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Conserved domains on  [gi|110347418|ref|NP_006435|]
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structural maintenance of chromosomes protein 2 [Homo sapiens]

Protein Classification

chromosome segregation protein SMC( domain architecture ID 12035156)

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

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 ...
2-1167 4.06e-159

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: 505.28  E-value: 4.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463   80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463  156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   562 KLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAF 641
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEM 721
Cdd:pfam02463  635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   722 KTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCA 801
Cdd:pfam02463  715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   802 KTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam02463  795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   882 ITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNN 961
Cdd:pfam02463  875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   962 PKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463  955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....*..
gi 110347418  1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2-1167 4.06e-159

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: 505.28  E-value: 4.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463   80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463  156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   562 KLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAF 641
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEM 721
Cdd:pfam02463  635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   722 KTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCA 801
Cdd:pfam02463  715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   802 KTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam02463  795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   882 ITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNN 961
Cdd:pfam02463  875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   962 PKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463  955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....*..
gi 110347418  1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-1144 2.23e-127

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: 420.62  E-value: 2.23e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKASV 79
Cdd:TIGR02168    2 LKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAEV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    80 SITFDNSDKkqsPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPP 159
Cdd:TIGR02168   80 ELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQF 239
Cdd:TIGR02168  156 ERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   240 LLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI--------------------LRSL 299
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqkqilrerLANL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   300 EDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQH 379
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   380 FNAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEvkkmdsgyrKDQEALEAVKRLKE 459
Cdd:TIGR02168  395 IASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEALE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   460 KLEAEMKKlnyeenKEESLLEKRRQLSRDIGRLKETyEALLARFPNLRFAYKDPEKN-WNRNCVKGLVASLISVkDTSAT 538
Cdd:TIGR02168  465 ELREELEE------AEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNqSGLSGILGVLSELISV-DEGYE 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   539 TALELVAGERLYNVVVDTEVTGKK---LLERGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVEYKPE 615
Cdd:TIGR02168  537 AAIEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPK 613
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   616 LQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENEL 695
Cdd:TIGR02168  614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   696 RALEEELAGLKntaekyrqlKQQWEMKTEEADLLQTKLQQS-SYHKQQEELDALKKTIEESEETLKNT-KEIQRKAEEKY 773
Cdd:TIGR02168  694 AELEKALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERIAQLsKELTELEAEIE 764
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   774 EVLENKMKNAE--AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYE 851
Cdd:TIGR02168  765 ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   852 SQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 931
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   932 SKMLKDYDWINAER-HLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYN 999
Cdd:TIGR02168  925 AQLELRLEGLEVRIdNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKERYD 1003
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1000 DLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTW 1078
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPPGKK 1083
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  1079 KENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02168 1084 NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
1-172 3.32e-103

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: 326.18  E-value: 3.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273     1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   81 ITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273    81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
                         170
                  ....*....|..
gi 110347418  161 ILSMIEEAAGTR 172
Cdd:cd03273   161 KESLTELSGGQR 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1-1157 6.16e-88

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 306.86  E-value: 6.16e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196     1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   78 SVSITFDNSDKKqSPLGFevhDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196    79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:COG1196   154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGE-LERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  318 DLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEAT 397
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN----YEEN 473
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  474 KEESLLEKRRQLSRDIGRLKETYEALL---ARFPNLRFAYKDPEKNWNRNCVKGLVASLISVkDTSATTALELVAGERLY 550
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  551 NVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTF 628
Cdd:COG1196   550 NIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  629 VCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASiltkfqelkdvqdELRIKENELRALEEELAglknt 708
Cdd:COG1196   628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA----- 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  709 aekyrqlkqqwemkteeadllqtklqqssyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERE 788
Cdd:COG1196   690 -------------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  789 RELKDAQKKLDcaktkadasskkmkEKQQEVEAITLELEELKRehtsykqqleavneaiksyesqievmaaevaknkesv 868
Cdd:COG1196   739 EELLEEEELLE--------------EEALEELPEPPDLEELER------------------------------------- 767
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  869 nkaqeevtkqkevitaqdtvikakyaevakhkeqnndsqlkikeldhniskhkreaedgaakvskmlkdydwinaerhlf 948
Cdd:COG1196       --------------------------------------------------------------------------------
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  949 gqpnsaydfktnnpkeagqRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 1028
Cdd:COG1196   768 -------------------ELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1029 ALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPA 1107
Cdd:COG1196   828 RFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPS 907
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|
gi 110347418 1108 PIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:COG1196   908 PFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
522-639 2.16e-33

