMRII------SRNGDTS--YKIDGKTVSYK 129
Cdd:COG4913   73 -YvRGKYGSERDEAGTRpvylrPGDTWS-----AIAATFAndGSGQTVTLAQVFwlkgdaSSLGDVKrfFVIADGPLDLE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  130 DYSIFLENENI-----LIKAKNFLVFQGDVE---------------------QIAAQSPV----ELSR--MFEE--VSGS 175
Cdd:COG4913  147 DFEEFAHGFDIralkaRLKKQGVEFFDSFSAylarlrrrlgigsekalrllhKTQSFKPIgdldDFVReyMLEEpdTFEA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  176 IQykkeyeelkekieklskSATESIKNRRRIHGELKTYKEGIN-------KNEEYRKQLDKKNELQKFQALWQLYHLEQQ 248
Cdd:COG4913  227 AD-----------------ALVEHFDDLERAHEALEDAREQIEllepireLAERYAAARERLAELEYLRAALRLWFAQRR 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  249 KEELTDKLSALNSEISSLKGKINnemkslqrskssfvKESAVISKQKSKLDyifkdkeklvsdlRLIKVPQQAAGKRISH 328
Cdd:COG4913  290 LELLEAELEELRAELARLEAELE--------------RLEARLDALREELD-------------ELEAQIRGNGGDRLEQ 342

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  329 IEKRIESLQKDLQRQKTYVERFETQLKV----VTRSKEAFEEEIKQSARNYDKFKLNENDLktynclhEKYLTEggsiLE 404
Cdd:COG4913  343 LEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEAL-------EEALAE----AE 411

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 14318514  405 EKIAVLNNDKREIQEELERFNKRAD-ISKR------RITEELSITGEKL 446
Cdd:COG4913  412 AALRDLRRELRELEAEIASLERRKSnIPARllalrdALAEALGLDEAEL 460
COG4637 COG4637
Predicted ATPase [General function prediction only];
3-49 1.89e-07

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 54.94  E-value: 1.89e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 14318514    3 RLVGLELSNFKSYRGVTkVGFGesNFTSIIGPNGSGKSNMMDAISFV 49
Cdd:COG4637    1 MITRIRIKNFKSLRDLE-LPLG--PLTVLIGANGSGKSNLLDALRFL 44
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
 7-127 3.63e-07

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: 53.07  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    7 LELSNFKSYRGVtKVGFGEsNFTSIIGPNGSGKSNMMDAISFVLGVRSnhLRSNILKDLIYRGvlndensddydnegaas 86
Cdd:cd03242    4 LELRNFRNYAEL-ELEFEP-GVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELIRWG----------------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 14318514   87 snPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVS 127
Cdd:cd03242   63 --AEEAKISAVLERQGGELALELTIRSGGGRKARLNGIKVR 101
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 2-69 4.53e-07

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: 51.83  E-value: 4.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    2 GRLVGLELSNFKSYrGVTKVGFGES-NFtsIIGPNGSGKSNMMDAISFVLGVRSNHL-RSNILKDLIYRG 69
Cdd:cd03277    1 GSIVRIKLENFVTY-DETEFRPGPSlNM--IIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVKRG 67
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 726-1073 9.27e-07

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: 53.10  E-value: 9.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    726 NLRTQVTQQKRSLDENRLEIKYHNDLIEkEIQPKITELKKKLDDLEN---TKDNLVKEKEALQNNIFKEFTSKIGfTIKE 802
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIIS-QLNEQISQLKKELTNSESensEKQRELEEKQNEIEKLKKENQSYKQ-EIKN 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    803 YENHSGEL---MRQQSKELQQLQKQILTVE---NKLQFETDRLSTTQRRYEKAQKDLENA----QVEMKSLEEQEYAIEM 872
Cdd:TIGR04523  389 LESQINDLeskIQNQEKLNQQKDEQIKKLQqekELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLET 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    873 KIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTalKNCKISNINIP 952
Cdd:TIGR04523  469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE--KESKISDLEDE 546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    953 ISS----------ETTID--DLPISSTDNEAITISNSIDINYKGLPKKYKENNTdsARKELEQKIHEVEEILNELQpnaR 1020
Cdd:TIGR04523  547 LNKddfelkkenlEKEIDekNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD--LIKEIEEKEKKISSLEKELE---K 621

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 14318514   1021 ALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSD 1073
Cdd:TIGR04523  622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
AAA_29 pfam13555
P-loop containing region of AAA domain;
4-60 1.21e-06

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 46.82  E-value: 1.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 14318514      4 LVGLELSNFKSYRGVTkVGFGESNFTSIIGPNGSGKSNMMDAISFVLgVRSNHLRSN 60
Cdd:pfam13555    1 LTRLQLINWGTFDGHT-IPIDPRGNTLLTGPSGSGKSTLLDAIQTLL-VPAKRARFN 55
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 244-902 1.50e-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: 52.81  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    244 HLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKS-SFVKESAVISKQKSKLDYIFKDKEKLVSDLrliKVPQQAA 322
Cdd:pfam15921  214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGL---TEKASSA 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    323 GKRISHIEKRIESLQKDLQRQKTYVERfetQLKVVTRSKEAFEEEIKQSARNY-DKFK-------LNENDLKTYNCLHEK 394
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYeDKIEelekqlvLANSELTEARTERDQ 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    395 YLTEGGSI---LEEKIAVLNNDKREIQEELERfNKRadISKRRITEELSItgekldtqlNDLRVSLNEKNaLHTERLHE- 470
Cdd:pfam15921  368 FSQESGNLddqLQKLLADLHKREKELSLEKEQ-NKR--LWDRDTGNSITI---------DHLRRELDDRN-MEVQRLEAl 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    471 LKKLQSDIESANNQEYDLNFKLRETLVKIDDLSAnQRETMKE--RKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYglav 548
Cdd:pfam15921  435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTA-QLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKE---- 509

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    549 STILGKNFD-SVIVENLTVAQECIAFLKKQRAGtasfipLDTIETELPTLSLP-DSQDYILSInaidYEPEYEKAMQYVc 626
Cdd:pfam15921  510 RAIEATNAEiTKLRSRVDLKLQELQHLKNEGDH------LRNVQTECEALKLQmAEKDKVIEI----LRQQIENMTQLV- 578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    627 gdsiicntlniakdlkwkkGIRGKlvTIEGALIHKAGLmtggiSGDANNRwdKEEYQSLMSLKDKLLIQIDEL------- 699
Cdd:pfam15921  579 -------------------GQHGR--TAGAMQVEKAQL-----EKEINDR--RLELQEFKILKDKKDAKIRELearvsdl 630

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    700 ---------SNGQRSNSIRAREVE-----NSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIE---KEIQPKITE 762
Cdd:pfam15921  631 elekvklvnAGSERLRAVKDIKQErdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmqlKSAQSELEQ 710

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    763 LKKKLDDLENTKDNLVKEKEALQNNI------FKEFTSKIGFTIKEYENHSGE--LMRQQSKELQQLQKQILTVENKLQF 834
Cdd:pfam15921  711 TRNTLKSMEGSDGHAMKVAMGMQKQItakrgqIDALQSKIQFLEEAMTNANKEkhFLKEEKNKLSQELSTVATEKNKMAG 790

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    835 ETDRLSTTQRRYEKAQKDLENA--QVEMKSLEEQEYAIEMKIGSIESKLeEHKNHLDELQKKFVTKQSEL 902
Cdd:pfam15921  791 ELEVLRSQERRLKEKVANMEVAldKASLQFAECQDIIQRQEQESVRLKL-QHTLDVKELQGPGYTSNSSM 859
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-517 1.56e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   163 VELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALWQL 242
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   243 YHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKeSAVISKQKSKldyifKDKEKLVSDLRlikvpqqAA 322
Cdd:PRK03918  394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK-CPVCGRELTE-----EHRKELLEEYT-------AE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   323 GKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEE--EIKQSARNYDKFKLnENDLKTYNCLHEKYLTEGG 400
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNLEEL-EKKAEEYEKLKEKLIKLKG 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   401 SILE-----EKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNE----KNALH--TERLH 469
Cdd:PRK03918  540 EIKSlkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelKDAEKelEREEK 619

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 14318514   470 ELKKLQSDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRE 517
Cdd:PRK03918  620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE 667
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 812-1066 2.15e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  812 RQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQeyaIEMKIGSIESKLEEHKNHLDEL 891
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  892 QkkfvtKQSELNSSEDILedMNSnlqvlkrerdgikEDIEKFdLERVTALKNckisninipissettiddlpISSTDNEA 971
Cdd:COG3883   96 Y-----RSGGSVSYLDVL--LGS-------------ESFSDF-LDRLSALSK--------------------IADADADL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  972 ItisnsidinykglpkkykeNNTDSARKELEQKIHEVEEILNELQPNARALERY-DEAEGRFEVINNETEQLKAEEKKIL 1050
Cdd:COG3883  135 L-------------------EELKADKAELEAKKAELEAKLAELEALKAELEAAkAELEAQQAEQEALLAQLSAEEAAAE 195

                        250
                 ....*....|....*.
gi 14318514 1051 NQFLKIKKKRKELFEK 1066
Cdd:COG3883  196 AQLAELEAELAAAEAA 211
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 1121-1206 2.50e-06

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: 49.52  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1121 KRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNvQRIAAYI---RRHRNPDLQFIVISLKNTMFEK 1197
Cdd:cd03276  102 AAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKISTDLlvkEAKKQPGRQFIFITPQDISGLA 180