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: 125.04  E-value: 2.16e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    522 VKGLVASLISVKDtSATTALELVAGERLYNVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 599
Cdd:smart00968    3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 110347418    600 PDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKV 639
Cdd:smart00968   81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
PTZ00121 PTZ00121
MAEBL; Provisional
165-961 4.36e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 87.50  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  165 IEEAagTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaed 244
Cdd:PTZ00121 1214 AEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------------- 1275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  245 tKVRSAEELKEMQDKviKLQEELSENDKKIKAlnheiEELEKRKDKEtggilRSLEDALAEAQRVNTKSQSAfdlKKKnl 324
Cdd:PTZ00121 1276 -EARKADELKKAEEK--KKADEAKKAEEKKKA-----DEAKKKAEEA-----KKADEAKKKAEEAKKKADAA---KKK-- 1337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  325 aCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmma 404
Cdd:PTZ00121 1338 -AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-------- 1407
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  405 ckNDISKAQTEAKQAQmklkhaqqELKNKQAEVKKMDSGYRKDQE---ALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:PTZ00121 1408 --DELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvkdtsattALELVAGErlynvvvdtEVTGK 561
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK------------------------ADEAKKAE---------EAKKA 1524
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  562 KLLERGELKRRytiiplnkisarciaPETLRVAQNLVGPDNVHVAlslveykPELQKAMEfvfgttfvCDNMDNAKKVAF 641
Cdd:PTZ00121 1525 DEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA-------EELKKAEE--------KKKAEEAKKAEE 1574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  642 DKRIMTRTVTLGGDV----FDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQ 717
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  718 QWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAE----AERERELK- 792
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKa 1732
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  793 -DAQKKLDCAKTKADASSKKMKEK----------QQEVEAITLELEELKREHTSYK--QQLEAVNEAIKSYESQIEVMAA 859
Cdd:PTZ00121 1733 eEAKKEAEEDKKKAEEAKKDEEEKkkiahlkkeeEKKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIE 1812
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  860 EVAKNKESVNKAQE-EVTKQKEVITAQDTVIKaKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV--SKMLK 936
Cdd:PTZ00121 1813 GGKEGNLVINDSKEmEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIE 1891
                         810       820
                  ....*....|....*....|....*
gi 110347418  937 DYDWINAERHLfgqPNSAYDFKTNN 961
Cdd:PTZ00121 1892 KIDKDDIEREI---PNNNMAGKNND 1913
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
680-912 2.72e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  680 ELKDVQDELRIKENELRALEEELAGLKNTaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 759
Cdd:NF033838  175 ELEIAESDVEVKKAELELVKEEAKEPRDE-EKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  760 KNTKEIQRKAEEKYEVL---------ENKMKNAEA------------ERERELKDAQKKLDCAKTKADASSKKMKEKQQE 818
Cdd:NF033838  254 ATSEQDKPKRRAKRGVLgepatpdkkENDAKSSDSsvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPT 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  819 VEAITLELEELKREHTSYKQQLEAVNEAIKSyesqievmaaevAKNKESVNKAQEEVTKQKEVITAQDTVI--KAKYAEV 896
Cdd:NF033838  334 NTYKTLELEIAESDVKVKEAELELVKEEAKE------------PRNEEKIKQAKAKVESKKAEATRLEKIKtdRKKAEEE 401
                         250
                  ....*....|....*.
gi 110347418  897 AKHKEQNNDsqlKIKE 912
Cdd:NF033838  402 AKRKAAEED---KVKE 414
growth_prot_Scy NF041483
polarized growth protein Scy;
663-866 9.44e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  663 LSGGARSQAASILTKFQELKDVQDELRIKENELRAlEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhkqq 742
Cdd:NF041483  420 LKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA-EAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADA----- 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  743 EELDALKKTieESE----ETLKNTKEIQRKAEEKYEvlenkMKNAEAERERelKDAQKKLDCAKTKADASSKKMKEK-QQ 817
Cdd:NF041483  494 DELRSTATA--ESErvrtEAIERATTLRRQAEETLE-----RTRAEAERLR--AEAEEQAEEVRAAAERAARELREEtER 564
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 110347418  818 EVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 866
Cdd:NF041483  565 AIAARQAEAaEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETE 614
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2-1167 4.06e-159