                 ....*....
gi 14318514 1198 SDALVGVYR 1206
Cdd:cd03276  181 SSDDVKVFR 189
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
676-1189 4.04e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   676 RWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRtQVTQQKRSLDENRLEIKYHNDLIE-- 753
Cdd:PRK03918  289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEea 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   754 KEIQPKITELKKKL-----DDLENTKDNLVKEKEALQNNIfKEFTSKIGFTIKEY------------------------- 803
Cdd:PRK03918  368 KAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI-SKITARIGELKKEIkelkkaieelkkakgkcpvcgrelt 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   804 ENHSGELMRQQSKELQQLQKQILTVENKLqfetdrlSTTQRRYEKAQKDLENAQ--VEMKSLEEQEYAIEMKIGSIE-SK 880
Cdd:PRK03918  447 EEHRKELLEEYTAELKRIEKELKEIEEKE-------RKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNlEE 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   881 LEEHKNHLDELQKKFVTKQSELNSSEDILEdmnsNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISSETTID 960
Cdd:PRK03918  520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK 595

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   961 DL-PISSTDNEAITISNSIDINYKGLPKKykENNTDSARKELEQKIHEVEEI---LNELQPN------ARALERYDE--- 1027
Cdd:PRK03918  596 ELePFYNEYLELKDAEKELEREEKELKKL--EEELDKAFEELAETEKRLEELrkeLEELEKKyseeeyEELREEYLElsr 673

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1028 ----AEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKEL--FEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTI 1101
Cdd:PRK03918  674 elagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekLEKALERVEELREKVKKYKALLKERALSKVGEIASEIF 753

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1102 EDEDEPFNAGIKYHATPPLKRFK--------DMEYLSGGEKTVAALALLFAINSYQPS--PFFVLDEVDAALDITNVQRI 1171
Cdd:PRK03918  754 EELTEGKYSGVRVKAEENKVKLFvvyqgkerPLTFLSGGERIALGLAFRLALSLYLAGniPLLILDEPTPFLDEERRRKL 833

                         570
                  ....*....|....*...
gi 14318514  1172 AAYIRRHRNPDLQFIVIS 1189
Cdd:PRK03918  834 VDIMERYLRKIPQVIIVS 851
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 444-943 4.05e-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: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    444 EKLDTQLNDLRVSLNEKNALHTERLHELKklQSDIesannqeyDLNFKLRETLVKIDDLS-ANQRETMKERKLRENIAML 522
Cdd:pfam15921   81 EEYSHQVKDLQRRLNESNELHEKQKFYLR--QSVI--------DLQTKLQEMQMERDAMAdIRRRESQSQEDLRNQLQNT 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    523 KRFFPGVKGLVHDLchpkkekygLAVSTILGKNFDSVIVENLTVAQECIAFLKK-QRAGTASFIPLDTIETeLPTLSLPD 601
Cdd:pfam15921  151 VHELEAAKCLKEDM---------LEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEHDSMST-MHFRSLGS 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    602 SQDYILsiNAIDYEPEYEKAMQYVCGDSIicNTLNIAKDLKWKKGIRGKLVTIEGALIHKAGLMTGGISGDANNRWDKEE 681
Cdd:pfam15921  221 AISKIL--RELDTEISYLKGRIFPVEDQL--EALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    682 YQSLMSLkdklliqIDELSNGQRSNSIRarevenSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKIT 761
Cdd:pfam15921  297 IQSQLEI-------IQEQARNQNSMYMR------QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEART 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    762 E--------------LKKKLDDLENTKDNLVKEKEalQNNIFKEFTSKIGFTIkeyeNHSGELMRQQSKELQQLQKQILT 827
Cdd:pfam15921  364 ErdqfsqesgnlddqLQKLLADLHKREKELSLEKE--QNKRLWDRDTGNSITI----DHLRRELDDRNMEVQRLEALLKA 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    828 VENKLQFETDRlsttqrryekaqkdlenaqvEMKSLEEQEYAIEmKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSED 907
Cdd:pfam15921  438 MKSECQGQMER--------------------QMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 14318514    908 ILEDMNSNLQVLKRERDGIKEDIEK------FDLERVTALKN 943
Cdd:pfam15921  497 TVSDLTASLQEKERAIEATNAEITKlrsrvdLKLQELQHLKN 538
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 678-1063 4.11e-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: 51.17  E-value: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    678 DKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDE----------------N 741
Cdd:TIGR04523  115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLlekeklniqknidkikN 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    742 RLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQ------NNIFKEFTSKIGFTIKEYENHSGELMRQQs 815
Cdd:TIGR04523  195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQqeinekTTEISNTQTQLNQLKDEQNKIKKQLSEKQ- 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    816 KELQQLQKQILTVENKLQFETDRLSTTQRryEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKF 895
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    896 VTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKF------------DLERVTALKNCKISNINIPISS-ETTIDDL 962
Cdd:TIGR04523  352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesqindleskiqNQEKLNQQKDEQIKKLQQEKELlEKEIERL 431

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    963 PISSTDNEAiTISNSIDINYKglpKKYKENNTDSARKELEQKIHEVEEILNELQPNARALER-YDEAEGRFEVINNETEQ 1041
Cdd:TIGR04523  432 KETIIKNNS-EIKDLTNQDSV---KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKeLKSKEKELKKLNEEKKE 507

                          410       420
                   ....*....|....*....|..
gi 14318514   1042 LKAEEKKILNQFLKIKKKRKEL 1063
Cdd:TIGR04523  508 LEEKVKDLTKKISSLKEKIEKL 529
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 3-55 5.83e-06

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: 50.00  E-value: 5.83e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 14318514    3 RLVGLELSNFKSYRGVTkVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSN 55
Cdd:COG3593    2 KLEKIKIKNFRSIKDLS-IEL-SDDLTVLVGENNSGKSSILEALRLLLGPSSS 52
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
 7-66 6.18e-06

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: 50.05  E-value: 6.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      7 LELSNFKSYRGVTkVGFgESNFTSIIGPNGSGKSNMMDAIsFVLGVRSNHlRSNILKDLI 66
Cdd:TIGR00611    6 LELTDFRNYDAVD-LEL-SPGVNVIVGPNGQGKTNLLEAI-YYLALGRSH-RTSRDKPLI 61
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 683-1023 7.09e-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: 50.40  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    683 QSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKeIQPKITE 762
Cdd:TIGR04523  207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ-NNKKIKE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    763 LKKKLDDLENTKDNLVKEKEALQNNIFKEFTSKIGFTIKEYENHsgelMRQQSKELQQLQKQILTVENKLQFETDRLSTT 842
Cdd:TIGR04523  286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQ----ISQNNKIISQLNEQISQLKKELTNSESENSEK 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    843 QRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDmnsnlqvLKRE 922
Cdd:TIGR04523  362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-------LKET 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    923 RDGIKEDIEkfDLERVTALKNCKISNINIPISSETTiddlPISSTDNEAITISNSIDINYKGLPKKYKE-NNTDSARKEL 1001
Cdd:TIGR04523  435 IIKNNSEIK--DLTNQDSVKELIIKNLDNTRESLET----QLKVLSRSINKIKQNLEQKQKELKSKEKElKKLNEEKKEL 508

                          330       340
                   ....*....|....*....|..
gi 14318514   1002 EQKIHEVEEILNELQPNARALE 1023
Cdd:TIGR04523  509 EEKVKDLTKKISSLKEKIEKLE 530
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
7-523 7.58e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     7 LELSNFKSYRGvTKVGFgESNFTSIIGPNGSGKSNMMDAI--SFVLGVRSNhlrsnilkdliYRGVLNDENSDDydnega 84
Cdd:PRK03918    6 LKIKNFRSHKS-SVVEF-DDGINLIIGQNGSGKSSILEAIlvGLYWGHGSK-----------PKGLKKDDFTRI------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    85 assNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFL----VFQGDVEQI--- 157
Cdd:PRK03918   67 ---GGSGTEIELKFEKNGRKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERLIPYHVFLnaiyIRQGEIDAIles 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   158 -------------------AAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNR-RRIHGELKTYKEGI 217
Cdd:PRK03918  144 desrekvvrqilglddyenAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREiNEISSELPELREEL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   218 NKNEEYRKQLDK-KNELQKFQAlwQLYHLEQQKEELTDKLSALNSEISSLKGKINN------EMKSLQRSKSSFVKESAV 290
Cdd:PRK03918  224 EKLEKEVKELEElKEEIEELEK--ELESLEGSKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEF 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   291 ISKQKSKLDYIFKDKEKLVSDLR-LIKVPQQAAGK--RISHIEKRIESLQKDLQRQKTYVERFETqlkvvTRSKEAFEEE 367
Cdd:PRK03918  302 YEEYLDELREIEKRLSRLEEEINgIEERIKELEEKeeRLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELER 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   368 IKQSARNYDKFKLNENDLKTYNCLHEkyLTEGGSILEEKIAVLNN---DKREIQEELERFNKRADISKRRITEElsitge 444
Cdd:PRK03918  377 LKKRLTGLTPEKLEKELEELEKAKEE--IEEEISKITARIGELKKeikELKKAIEELKKAKGKCPVCGRELTEE------ 448

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514   445 kldtqlndlrvslnEKNALHTERLHELKKLQSDIESANNQEYdlnfKLRETLVKIDDLSANQRETMKERKLRENIAMLK 523
Cdd:PRK03918  449 --------------HRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIKLKELAEQLKELE 509
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
754-1187 8.02e-06