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: 505.28  E-value: 4.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463   80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463  156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   562 KLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAF 641
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   642 DKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEM 721
Cdd:pfam02463  635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   722 KTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCA 801
Cdd:pfam02463  715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   802 KTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam02463  795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   882 ITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNN 961
Cdd:pfam02463  875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   962 PKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463  955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....*..
gi 110347418  1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-1144 2.23e-127

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: 420.62  E-value: 2.23e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKASV 79
Cdd:TIGR02168    2 LKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAEV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    80 SITFDNSDKkqsPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPP 159
Cdd:TIGR02168   80 ELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   160 EILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQF 239
Cdd:TIGR02168  156 ERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   240 LLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI--------------------LRSL 299
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqkqilrerLANL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   300 EDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQH 379
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   380 FNAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEvkkmdsgyrKDQEALEAVKRLKE 459
Cdd:TIGR02168  395 IASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEALE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   460 KLEAEMKKlnyeenKEESLLEKRRQLSRDIGRLKETyEALLARFPNLRFAYKDPEKN-WNRNCVKGLVASLISVkDTSAT 538
Cdd:TIGR02168  465 ELREELEE------AEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNqSGLSGILGVLSELISV-DEGYE 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   539 TALELVAGERLYNVVVDTEVTGKK---LLERGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVEYKPE 615
Cdd:TIGR02168  537 AAIEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPK 613
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   616 LQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENEL 695
Cdd:TIGR02168  614 LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   696 RALEEELAGLKntaekyrqlKQQWEMKTEEADLLQTKLQQS-SYHKQQEELDALKKTIEESEETLKNT-KEIQRKAEEKY 773
Cdd:TIGR02168  694 AELEKALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERIAQLsKELTELEAEIE 764
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   774 EVLENKMKNAE--AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYE 851
Cdd:TIGR02168  765 ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   852 SQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 931
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   932 SKMLKDYDWINAER-HLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYN 999
Cdd:TIGR02168  925 AQLELRLEGLEVRIdNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKERYD 1003
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1000 DLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTW 1078
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPPGKK 1083
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  1079 KENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02168 1084 NQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-1168 1.58e-121

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: 404.06  E-value: 1.58e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK-NGQAGITKASVS 80
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    81 ITFDNSDKKqsplgfeVHDEITVTRQVVIGGRNK---YLINGVNANNTRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMK 157
Cdd:TIGR02169   80 VTFKNDDGK-------FPDELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:TIGR02169  152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLK 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   318 DLKKKNL-------ACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSN 390
Cdd:TIGR02169  311 AEKERELedaeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   391 EDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMK 466
Cdd:TIGR02169  391 REKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewkLEQLAADLSKYEQ 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   467 KLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKdpEKNWNRNCVKGLVASLISVKDTSATtALELVAG 546
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE--VLKASIQGVHGTVAQLGSVGERYAT-AIEVAAG 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   547 ERLYNVVVDTEVTGKKLLERgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPDNVHVALSLVEYKPELQKAMEF 622
Cdd:TIGR02169  547 NRLNNVVVEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAFKY 618
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   623 VFGTTFVCDNMDNAKkvafdkRIM--TRTVTLGGDVFDPHGTLSGGARSQAASILTKFQ---ELKDVQDELRIKENELRA 697
Cdd:TIGR02169  619 VFGDTLVVEDIEAAR------RLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaELQRLRERLEGLKRELSS 692
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   698 LEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLE 777
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   778 ---NKMKNAEAERERELKDAQKKldcaktKADASSKKMKEKQQEVEAITLELE-ELKREHTSyKQQLEavnEAIKSYESQ 853
Cdd:TIGR02169  772 edlHKLEEALNDLEARLSHSRIP------EIQAELSKLEEEVSRIEARLREIEqKLNRLTLE-KEYLE---KEIQELQEQ 841
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   854 IEvmaaEVAKNKESVNKAQEEVTKQKEVItaqDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSK 933
Cdd:TIGR02169  842 RI----DLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   934 MLKDYDWINAERHLFGQPNSAYDFKTNNPKE---AGQRLQKLQEMKEKLGRN------VNMRAMNVLTEAEERYNDLMKK 1004
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEiralepVNMLAIQEYEEVLKRLDELKEK 994
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1005 KRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGanamlappEGQTVLD--------GLEFKVALGN 1076
Cdd:TIGR02169  995 RAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGG--------TGELILEnpddpfagGLELSAKPKG 1066
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  1077 TWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA-NV 1155
Cdd:TIGR02169 1067 KPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAdRA 1146
                         1210
                   ....*....|...
gi 110347418  1156 LFKTKFVDGVSTV 1168
Cdd:TIGR02169 1147 IGVTMRRNGESQV 1159
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
1-172 3.32e-103