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


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 50.12  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  754 KEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSKIGFTIKEYENHSgeLMRQQSKELQQLQKQILTVENKLQ 833
Cdd:COG4694  102 IELEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLF--ASSGRNYRKANLEKKLSALKSSSE 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  834 FETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAI--EMKIGSIESKLEEHKNHLD---------------------- 889
Cdd:COG4694  180 DELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLleKSAVSSAIEELAALIQNPGnsdwveqglayhkeeeddtcpf 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  890 ---ELQKKFVTKQSEL--NSSEDILEDMNSNLQVLKRERDGIKE---DIEKFDLERVTALKNCKISNINIPISSETTI-- 959
Cdd:COG4694  260 cqqELAAERIEALEAYfdDEYEKLLAALKDLLEELESAINALSAlllEILRTLLPSAKEDLKAALEALNALLETLLAAle 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  960 --DDLPISSTDNEAITISNSIDINYKGLPKKYKENNT-----DSARKELEQKI--HEVEEILNELqpnARALERYDEAEG 1030
Cdd:COG4694  340 ekIANPSTSIDLDDQELLDELNDLIAALNALIEEHNAkianlKAEKEEARKKLeaHELAELKEDL---SRYKAEVEELIE 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1031 RFEVINNETEQLKAEEKKIlnqflkiKKKRKELFEktfdyVSDHLDAIyreltknpnsNVELAG-GNASLTIEDEDEpfn 1109
Cdd:COG4694  417 ELKTIKALKKALEDLKTEI-------SELEAELSS-----VDEAADEI----------NEELKAlGFDEFSLEAVED--- 471

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1110 aGIKYHAtppLKRFKDMEY-----LSGGEKTVAA----LALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRN 1180
Cdd:COG4694  472 -GRSSYR---LKRNGENDAkpaktLSEGEKTAIAlayfLAELEGDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKELSK 547


                 ....*..
gi 14318514 1181 PDLQFIV 1187
Cdd:COG4694  548 KAKQVIV 554
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 695-894 1.06e-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: 49.38  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  695 QIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKyhndLIEKEIQPKITELKKKLDDLENTK 774
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  775 DNLVKEKEALQNN--------IFKEFTSKIGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRY 846
Cdd:COG4942  104 EELAELLRALYRLgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14318514  847 EKAQKDLENAQVEMKSLEEQeyaiemkigsIESKLEEHKNHLDELQKK 894
Cdd:COG4942  184 EEERAALEALKAERQKLLAR----------LEKELAELAAELAELQQE 221
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 809-1067 2.67e-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: 47.84  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  809 ELMRQQSKELQQLQKQILTVENKLQfetdrlsTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHL 888
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  889 DELQKKFVTKQSELN-------------------SSEDILeDMNSNLQVLKRERDGIKEDIEKF--DLERVTALKNckis 947
Cdd:COG4942   93 AELRAELEAQKEELAellralyrlgrqpplalllSPEDFL-DAVRRLQYLKYLAPARREQAEELraDLAELAALRA---- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  948 ninipissettiddlpisstdneaitisnsiDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERyde 1027
Cdd:COG4942  168 -------------------------------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--- 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 14318514 1028 aegrfevinnETEQLKAEEKKILNQFLKIKKKRKELFEKT 1067
Cdd:COG4942  214 ----------ELAELQQEAEELEALIARLEAEAAAAAERT 243
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 690-1084 2.80e-05

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: 48.31  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    690 DKLLIQIDELSNGQRSNSIRA--REVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIkyhndlieKEIQPKITELKKKL 767
Cdd:pfam06160   66 EELLFEAEELNDKYRFKKAKKalDEIEELLDDIEEDIKQILEELDELLESEEKNREEV--------EELKDKYRELRKTL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    768 ----DDLENTKDNLVKEKEALQNNiFKEFtskigftikEYENHSGELMrQQSKELQQLQKQILTVENKLQFETDRLSTTQ 843
Cdd:pfam06160  138 lanrFSYGPAIDELEKQLAEIEEE-FSQF---------EELTESGDYL-EAREVLEKLEEETDALEELMEDIPPLYEELK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    844 RRYEKAQKDLENAqveMKSLEEQEYA-----IEMKIGSIESKLEEHKNHLDELqkkfvtkqsELNSSEDILEDMNSNLqv 918
Cdd:pfam06160  207 TELPDQLEELKEG---YREMEEEGYAlehlnVDKEIQQLEEQLEENLALLENL---------ELDEAEEALEEIEERI-- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    919 lkrerDGIKEDIEKFDLERVTALKNCKIsninipissettiddlpISSTDNEAITISNSIDINYKGLPKKYKENNTDSAR 998
Cdd:pfam06160  273 -----DQLYDLLEKEVDAKKYVEKNLPE-----------------IEDYLEHAEEQNKELKEELERVQQSYTLNENELER 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    999 -KELEQKIHEVEEILNELQPNARALE-RYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDhLD 1076
Cdd:pfam06160  331 vRGLEKQLEELEKRYDEIVERLEEKEvAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLE-LR 409


                   ....*...
gi 14318514   1077 AIYRELTK 1084
Cdd:pfam06160  410 EIKRLVEK 417
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 7-50 3.38e-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: 46.06  E-value: 3.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 14318514    7 LELSNFKSYRGVTKVGFgESNFTSIIGPNGSGKSNMMDAISFVL 50
Cdd:cd03240    4 LSIRNIRSFHERSEIEF-FSPLTLIVGQNGAGKTTIIEALKYAL 46
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
767-1066 3.52e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   767 LDDLENTKDNLVKEKEALQNNI-----FKEFTSKIGFTIKEYENHSGELMRQQSKelqqlqkqILTVENKLQFETDRLST 841
Cdd:PRK03918  157 LDDYENAYKNLGEVIKEIKRRIerlekFIKRTENIEELIKEKEKELEEVLREINE--------ISSELPELREELEKLEK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   842 TQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKfVTKQSELNSSEDILEDMNSNLQVLKR 921
Cdd:PRK03918  229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   922 ERDGIKEDIEKFDLERvtalknckisninipissettiddlpisstdneaitisnsidinyKGLPKKYKENNTDSAR-KE 1000
Cdd:PRK03918  308 ELREIEKRLSRLEEEI---------------------------------------------NGIEERIKELEEKEERlEE 342

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318514  1001 LEQKIHEVEEILNELQPNARALERYDEAEGRFEVI-----NNETEQLKAEEKKILNQFLKIKKKRKELFEK 1066
Cdd:PRK03918  343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1074-1179 4.31e-05

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: 45.93  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514 1074 HLDAIYRELTknPNSNVELAGGNASLTIEDEDepfnagikyhATPPLKRF-------KDMEYLSGGEKTVAALALLFAin 1146
Cdd:COG4133   82 HADGLKPELT--VRENLRFWAALYGLRADREA----------IDEALEAVglagladLPVRQLSAGQKRRVALARLLL-- 147

                         90       100       110
                 ....*....|....*....|....*....|...
gi 14318514 1147 syQPSPFFVLDEVDAALDITNVQRIAAYIRRHR 1179
Cdd:COG4133  148 --SPAPLWLLDEPFTALDAAGVALLAELIAAHL 178
46 PHA02562
endonuclease subunit; Provisional
 838-1199 5.51e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   838 RLSTTQRRyeKAQKDLENAQV--EM--------KSLEEQEYAIEMKIGSIESKLEEHKNHLDEL-----------QKKFV 896
Cdd:PHA02562  146 QLSAPARR--KLVEDLLDISVlsEMdklnkdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngeniarkQNKYD 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   897 TKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERvtALKNCKISNINIPISSETTIDDLP-----ISSTDNEA 971
Cdd:PHA02562  224 ELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA--AKIKSKIEQFQKVIKMYEKGGVCPtctqqISEGPDRI 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   972 ITISNSIdinyKGLPKKYKENNTdsARKELEQKIHE-------VEEILNELQPNARALERY-----------DEAEGRFE 1033
Cdd:PHA02562  302 TKIKDKL----KELQHSLEKLDT--AIDELEEIMDEfneqskkLLELKNKISTNKQSLITLvdkakkvkaaiEELQAEFV 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1034 VINNETEQLKAEEKKILNQFLKIKKKRKELfektfDYVSDHL--DAIYRELTKN--P------NSNVELAGGNASLTIed 1103
Cdd:PHA02562  376 DNAEELAKLQDELDKIVKTKSELVKEKYHR-----GIVTDLLkdSGIKASIIKKyiPyfnkqiNHYLQIMEADYNFTL-- 448

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1104 eDEPFNAGIKyhatpplKRFKD-MEY--LSGGEKTVAALALLFA-------INSYQPSpFFVLDEV-DAALDITNVQRIA 1172
Cdd:PHA02562  449 -DEEFNETIK-------SRGREdFSYasFSQGEKARIDLALLFTwrdvaskVSGVDTN-LLILDEVfDGALDAEGTKALL 519

                         410       420
                  ....*....|....*....|....*..
gi 14318514  1173 AYIRRHRNPDlqFIVISLKNTMFEKSD 1199
Cdd:PHA02562  520 SILDSLKDTN--VFVISHKDHDPQKFD 544
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 711-1082 6.23e-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: 47.42  E-value: 6.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    711 REVENSVSLLNSDIANLRTQVTQQKrSLDENRLEI--KYHNDLIEK---EIQPKITELKKKLDDLENTKDNL------VK 779
Cdd:pfam15921  227 RELDTEISYLKGRIFPVEDQLEALK-SESQNKIELllQQHQDRIEQlisEHEVEITGLTEKASSARSQANSIqsqleiIQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    780 EKEALQNNIFKEFTSKIGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKL--------QFET------DRLSTTQRR 845
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELtearterdQFSQesgnldDQLQKLLAD 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    846 YEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSE-----------LNSSEDILEDMNS 914
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmerqmaaIQGKNESLEKVSS 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    915 NLQVLKRERDGIKEDIEKFDLERVTALknckisninipiSSETTIDDL---------PISSTDNEAITISNSIDINYKGL 985
Cdd:pfam15921  466 LTAQLESTKEMLRKVVEELTAKKMTLE------------SSERTVSDLtaslqekerAIEATNAEITKLRSRVDLKLQEL 533

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    986 PK--------KYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVinnETEQLKAEekkilnqflkIK 1057
Cdd:pfam15921  534 QHlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQV---EKAQLEKE----------IN 600

                          410       420
                   ....*....|....*....|....*
gi 14318514   1058 KKRKELfeKTFDYVSDHLDAIYREL 1082
Cdd:pfam15921  601 DRRLEL--QEFKILKDKKDAKIREL 623
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 757-932 6.52e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  757 QPKITELKKKLDDLENTKDNLVKEKEALQNnifkeftsKIGFTIKEYENHSGELMRQQsKELQQLQKQILTVENKLQ--- 833
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQA--------ELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEerr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  834 ----------------------------FET--DRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEE 883
Cdd:COG3883   86 eelgeraralyrsggsvsyldvllgsesFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 14318514  884 HKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEK 932
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
46 PHA02562
endonuclease subunit; Provisional
 718-924 6.83e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.93  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   718 SLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEkEIQPK----ITELKKKLDDLENTKDNLVKEKEALQNNIfkeft 793
Cdd:PHA02562  170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIE-EQRKKngenIARKQNKYDELVEEAKTIKAEIEELTDEL----- 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   794 SKIGFTIKEYENHSGELMRQQSK---ELQQLQK----------------QILTVENKLQFETDRLSTTQRRYEKAQKDLE 854
Cdd:PHA02562  244 LNLVMDIEDPSAALNKLNTAAAKiksKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAID 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   855 NAQVEMKSLEEQeyaiEMKIGSIESKLEEHKNHL--------------DELQKKFVTKQSELNSSEDILEDMNSNLQVLK 920
Cdd:PHA02562  324 ELEEIMDEFNEQ----SKKLLELKNKISTNKQSLitlvdkakkvkaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELV 399


                  ....
gi 14318514   921 RERD 924
Cdd:PHA02562  400 KEKY 403
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 7-50 7.18e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 45.34  E-value: 7.18e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 14318514    7 LELSNFKSYRGVTKVGF---GESNFTSIIGPNGSGKSNMMDAISFVL 50
Cdd:cd03279    6 LELKNFGPFREEQVIDFtglDNNGLFLICGPTGAGKSTILDAITYAL 52
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 683-1069 9.33e-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: 46.94  E-value: 9.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    683 QSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSvsllNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKeiqpkite 762
Cdd:TIGR04523   82 QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND----KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK-------- 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    763 LKKKLDDLENTKDNLVKEKEALQN--NIFKEFTSKIG-----------------FTIKEYENHSGELMRQ---------- 813
Cdd:TIGR04523  150 KEKELEKLNNKYNDLKKQKEELENelNLLEKEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESQiselkkqnnq 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    814 -------QSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEH-- 884
Cdd:TIGR04523  230 lkdniekKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwn 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    885 ---KNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKfdLERVTALKNCKISNINIPISSE-TTID 960
Cdd:TIGR04523  310 kelKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE--KQRELEEKQNEIEKLKKENQSYkQEIK 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    961 DLPISSTD-----NEAITISNSIDINYKGLPKKY----------KENNTDSAR--KELEQKIHEVEEILNELQPNARALE 1023
Cdd:TIGR04523  388 NLESQINDleskiQNQEKLNQQKDEQIKKLQQEKellekeierlKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLE 467

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 14318514   1024 RY-DEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFD 1069
Cdd:TIGR04523  468 TQlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
PRK01156 PRK01156
chromosome segregation protein; Provisional
 7-473 1.07e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     7 LELSNFKSYRGVTKvgFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSnhlRSNILKDLIYRGVLNDENSDDYDNEGaas 86
Cdd:PRK01156    6 IRLKNFLSHDDSEI--EFDTGINIITGKNGAGKSSIVDAIRFALFTDK---RTEKIEDMIKKGKNNLEVELEFRIGG--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    87 snpQSAYVKAFYQKGNKLVELMRIISRNGDTSykidgkTVSYKDYSIFLEnENILIKAKN-----FLVFQGDVEQIAAQS 161
Cdd:PRK01156   78 ---HVYQIRRSIERRGKGSRREAYIKKDGSII------AEGFDDTTKYIE-KNILGISKDvflnsIFVGQGEMDSLISGD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   162 PVELSRMFEEvsgsIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELqkfqalwq 241
Cdd:PRK01156  148 PAQRKKILDE----ILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI-------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   242 lyhLEQQKEELTDKLSALNSEISSLKGKINNeMKSLQRSKSSFVKEsavISKQKSKLDYIFKDKEKLVS-DLRLIKVPQQ 320
Cdd:PRK01156  216 ---TLKEIERLSIEYNNAMDDYNNLKSALNE-LSSLEDMKNRYESE---IKTAESDLSMELEKNNYYKElEERHMKIIND 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   321 AAGKRISHI------EKRIESLQKDLQRQKTYVERFETQLKVVTrSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEK 394
Cdd:PRK01156  289 PVYKNRNYIndyfkyKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS 367

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514   395 YLTEGGSIlEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDtQLNDLRVSLNEKNALHTERLHELKK 473
Cdd:PRK01156  368 YLKSIESL-KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ-DISSKVSSLNQRIRALRENLDELSR 444
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 730-934 1.18e-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: 45.91  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  730 QVTQQKRSLDENRLEIKYHNDLIeKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIfKEFTSKIGFTIKEYENHSGE 809
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  810 LMRQQ---SKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKN 886
Cdd:COG4942   99 LEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14318514  887 HLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFD 934
Cdd:COG4942  179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 221-935 1.27e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    221 EEYRKQLDKKNELQKFQALW----------QLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSsfVKESAV 290
Cdd:pfam15921   88 KDLQRRLNESNELHEKQKFYlrqsvidlqtKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC--LKEDML 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    291 --ISKQKSKLDYIFKDKEKLVSDLRLIKVP-QQAAGKRI---------------SHIEKRIESLQKDLQRQKTYVERFET 352
Cdd:pfam15921  166 edSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIyehdsmstmhfrslgSAISKILRELDTEISYLKGRIFPVED 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    353 QLkvvtrskeafeEEIKQSARNYDKFKLNENDLKTYNCLHEKYLTEGGsiLEEKIAVLNNDKREIQEELERFNKRADISK 432
Cdd:pfam15921  246 QL-----------EALKSESQNKIELLLQQHQDRIEQLISEHEVEITG--LTEKASSARSQANSIQSQLEIIQEQARNQN 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    433 RRITEELSitgeKLDTQLNDLRVSLNEKNALHTERLHELKK----LQSDIESA-------NNQEYDLNFKLRETLVkidD 501
Cdd:pfam15921  313 SMYMRQLS----DLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEArterdqfSQESGNLDDQLQKLLA---D 385

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    502 LSANQRETMKERKlrENiamlKRFFPGVKGLVHDLCHPKKEkyglavstILGKNFDSVIVENL--TVAQECIAFLKKQRA 579
Cdd:pfam15921  386 LHKREKELSLEKE--QN----KRLWDRDTGNSITIDHLRRE--------LDDRNMEVQRLEALlkAMKSECQGQMERQMA 451

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    580 gtasfipldtietelptlSLPDSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRGKLVTIEGALI 659
Cdd:pfam15921  452 ------------------AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE 513

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    660 HKAGLMTggisgDANNRWDKEeYQSLMSLKDklliQIDELSNGQ---RSNSIRAREVENSVSLLNSDIANLRTQVTQQKR 736
Cdd:pfam15921  514 ATNAEIT-----KLRSRVDLK-LQELQHLKN----EGDHLRNVQtecEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    737 S--------------LDENRLEIKYHNDLIEKEiQPKITELKKKLDDLENTKDNLVKE-KEALQnnIFKEFTSKIGFTIK 801
Cdd:pfam15921  584 TagamqvekaqlekeINDRRLELQEFKILKDKK-DAKIRELEARVSDLELEKVKLVNAgSERLR--AVKDIKQERDQLLN 660

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    802 EYENHSGELmRQQSKELQQLQKQILTVENKLQFETDRLsttQRRYEKAQKDLENAQVEMKSLEEQE-YAIEMKIGsIESK 880
Cdd:pfam15921  661 EVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETTTNKL---KMQLKSAQSELEQTRNTLKSMEGSDgHAMKVAMG-MQKQ 735