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: 326.18  E-value: 3.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273     1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   81 ITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273    81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
                         170
                  ....*....|..
gi 110347418  161 ILSMIEEAAGTR 172
Cdd:cd03273   161 KESLTELSGGQR 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1-1157 6.16e-88

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 306.86  E-value: 6.16e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196     1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   78 SVSITFDNSDKKqSPLGFevhDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196    79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAY 237
Cdd:COG1196   154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGE-LERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  238 QFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkDKETGGILRSLEDALAEAQRVNTKSQSAF 317
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  318 DLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEAT 397
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN----YEEN 473
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  474 KEESLLEKRRQLSRDIGRLKETYEALL---ARFPNLRFAYKDPEKNWNRNCVKGLVASLISVkDTSATTALELVAGERLY 550
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  551 NVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTF 628
Cdd:COG1196   550 NIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  629 VCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASiltkfqelkdvqdELRIKENELRALEEELAglknt 708
Cdd:COG1196   628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA----- 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  709 aekyrqlkqqwemkteeadllqtklqqssyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERE 788
Cdd:COG1196   690 -------------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  789 RELKDAQKKLDcaktkadasskkmkEKQQEVEAITLELEELKRehtsykqqleavneaiksyesqievmaaevaknkesv 868
Cdd:COG1196   739 EELLEEEELLE--------------EEALEELPEPPDLEELER------------------------------------- 767
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  869 nkaqeevtkqkevitaqdtvikakyaevakhkeqnndsqlkikeldhniskhkreaedgaakvskmlkdydwinaerhlf 948
Cdd:COG1196       --------------------------------------------------------------------------------
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  949 gqpnsaydfktnnpkeagqRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 1028
Cdd:COG1196   768 -------------------ELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1029 ALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPA 1107
Cdd:COG1196   828 RFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPS 907
                        1130      1140      1150      1160      1170
                  ....*....|....*....|....*....|....*....|....*....|
gi 110347418 1108 PIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:COG1196   908 PFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
1074-1168 2.18e-63

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: 216.01  E-value: 2.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1074 LGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA 1153
Cdd:cd03273   156 MGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNA 235
                          90
                  ....*....|....*
gi 110347418 1154 NVLFKTKFVDGVSTV 1168
Cdd:cd03273   236 NVLFRTRFVDGTSTV 250
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
522-639 2.16e-33

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: 125.04  E-value: 2.16e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    522 VKGLVASLISVKDtSATTALELVAGERLYNVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 599
Cdd:smart00968    3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 110347418    600 PDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKV 639
Cdd:smart00968   81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
1085-1167 5.01e-31

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: 120.49  E-value: 5.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTKFVD 1163
Cdd:cd03239    95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174

                  ....
gi 110347418 1164 GVST 1167
Cdd:cd03239   175 GVST 178
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
3-164 7.86e-29

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: 116.21  E-value: 7.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVYKNGQAGITKASVSIT 82
Cdd:cd03272     1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   83 FDNSDKKqsplgFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIL 162
Cdd:cd03272    80 FDNSDNR-----FPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154

                  ..
gi 110347418  163 SM 164
Cdd:cd03272   155 EM 156
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
3-86 4.15e-26

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: 106.24  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQdLVYKNGQAGITKASVSIT 82
Cdd:cd03239     1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78

                  ....
gi 110347418   83 FDNS 86
Cdd:cd03239    79 FDKS 82
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
3-89 4.57e-25

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: 103.70  E-value: 4.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK--NGQAGITKASVS 80
Cdd:cd03278     1 LKKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVT 79

                  ....*....
gi 110347418   81 ITFDNSDKK 89
Cdd:cd03278    80 LTFDNSDGR 88
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
1081-1157 1.75e-23

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


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 99.46  E-value: 1.75e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:cd03278   110 RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
522-640 4.01e-23