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318514    881 LEEHKNHLDELQKK----------------FVTKQ-----SELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDL 935
Cdd:pfam15921  736 ITAKRGQIDALQSKiqfleeamtnankekhFLKEEknklsQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEV 811
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 695-883 1.33e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  695 QIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIkyhnDLIEKEIQPKITELKKKLDDLENTK 774
Cdd:COG3883   24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEERREELGERARALYRSG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  775 DNLVKEKEALQNNIFKEFTSKIGFTIKeyenhsgeLMRQQSKELQQLQKQILTVENK---LQFETDRLSTTQRRYEKAQK 851
Cdd:COG3883  100 GSVSYLDVLLGSESFSDFLDRLSALSK--------IADADADLLEELKADKAELEAKkaeLEAKLAELEALKAELEAAKA 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 14318514  852 DLENAQVE----MKSLEEQEYAIEMKIGSIESKLEE 883
Cdd:COG3883  172 ELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAA 207
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 679-1062 1.43e-04

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: 46.25  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    679 KEEYQSLMSLKDK----LLIQIDELSNGQRSNSIRAREVENSVSLLNSdianlRTQVTQQK-RSLDENRLEIKYHNDLIE 753
Cdd:pfam05483  228 EEEYKKEINDKEKqvslLLIQITEKENKMKDLTFLLEESRDKANQLEE-----KTKLQDENlKELIEKKDHLTKELEDIK 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    754 KEIQPKITELKKKLDDLE---NTKDNLVKEKEALQNNIFKEFTSKiGFTIKEYENHSGELMRQQSKELQQLQKQiltvEN 830
Cdd:pfam05483  303 MSLQRSMSTQKALEEDLQiatKTICQLTEEKEAQMEELNKAKAAH-SFVVTEFEATTCSLEELLRTEQQRLEKN----ED 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    831 KLQFETDRLSTTQRRYEKAQKDLENAQVEMKSL-----EEQEYAIEMKigSIESKLEEHKNHLDELQKKFVTKQSELNSS 905
Cdd:pfam05483  378 QLKIITMELQKKSSELEEMTKFKNNKEVELEELkkilaEDEKLLDEKK--QFEKIAEELKGKEQELIFLLQAREKEIHDL 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    906 EDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNC-KISNINIPISSETTIDDLPISSTDNEAITISNSIDINYKG 984
Cdd:pfam05483  456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ 535

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    985 LPKKYKE-----NNTDSARKELEQKIHEVEEILNELQPNARALE-RYDEAEGRFEVINNETEQLKaeeKKILNQFLKIKK 1058
Cdd:pfam05483  536 IENLEEKemnlrDELESVREEFIQKGDEVKCKLDKSEENARSIEyEVLKKEKQMKILENKCNNLK---KQIENKNKNIEE 612


                   ....
gi 14318514   1059 KRKE 1062
Cdd:pfam05483  613 LHQE 616
PRK01156 PRK01156
chromosome segregation protein; Provisional
 678-1219 1.77e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.05  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   678 DKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENsvslLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEK--- 754
Cdd:PRK01156  337 DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKeln 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   755 EIQPKITELKKKLDDLENTKDNLVKEKEALQNNI-------------FKEFTSKIGFTIKEYENHSGEL------MRQQS 815
Cdd:PRK01156  413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgTTLGEEKSNHIINHYNEKKSRLeekireIEIEV 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   816 KELQQLQKQILTVENKLQF-ETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIE--------MKIGSIESKLEEHKN 886
Cdd:PRK01156  493 KDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEeiknryksLKLEDLDSKRTSWLN 572

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   887 HL--------DELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEkfdlERVTALKNCKISNINIPISSET- 957
Cdd:PRK01156  573 ALavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE----NEANNLNNKYNEIQENKILIEKl 648

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   958 --TIDDL--------PISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKE-----LEQKIHEVEEILNELQPNARAL 1022
Cdd:PRK01156  649 rgKIDNYkkqiaeidSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEstieiLRTRINELSDRINDINETLESM 728

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1023 ERYDEAEGRFEVINN--ETEQLKAEEKKILNQFLKiKKKRKELFEKTFDYvsdhlDAIyreltknpnsnvelaggnaslt 1100
Cdd:PRK01156  729 KKIKKAIGDLKRLREafDKSGVPAMIRKSASQAMT-SLTRKYLFEFNLDF-----DDI---------------------- 780

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1101 ieDEDEPFNAGIKYHATPplkrfKDMEYLSGGEKTVAALALLFAINSY--QPSPFFVLDEVDAALD---ITNVQRIAAYI 1175
Cdd:PRK01156  781 --DVDQDFNITVSRGGMV-----EGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDedrRTNLKDIIEYS 853

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 14318514  1176 RRHRNPDLQFIVISLKNTMFEKSDALVGVyrQQQENSSKIITLD 1219
Cdd:PRK01156  854 LKDSSDIPQVIMISHHRELLSVADVAYEV--KKSSGSSKVIPLR 895
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
811-1116 1.88e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  811 MRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDE 890
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  891 LQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISSETTIDDLPISSTDNE 970
Cdd:COG4372  141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  971 AITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQ---PNARALERYDEAEGRFEVINNETEQLKAEEK 1047
Cdd:COG4372  221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilvEKDTEEEELEIAALELEALEEAALELKLLAL 300

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514 1048 KILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYHA 1116
Cdd:COG4372  301 LLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
4-78 2.56e-04

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


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 44.65  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    4 LVGLELSNFKSYRGVTKVGFGESNFTS-----IIGPNGSGKSNMMDAISFvlgVRSNHLRSNILKDLIYRGVLNDENSDD 78
Cdd:COG1106    2 LISFSIENFRSFKDELTLSMVASGLRLlrvnlIYGANASGKSNLLEALYF---LRNLVLNSSQPGDKLVEPFLLDSESKN 78
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 212-501 2.63e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    212 TYKEGINKNEEYRKQLDKK-----NELQKFQA-----LWQLYHLEQQKEELTDKLSALNSEISSLKGKI---NNEMKSLQ 278
Cdd:TIGR04523   23 GYKNIANKQDTEEKQLEKKlktikNELKNKEKelknlDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLkknKDKINKLN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    279 RSKSSFVKESAVISKQKSKLDYIFKDKEKlvsDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVT 358
Cdd:TIGR04523  103 SDLSKINSEIKNDKEQKNKLEVELNKLEK---QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    359 RSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHeKYLTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITeE 438
Cdd:TIGR04523  180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-Q 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318514    439 LSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQ-EYDLNFKLRETLVKIDD 501
Cdd:TIGR04523  258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEK 321
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 7-66 3.60e-04

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: 42.97  E-value: 3.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318514    7 LELSNFKSYRGVtKVGFGeSNFTSIIGPNGSGKSNMMDAISFVLGVRSNHL-RSNILKDLI 66
Cdd:cd03276    4 ITLKNFMCHRHL-QIEFG-PRVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLI 62
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 221-490 3.86e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   221 EEYRKQLDKKneLQKFQalwqLYHLEQQKEELTDklsALNSEISSLKGKINNEMKSLQRSKSSF-VKESAVISKQKSKLD 299
Cdd:PRK05771   15 KSYKDEVLEA--LHELG----VVHIEDLKEELSN---ERLRKLRSLLTKLSEALDKLRSYLPKLnPLREEKKKVSVKSLE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   300 YIFKDKEKLVSDLRlikvpqqaagKRISHIEKRIESLQ---KDLQRQKTYVERFE--------------TQLKVVTRSKE 362
Cdd:PRK05771   86 ELIKDVEEELEKIE----------KEIKELEEEISELEneiKELEQEIERLEPWGnfdldlslllgfkyVSVFVGTVPED 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   363 AFEEEIKQSARNYDKF------------------------KLNENDLKTYNCLHEKYLTEGGSILEEKIAVLNNDKREIQ 418
Cdd:PRK05771  156 KLEELKLESDVENVEYistdkgyvyvvvvvlkelsdeveeELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   419 EELERFNKRADISKRRITEELSITGEKLDTQLNDLRvslneknalhTERLH---------ELKKLQSDIESANNQEYDLN 489
Cdd:PRK05771  236 EELKELAKKYLEELLALYEYLEIELERAEALSKFLK----------TDKTFaiegwvpedRVKKLKELIDKATGGSAYVE 305


                  .
gi 14318514   490 F 490
Cdd:PRK05771  306 F 306
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
709-1215 5.64e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   709 RAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIK-----------------YHNDLIEKE---IQPKITELKKKLD 768
Cdd:PRK02224  357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelrerfgdapvdlgnaeDFLEELREErdeLREREAELEATLR 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   769 DLENTkdnlVKEKEALQN--------NIFKEftSKIGFTIKEYENHSGELmrqqSKELQQLQKQILTVENKLQFETDrLS 840
Cdd:PRK02224  437 TARER----VEEAEALLEagkcpecgQPVEG--SPHVETIEEDRERVEEL----EAELEDLEEEVEEVEERLERAED-LV 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   841 TTQRRYEKAQKDLENAQvemKSLEEQEYAIEMKigsiESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLK 920
Cdd:PRK02224  506 EAEDRIERLEERREDLE---ELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   921 RERDGIKEDIEKFD--LERVTALKNC--KISNINIPISSETTIDDLPIS--STDNEAItisnsidinyKGLPKKYKENNT 994
Cdd:PRK02224  579 SKLAELKERIESLEriRTLLAAIADAedEIERLREKREALAELNDERRErlAEKRERK----------RELEAEFDEARI 648

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   995 DSAR---KELEQKIHEVEEILNELQpnaralERYDEAEGRFEVINNETEQLKA--EEKKILNQflkikkkRKELFEKTFD 1069
Cdd:PRK02224  649 EEARedkERAEEYLEQVEEKLDELR------EERDDLQAEIGAVENELEELEElrERREALEN-------RVEALEALYD 715

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1070 YVSDhLDAIYRELTKN-PNSNVE------------LAGGNASLTIEDEDEpfnagikYHAT------PPLkrfkDMEYLS 1130
Cdd:PRK02224  716 EAEE-LESMYGDLRAElRQRNVEtlermlnetfdlVYQNDAYSHIELDGE-------YELTvyqkdgEPL----EPEQLS 783

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  1131 GGEKTVAALALLFAInsYQ----------PSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDL-QFIVISLKNTMFEKSD 1199
Cdd:PRK02224  784 GGERALFNLSLRCAI--YRllaegiegdaPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGVeQIVVVSHDDELVGAAD 861

                         570
                  ....*....|....*.
gi 14318514  1200 ALVGVYRQQQENSSKI 1215
Cdd:PRK02224  862 DLVRVEKDPTTNRSSV 877
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 247-508 5.69e-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: 43.60  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  247 QQKEELTDKLSALNSEISSLKGKInnemKSLQRSKSSFVKESAVISKQKSKLdyifkdkeklVSDLRLIKVPQQAAGKRI 326
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAAL----------ARRIRALEQELAALEAEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  327 SHIEKRIESLQKDLQRQKtyvERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNclhekylteggSILEEK 406
Cdd:COG4942   86 AELEKEIAELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-----------PARREQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  407 IAVLNNDKREIQEelerfnKRADISKRRiteelsitgEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQEY 486
Cdd:COG4942  152 AEELRADLAELAA------LRAELEAER---------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                        250       260
                 ....*....|....*....|..
gi 14318514  487 DLNFKLRETLVKIDDLSANQRE 508
Cdd:COG4942  217 ELQQEAEELEALIARLEAEAAA 238
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 726-1063 5.87e-04

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: 44.33  E-value: 5.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    726 NLRTQVTQQKRSLDENRLEIKYHNDLIEkEIQPKITELKKKLDDLENTKDNLVKEKEALQN--NIFKEFTSKIGFTIKEY 803
Cdd:pfam05483   96 SIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVSLKLEEEIQENKDLIKENNATRHlcNLLKETCARSAEKTKKY 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    804 EnHSGELMRQQSKELQQ-LQKQILTVEN-KLQFETDRLST---TQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIE 878
Cdd:pfam05483  175 E-YEREETRQVYMDLNNnIEKMILAFEElRVQAENARLEMhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    879 SKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINI---PISS 955
Cdd:pfam05483  254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcqlTEEK 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    956 ETTIDDLpisstdNEAITISNSIDINYKGLPKKYKEnNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVI 1035
Cdd:pfam05483  334 EAQMEEL------NKAKAAHSFVVTEFEATTCSLEE-LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE 406

                          330       340
                   ....*....|....*....|....*...
gi 14318514   1036 NNETEQLKAEEKKILNQFLKIKKKRKEL 1063
Cdd:pfam05483  407 LEELKKILAEDEKLLDEKKQFEKIAEEL 434
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
711-867 7.33e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  711 REVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIE-KEIQPKITELKKKLDDLENTKD---NLVKEKEALQN 786
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEelrELEEELEELEA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  787 NIfkeftskigftiKEYENHSGELMRQQS----KELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKS 862
Cdd:COG4717  171 EL------------AELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238


                 ....*
gi 14318514  863 LEEQE 867
Cdd:COG4717  239 AALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 691-890 7.68e-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: 42.60  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  691 KLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKeiqpkiteLKKKLDDL 770
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--------YEEQLGNV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  771 ENTKD--NLVKEKEALQnnifkeftskigftikeyenhsgelmrqqsKELQQLQKQILTVENKLQFETDRLSTTQRRYEK 848
Cdd:COG1579   86 RNNKEyeALQKEIESLK------------------------------RRISDLEDEILELMERIEELEEELAELEAELAE 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 14318514  849 AQKDLENAQVEmksLEEQEYAIEMKIGSIESKLEEHKNHLDE 890
Cdd:COG1579  136 LEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
AAA_23 pfam13476
AAA domain;
7-150 1.09e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 41.71  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      7 LELSNFKSYRGVTkVGFgESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGVLNdensddydnegaAS 86
Cdd:pfam13476    1 LTIENFRSFRDQT-IDF-SKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRI------------GL 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14318514     87 SNPQSAYVKAFYQKGNK-----LVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVF 150
Cdd:pfam13476   67 EGKGKAYVEITFENNDGrytyaIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLV 135
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 1129-1189 1.13e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 41.74  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318514 1129 LSGGEKTVAALALLFAINsyqPSpFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVIS 1189
Cdd:cd03217  105 FSGGEKKRNEILQLLLLE---PD-LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIT 161
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
 25-127 1.53e-03

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (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 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 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: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 41.80  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   25 ESNFTSIIGPNGSGKSNMMDAISFVLGVRSNH--LRSNILKDLIyrgvlndENSDDYDNEgaassNPQSAYVKAFYQKGN 102
Cdd:cd03241   20 EEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVV-------EGVFDISDE-----EEAKALLLELGIEDD 87

                         90       100
                 ....*....|....*....|....*
gi 14318514  103 KLVELMRIISRNGDTSYKIDGKTVS 127
Cdd:cd03241   88 DDLIIRREISRKGRSRYFINGQSVT 112
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 1130-1171 1.60e-03

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: 41.43  E-value: 1.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 14318514 1130 SGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRI 1171
Cdd:cd03277  128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKV 169
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
754-932 1.63e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  754 KEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSK-IGFTIKEYENHSGEL--MRQQSKELQQLQKQILTVEN 830
Cdd:COG4913  620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELerLDASSDDLAALEEQLEELEA 699

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  831 KLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQ-EYAIEMKIGSIESKLEEhknHLDELQKKfvtkqselNSSEDIL 909
Cdd:COG4913  700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlEAAEDLARLELRALLEE---RFAAALGD--------AVERELR 768

                        170       180
                 ....*....|....*....|...
gi 14318514  910 EDMNSNLQVLKRERDGIKEDIEK 932
Cdd:COG4913  769 ENLEERIDALRARLNRAEEELER 791
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
819-1046 1.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  819 QQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMK--SLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFV 896
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  897 TKQSELNSSEDILEDMNSNLQVlkrerDGIKEDIEKFDLERVTALKNCKISNINIpISSETTIDDLpISSTDNEAITISN 976
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNHPDV-IALRAQIAAL-RAQLQQEAQRILA 316

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318514  977 SIDINYKGLpkKYKENNTDSARKELEQKIheveEILNELQPNARALER-YDEAEGRFEVINNETEQLKAEE 1046
Cdd:COG3206  317 SLEAELEAL--QAREASLQAQLAQLEARL----AELPELEAELRRLEReVEVARELYESLLQRLEEARLAE 381
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
221-397 1.96e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  221 EEYRKQLDKK-NELQKFQALWQLYHLEQQKEELTDKLSALNSEISSLKGKIN---------NEMKSLQRSKSSFVKESAV 290
Cdd:COG3206  185 PELRKELEEAeAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAeaearlaalRAQLGSGPDALPELLQSPV 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  291 ISKQKSKLDyifkDKEKLVSDLRLIKVPQ----QAAGKRISHIEKRIES-LQKDLQRQKTYVERFETQLKVVTRSKEAFE 365
Cdd:COG3206  265 IQQLRAQLA----ELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLE 340

                        170       180       190
                 ....*....|....*....|....*....|..
gi 14318514  366 EEIKQSARNYDKFKLNENDLKTYNCLHEKYLT 397
Cdd:COG3206  341 ARLAELPELEAELRRLEREVEVARELYESLLQ 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 241-438 2.34e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  241 QLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDyifKDKEKLVSDLRLikvpQQ 320
Cdd:COG3883   24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---ERREELGERARA----LY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  321 AAGKRISHIE------------KRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLkty 388
Cdd:COG3883   97 RSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--- 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 14318514  389 nclhEKYLTEggsiLEEKIAVLNNDKREIQEELERFNKRADISKRRITEE 438
Cdd:COG3883  174 ----EAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 28-61 2.45e-03

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: 41.61  E-value: 2.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 14318514     28 FTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNI 61
Cdd:pfam13304    1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTD 34
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 746-935 2.65e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.75  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   746 KYHndLIEKEIQPKITELKKKLDDLENTKDNLvKEKEALQNNifKEFTSKIG--FTIKEYENHSGELMRQQSKELQQLQK 823
Cdd:PRK04778  246 GYH--LDHLDIEKEIQDLKEQIDENLALLEEL-DLDEAEEKN--EEIQERIDqlYDILEREVKARKYVEKNSDTLPDFLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   824 QILTVENKLQFETDRLsttQRRYEKAQKDLENAQV---EMKSLEEQEYAIEMKIG-------SIESKLEEHKNHLDELQK 893
Cdd:PRK04778  321 HAKEQNKELKEEIDRV---KQSYTLNESELESVRQlekQLESLEKQYDEITERIAeqeiaysELQEELEEILKQLEEIEK 397