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


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 95.41  E-value: 4.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   522 VKGLVASLISVKDTsATTALELVAGERLYNVVVDTEVTGKKLLErgELKR----RYTIIPLNKISARCIAPETLRVAqnl 597
Cdd:pfam06470    4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIE--FLKKnklgRATFLPLDRLKPRPRRPGADLKG--- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 110347418   598 vgpdNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVA 640
Cdd:pfam06470   78 ----GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
3-159 2.62e-21

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: 94.56  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVY--KNGQAGITKASVS 80
Cdd:cd03275     1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418   81 ITFDNSDKkqsplgfevhdEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:cd03275    79 AVYEDDDG-----------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1082-1167 5.96e-19

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: 85.10  E-value: 5.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1082 LTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03227    75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154

                  ....*...
gi 110347418 1161 FV-DGVST 1167
Cdd:cd03227   155 KViTGVYK 162
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
1081-1168 4.61e-18

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: 85.00  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03272   155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234

                  ....*...
gi 110347418 1161 FVDGVSTV 1168
Cdd:cd03272   235 FRNKVSTI 242
PTZ00121 PTZ00121
MAEBL; Provisional
165-961 4.36e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 87.50  E-value: 4.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  165 IEEAagTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaed 244
Cdd:PTZ00121 1214 AEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------------- 1275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  245 tKVRSAEELKEMQDKviKLQEELSENDKKIKAlnheiEELEKRKDKEtggilRSLEDALAEAQRVNTKSQSAfdlKKKnl 324
Cdd:PTZ00121 1276 -EARKADELKKAEEK--KKADEAKKAEEKKKA-----DEAKKKAEEA-----KKADEAKKKAEEAKKKADAA---KKK-- 1337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  325 aCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmma 404
Cdd:PTZ00121 1338 -AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-------- 1407
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  405 ckNDISKAQTEAKQAQmklkhaqqELKNKQAEVKKMDSGYRKDQE---ALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:PTZ00121 1408 --DELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  482 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvkdtsattALELVAGErlynvvvdtEVTGK 561
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK------------------------ADEAKKAE---------EAKKA 1524
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  562 KLLERGELKRRytiiplnkisarciaPETLRVAQNLVGPDNVHVAlslveykPELQKAMEfvfgttfvCDNMDNAKKVAF 641
Cdd:PTZ00121 1525 DEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA-------EELKKAEE--------KKKAEEAKKAEE 1574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  642 DKRIMTRTVTLGGDV----FDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQ 717
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  718 QWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAE----AERERELK- 792
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKa 1732
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  793 -DAQKKLDCAKTKADASSKKMKEK----------QQEVEAITLELEELKREHTSYK--QQLEAVNEAIKSYESQIEVMAA 859
Cdd:PTZ00121 1733 eEAKKEAEEDKKKAEEAKKDEEEKkkiahlkkeeEKKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIE 1812
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  860 EVAKNKESVNKAQE-EVTKQKEVITAQDTVIKaKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV--SKMLK 936
Cdd:PTZ00121 1813 GGKEGNLVINDSKEmEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIE 1891
                         810       820
                  ....*....|....*....|....*
gi 110347418  937 DYDWINAERHLfgqPNSAYDFKTNN 961
Cdd:PTZ00121 1892 KIDKDDIEREI---PNNNMAGKNND 1913
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
1085-1156 3.27e-16

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


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 79.54  E-value: 3.27e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFT-HSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03275   156 LSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADAL 228
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
3-156 7.32e-16

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: 77.72  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASNLQDLVYK-NGQAGITKASVSI 81
Cdd:cd03274     3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSVEV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347418   82 TFDnsdkkqsplgfEVHDEitvtrqvviggrnkylingvnanntrvqDLFCSVGLNVNNPHFLIMQGRITKVLNM 156
Cdd:cd03274    82 HFQ-----------EIIDK----------------------------PLLKSKGIDLDHNRFLILQGEVEQIAQM 117
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
1078-1156 2.60e-15

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


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 76.18  E-value: 2.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418 1078 WKeNLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03274   122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
5-83 2.97e-14

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: 71.62  E-value: 2.97e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418    5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasnlqdlvYKNGQAGITKASVSITF 83
Cdd:cd03227     1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-203 4.15e-13