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14318514   894 KFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDL 935
Cdd:PRK04778  398 EQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNL 439
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 7-367 2.67e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514      7 LELSNFKSYRGVTKVGFG-ESNFTSIIGPNGSGKSNMMDAISFVL----GVRSNHLRSniLKDLIYRGVLNDENSDDYDN 81
Cdd:TIGR00618    6 LTLKNFGSYKGTHTIDFTaLGPIFLICGKTGAGKTTLLDAITYALygklPRRSEVIRS--LNSLYAAPSEAAFAELEFSL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514     82 EGAASSNPQSAYVKAFYQKGNKLVELmRIISRNGDTSYKIDGK--------TVSYKDYSIFlenenilikAKNFLVFQGD 153
Cdd:TIGR00618   84 GTKIYRVHRTLRCTRSHRKTEQPEQL-YLEQKKGRGRILAAKKseteevihDLLKLDYKTF---------TRVVLLPQGE 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    154 VEQIAAQSPVELSRMFEEVSGSIQYKKEyeelkekieklsksATESIKNRRRIHGE----------LKTYKEGINKNEEY 223
Cdd:TIGR00618  154 FAQFLKAKSKEKKELLMNLFPLDQYTQL--------------ALMEFAKKKSLHGKaelltlrsqlLTLCTPCMPDTYHE 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    224 RKQLDKKNELQKFQALWQlyhLEQQKEELTDKLSALNSeisslKGKINNEMKSLQRSKSSFVKESAVISKQKSKLdyifk 303
Cdd:TIGR00618  220 RKQVLEKELKHLREALQQ---TQQSHAYLTQKREAQEE-----QLKKQQLLKQLRARIEELRAQEAVLEETQERI----- 286

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318514    304 dkeklvsDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEE 367
Cdd:TIGR00618  287 -------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 1128-1180 2.89e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 40.63  E-value: 2.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 14318514  1128 YLSGGEKTVAALALLFAINSyqpsPFFVLDEVDAALDITNVQRIAAYIRRHRN 1180
Cdd:PRK13539  127 YLSAGQKRRVALARLLVSNR----PIWILDEPTAALDAAAVALFAELIRAHLA 175
Tht1 pfam04163
Tht1-like nuclear fusion protein;
683-933 2.94e-03

Tht1-like nuclear fusion protein;


Pssm-ID: 282073  Cd Length: 595  Bit Score: 41.74  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    683 QSLMSLKDKLLIQIDELSNGQRSNSIRAREV-ENSVSLLNSDIANLRTQVTQQKRSLDENRLEikyhndliEKEIQPKIT 761
Cdd:pfam04163  195 QDFENFLDDLAQMFDKFDGEFNNATESNRIIiENDFKDFNFKVNDEIMGLVELENHEQEGMVL--------EKEIIEKIK 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    762 ELKKKLDDLENTKDNLVKEKEALQNNIFK-----EFTSKIGFTIKEYENHSGELMRQQSKELQQLqkqILTVENKLQfet 836
Cdd:pfam04163  267 QLKNEIDDIHHFFADFADELAGYKNDIIEkindlKDDSENAIALSAIGKYTSEFSAFMEKNIKDL---IEMSEDSLK--- 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    837 drlsttqrryEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKN--HLDELQKKfvtkqSELNSsedILEDMNS 914
Cdd:pfam04163  341 ----------ESVQRNIDFVNSGFQELEDFSIGLKEELGGLKKDLSEQQNleAEEILQWK-----SDFLN---ILHDHLK 402

                          250
                   ....*....|....*....
gi 14318514    915 NLQVLKRERDGIKEDIEKF 933
Cdd:pfam04163  403 VLQQLPPLIDEIVPEMEKF 421
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 733-931 3.15e-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: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    733 QQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENtkdnlvKEKEALQNNIFKeftskigftIKEYENHSGELMR 812
Cdd:pfam17380  388 QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA------EQEEARQREVRR---------LEEERAREMERVR 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    813 QQSKELQQlqkqilTVENKLQFETDR----LSTTQRRYEKAQKDLENAQVEMKSLEEQEYAI---EMKIGSIESKLEEHK 885
Cdd:pfam17380  453 LEEQERQQ------QVERLRQQEEERkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMieeERKRKLLEKEMEERQ 526

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 14318514    886 NHLDELQKKFVT-----KQSELNSSEDILEDM------NSNLQVLKRERDGIKEDIE 931
Cdd:pfam17380  527 KAIYEEERRREAeeerrKQQEMEERRRIQEQMrkateeRSRLEAMEREREMMRQIVE 583
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 324-487 3.32e-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: 40.68  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  324 KRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKF--KLNE-NDLKTYNCL-HEKylteg 399
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeQLGNvRNNKEYEALqKEI----- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  400 gSILEEKIAVLNNDKREIQEELERFNKRADiskrRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIE 479
Cdd:COG1579   99 -ESLKRRISDLEDEILELMERIEELEEELA----ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173


                 ....*...
gi 14318514  480 SANNQEYD 487
Cdd:COG1579  174 PELLALYE 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 204-465 3.56e-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: 41.64  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    204 RRIHGELKTYK-EGINKNEEYRKQLDKKNE-LQKFQALwqLYHLEQQKEEL---TDKLSALNSEISSLKGKINNEMKSLQ 278
Cdd:pfam15921  429 QRLEALLKAMKsECQGQMERQMAAIQGKNEsLEKVSSL--TAQLESTKEMLrkvVEELTAKKMTLESSERTVSDLTASLQ 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    279 RSKSSFVKESAVISKQKSKLDYIFKDKEKLVSD---LRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLK 355
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    356 VVTRSKEAFEEEIKQSARNYDKFKL--NENDLKTYNC--------LHEKYLTEGGS--------ILEEKIAVLNNDKREi 417
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELearvsdleLEKVKLVNAGSerlravkdIKQERDQLLNEVKTS- 665

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 14318514    418 QEELERFNKRADISKRRI---TEELSITGEKLDTQLNDLRVSLNE-KNALHT 465
Cdd:pfam15921  666 RNELNSLSEDYEVLKRNFrnkSEEMETTTNKLKMQLKSAQSELEQtRNTLKS 717
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 858-1065 3.57e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   858 VEMKSLEEQEYAieMKIGSIESKLEEHKNHLDELQ---KKFVTKQSELN-----SSEDILEDMNSNLQVLKRERDGIKED 929
Cdd:PRK05771   31 VHIEDLKEELSN--ERLRKLRSLLTKLSEALDKLRsylPKLNPLREEKKkvsvkSLEELIKDVEEELEKIEKEIKELEEE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   930 IEKFDlERVTALKNCK-----ISNINIPIS---------------SETTIDDLPISSTDNEAITISNSIDINYKGL--PK 987
Cdd:PRK05771  109 ISELE-NEIKELEQEIerlepWGNFDLDLSlllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVvvLK 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14318514   988 KYKenntDSARKELeqKIHEVEEIlnELQPNARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFE 1065
Cdd:PRK05771  188 ELS----DEVEEEL--KKLGFERL--ELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLE 257
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 23-54 3.67e-03

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: 39.54  E-value: 3.67e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 14318514   23 FGESNFTSIIGPNGSGKSNMMDAISFVLGVRS 54
Cdd:cd00267   22 LKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS 53
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
711-1042 3.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   711 REVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEkEIQPKITELKKKLD-------DLENTKDNLVKEKEA 783
Cdd:PRK02224  247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEAGlddadaeAVEARREELEDRDEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   784 LQNNIFKEFTSKIGFT---------IKEYENHSGELMRQQS---KELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQK 851
Cdd:PRK02224  326 LRDRLEECRVAAQAHNeeaeslredADDLEERAEELREEAAeleSELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   852 DLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQK-----KFVTKQSELNSSE--DILEDMNSNLQVLKRERD 924
Cdd:PRK02224  406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagKCPECGQPVEGSPhvETIEEDRERVEELEAELE 485

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   925 GIKEDIEKFD--LERVTALKnckisninipiSSETTIDDLpisstDNEAITISNSIDINYKGLPKKYKENNTDSARK-EL 1001
Cdd:PRK02224  486 DLEEEVEEVEerLERAEDLV-----------EAEDRIERL-----EERREDLEELIAERRETIEEKRERAEELRERAaEL 549

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 14318514  1002 EQKIHEVEEILNELQPNA-RALERYDEAEGRFEVINNETEQL 1042
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESL 591
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 194-1103 3.82e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    194 KSATESIKNRR--------RIHGELKTYKEGINKNEEYRKQ-----LDKKNELQKFQALWQLYHLEQQKEELTDKLSALN 260
Cdd:TIGR01612  927 ENTKESIEKFHnkqnilkeILNKNIDTIKESNLIEKSYKDKfdntlIDKINELDKAFKDASLNDYEAKNNELIKYFNDLK 1006

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    261 SEISSLKGK-INNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKdkeklVSDLRLIKVPQQAAGKRISHIEKRIeslQKD 339
Cdd:TIGR01612 1007 ANLGKNKENmLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIH-----TSIYNIIDEIEKEIGKNIELLNKEI---LEE 1078

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    340 LQRQKTYVERFETQLKVVTRSKEAFEEEIKQSarnyDKFKLNENDLKTYNCLHEKYLTEggsiLEEkiaVLNNDKREIQE 419
Cdd:TIGR01612 1079 AEINITNFNEIKEKLKHYNFDDFGKEENIKYA----DEINKIKDDIKNLDQKIDHHIKA----LEE---IKKKSENYIDE 1147

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    420 ELERFNKRADISKRRIT----EELSITGEKLDTQLNDLRVSLNEKNALHTErLHELKKLQSDIESANNQEYDLNFKLRET 495
Cdd:TIGR01612 1148 IKAQINDLEDVADKAISnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKTSLEEVKGINLSYGKNLGKL 1226

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    496 -LVKIDDLSANQRETMKE-RKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKNFDSVIVENLTVAQECIAF 573
Cdd:TIGR01612 1227 fLEKIDEEKKKSEHMIKAmEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK 1306

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    574 LKKQRAGTASFIPLDTIETELPTlSLPDSQDYILSINaidyepeyekamQYVcgdSIICNTLNIAKDLKWKKGI-RGKLV 652
Cdd:TIGR01612 1307 SLKIIEDFSEESDINDIKKELQK-NLLDAQKHNSDIN------------LYL---NEIANIYNILKLNKIKKIIdEVKEY 1370

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    653 TIE--------GALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDklliqIDELSNG--QRSNSIRAREVENSVSLLNS 722
Cdd:TIGR01612 1371 TKEieennkniKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKD-----IDECIKKikELKNHILSEESNIDTYFKNA 1445

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    723 DIANLRTQVTQQKRSLDENRLE--IKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNN--IFKEFTSKIGF 798
Cdd:TIGR01612 1446 DENNENVLLLFKNIEMADNKSQhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNkeLFEQYKKDVTE 1525

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    799 TIKEYE--------NHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYE-------KAQKDLENAQVEMKSL 863
Cdd:TIGR01612 1526 LLNKYSalaiknkfAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEddaakndKSNKAAIDIQLSLENF 1605

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    864 EEQeyaiEMKIGSIESKLEEHKNHLDELQKKFV-----TKQSELNSSEDILEDMNSNLQVLKRERDGIKEdiEKFDLERV 938
Cdd:TIGR01612 1606 ENK----FLKISDIKKKINDCLKETESIEKKISsfsidSQDTELKENGDNLNSLQEFLESLKDQKKNIED--KKKELDEL 1679

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    939 talkNCKISNINIPISSETTIDDLPI--------SSTDNEAITISNSIDINYKGLPKKYKENNTD--SARKELEQKIHEV 1008
Cdd:TIGR01612 1680 ----DSEIEKIEIDVDQHKKNYEIGIiekikeiaIANKEEIESIKELIEPTIENLISSFNTNDLEgiDPNEKLEEYNTEI 1755

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   1009 EEILNELqpnaraLERYDEAEGRFEVINNET---EQLKAEEKKILNQFLK---IKKKRKELFE----KTFDYVSDH---- 1074
Cdd:TIGR01612 1756 GDIYEEF------IELYNIIAGCLETVSKEPityDEIKNTRINAQNEFLKiieIEKKSKSYLDdieaKEFDRIINHfkkk 1829

                          970       980
                   ....*....|....*....|....*....
gi 14318514   1075 LDAIYRELTkNPNSNVELAGGNASLTIED 1103
Cdd:TIGR01612 1830 LDHVNDKFT-KEYSKINEGFDDISKSIEN 1857
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
709-930 3.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   709 RAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHndlieKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNI 788
Cdd:PRK02224  207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH-----EERREELETLEAEIEDLRETIAETEREREELAEEV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   789 --FKEFTSKIGFTIKEYENHSG-ELMRQQSKELQQ--LQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSL 863
Cdd:PRK02224  282 rdLRERLEELEEERDDLLAEAGlDDADAEAVEARReeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14318514   864 EEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDI 930
Cdd:PRK02224  362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 7-47 4.46e-03

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 40.11  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 14318514    7 LELSNF-KSYRGVT-------KVGFGEsnFTSIIGPNGSGKSNMMDAIS 47
Cdd:cd03219    1 LEVRGLtKRFGGLValddvsfSVRPGE--IHGLIGPNGAGKTTLFNLIS 47
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
319-524 4.91e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  319 QQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTrskeafeeeikqsarnydkfklnendlktynclhekyLTE 398
Cdd:COG3206  170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-------------------------------------LSE 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  399 GGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGE--------KLDTQLNDLRVSLNEKNALHTERLHE 470
Cdd:COG3206  213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSARYTPNHPD 292

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14318514  471 LKKLQSDIESANNQeydlnfkLRETLVKIDDLSANQRETMKERK--LRENIAMLKR 524
Cdd:COG3206  293 VIALRAQIAALRAQ-------LQQEAQRILASLEAELEALQAREasLQAQLAQLEA 341
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 31-47 5.46e-03

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443710 [Multi-domain]  Cd Length: 250  Bit Score: 40.10  E-value: 5.46e-03
                         10
                 ....*....|....*..
gi 14318514   31 IIGPNGSGKSNMMDAIS 47
Cdd:COG4674   41 IIGPNGAGKTTLMDVIT 57
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 721-931 6.71e-03

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: 40.65  E-value: 6.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    721 NSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQ---PKITELKKKLDDLENTKDNLVKEKEALQnnifkeftskig 797
Cdd:pfam07888   54 NRQREKEKERYKRDREQWERQRRELESRVAELKEELRqsrEKHEELEEKYKELSASSEELSEEKDALL------------ 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    798 ftikEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRL--STTQRRYEKAQKdlENAQVEMKSLEEQEYAIEMKIG 875
Cdd:pfam07888  122 ----AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAkkAGAQRKEEEAER--KQLQAKLQQTEEELRSLSKEFQ 195

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14318514    876 SIESKLEEHKNHLDELQKKFVTKQSELNS-------SEDILEDMNSNLQVL---KRERDGIKEDIE 931
Cdd:pfam07888  196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeNEALLEELRSLQERLnasERKVEGLGEELS 261
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
286-485 6.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  286 KESAVISKQKSKLDYIFKDK-EKLVSDLRLIKVPQ---QAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKV--VTR 359
Cdd:COG4717   53 KEADELFKPQGRKPELNLKElKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQ 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514  360 SKEAFEEEIKQSARNYDKFKLNENDLKTynclhekylteggsiLEEKIAVLNNDKREIQEELERFNKRADISKRRITEEL 439
Cdd:COG4717  133 ELEALEAELAELPERLEELEERLEELRE---------------LEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 14318514  440 SITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQE 485
Cdd:COG4717  198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 246-937 7.12e-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: 40.77  E-value: 7.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    246 EQQKEELTDKLSALNSEISSLKGKI---NNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKlvsDLRLIKVPQQAA 322
Cdd:TIGR04523   67 EEKINNSNNKIKILEQQIKDLNDKLkknKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEK---QKKENKKNIDKF 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    323 GKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHeKYLTEGGSI 402
Cdd:TIGR04523  144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISE 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    403 LEEKIAVLNNDKREIQEELERFNKRADISKRRITEeLSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESAN 482
Cdd:TIGR04523  223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    483 NQ-EYDLNFKLRETLVKIDdlsaNQRETMkERKLRENIAMLKRFFPGVKGLvhdlchpKKEKYGLavstilgKNFDSVIV 561
Cdd:TIGR04523  302 NQkEQDWNKELKSELKNQE----KKLEEI-QNQISQNNKIISQLNEQISQL-------KKELTNS-------ESENSEKQ 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    562 ENLTVAQECIAFLKKQRAGTasfipLDTIETelptlslpdsqdyiLSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDL 641
Cdd:TIGR04523  363 RELEEKQNEIEKLKKENQSY-----KQEIKN--------------LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    642 KWKKGIRGKLVTIEGAlihkaglmtGGISGDANNRWDKE-EYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLL 720
Cdd:TIGR04523  424 LEKEIERLKETIIKNN---------SEIKDLTNQDSVKElIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    721 NSDIANLrtqvTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSKIGFTI 800
Cdd:TIGR04523  495 EKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    801 KEYENHSGELMRQQSK---ELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSI 877
Cdd:TIGR04523  571 EELKQTQKSLKKKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514    878 ESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERdgIKEDIEKFDLER 937
Cdd:TIGR04523  651 KETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKY--ITRMIRIKDLPK 708
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
7-51 7.40e-03

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 39.98  E-value: 7.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 14318514    7 LELSNFKSYRGVTkVGFGE-SNFTSIIGPNGSGKSNMMDAISFVLG 51
Cdd:COG3950    6 LTIENFRGFEDLE-IDFDNpPRLTVLVGENGSGKTTLLEAIALALS 50
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 693-906 7.94e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   693 LIQIDELSNGQRSNSIR-----AREVENSVSLLNSDIANLRT----QVTQQKRSLDEnrleIKYHNDLIEKEIQPKITEL 763
Cdd:PRK05771   30 VVHIEDLKEELSNERLRklrslLTKLSEALDKLRSYLPKLNPlreeKKKVSVKSLEE----LIKDVEEELEKIEKEIKEL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   764 KKKLDDLENTKDNLVKEKEALQnnIFKEFTSKIgftIKEYENHS-----GELmrqqSKELQQLQKQILTVENKLQFETDR 838
Cdd:PRK05771  106 EEEISELENEIKELEQEIERLE--PWGNFDLDL---SLLLGFKYvsvfvGTV----PEDKLEELKLESDVENVEYISTDK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318514   839 LSTT------QRRYEKAQKDLENAQVEMKSLEEQEY------AIEMKIGSIESKLEEHKNHLDELQKK---FVTKQSELN 903
Cdd:PRK05771  177 GYVYvvvvvlKELSDEVEEELKKLGFERLELEEEGTpselirEIKEELEEIEKERESLLEELKELAKKyleELLALYEYL 256


                  ...
gi 14318514   904 SSE 906
Cdd:PRK05771  257 EIE 259
 
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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