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 69.65  E-value: 4.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSqvRASNLQDLVYKngqaGITKASVSI 81
Cdd:COG0419     1 KLLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINV----GSEEASVEL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   82 TFDNSDKkqsplgfevhdEITVTRQvviggrnkylingvnanntrvqdlfcsvglnvnnphflimQGRITKVLNMKPPEI 161
Cdd:COG0419    74 EFEHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSER 102
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110347418  162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI--LEEEI 203
Cdd:COG0419   103 KEALKRLLGLEIYEELKERLKELEEALESALEELAELqkLKQEI 146
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1-913 1.83e-12

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: 71.92  E-value: 1.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     1 MHIKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLLgisnLSQVRASNlQDLVYKNGQAGITKAS 78
Cdd:TIGR00618    1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRS-EVIRSLNSLYAAPSEA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    79 VSITFDNSDKKQSplgFEVHDEITVTR---------QVVI---GGRNKYLINGVNANNTRVQDLfcsvgLNVNNPHF--- 143
Cdd:TIGR00618   75 AFAELEFSLGTKI---YRVHRTLRCTRshrkteqpeQLYLeqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrv 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   144 -LIMQGRITKVLNMKPPEILSMIEEAAGTRMYE---------YKKIAAQKTIEKKEAKL------------KEIKTILEE 201
Cdd:TIGR00618  147 vLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTqlalmefakKKSLHGKAELLTLRSQLltlctpcmpdtyHERKQVLEK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   202 EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHeI 281
Cdd:TIGR00618  227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ-I 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   282 EELEKRKDKETGGILRSLEDALAEAQRVnTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEvKKITDGLHA 361
Cdd:TIGR00618  306 EQQAQRIHTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHT 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   362 LQEASNKDAEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK 439
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   440 MDSGYRKDQEALEAVKRLKEKlEAEMKKLnyEENKEESLLEKRRQLSrdiGRLKETYEAllarfpnlrfaykdpeknwnr 519
Cdd:TIGR00618  464 SAQSLKEREQQLQTKEQIHLQ-ETRKKAV--VLARLLELQEEPCPLC---GSCIHPNPA--------------------- 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   520 ncvkgLVASLISVKDTSATTALE------LVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISA-RCIAPETLR 592
Cdd:TIGR00618  517 -----RQDIDNPGPLTRRMQRGEqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNLQN 591
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   593 VAQNLvgpdnvhvalslveyKPELQKamefvfgttfvcdNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAA 672
Cdd:TIGR00618  592 ITVRL---------------QDLTEK-------------LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   673 SILTKFQELKDVQDE------LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQ---TKLQQSS--YHKQ 741
Cdd:TIGR00618  644 KLTALHALQLTLTQErvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLReleTHIEEYDreFNEI 723
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   742 QEELDALKKTIEESEETLKNT-KEIQRKAEEKYEVLENKMKNAEaerERELKDAQKKLDCAKTKADasskkMKEKQQEVE 820
Cdd:TIGR00618  724 ENASSSLGSDLAAREDALNQSlKELMHQARTVLKARTEAHFNNN---EEVTAALQTGAELSHLAAE-----IQFFNRLRE 795
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   821 AITLELEELKREHTSYkqqleavneaIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQdtviKAKYAEVAKHK 900
Cdd:TIGR00618  796 EDTHLLKTLEAEIGQE----------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ----LLKYEECSKQL 861
                          970
                   ....*....|...
gi 110347418   901 EQNNDSQLKIKEL 913
Cdd:TIGR00618  862 AQLTQEQAKIIQL 874
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
198-947 2.30e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.87  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  198 ILEE-EITPTIQKLKEERSSYLEYQKVM----REIEHLSRLYIAYQFLLAEDTKVRSAEELKEM------QDKVIKLQEE 266
Cdd:COG4913   217 MLEEpDTFEAADALVEHFDDLERAHEALedarEQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  267 LSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAEA--QRVNtksqsafDLKKknlaceESKRKEleknmvedsKT 344
Cdd:COG4913   297 LEELRAELARLEAELERLEARLD-ALREELDELEAQIRGNggDRLE-------QLER------EIERLE---------RE 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  345 LAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmmackndiskAQTEAKQAQMKLK 424
Cdd:COG4913   354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLR 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  425 HAQQELKNKQAEVKKMDSGYRKDQEALeavkrlkekleaemkklnyeenkeesllekRRQLSRDIGrLKETyeallarfp 504
Cdd:COG4913   419 RELRELEAEIASLERRKSNIPARLLAL------------------------------RDALAEALG-LDEA--------- 458
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  505 NLRFaykdpeknwnrncvkglVASLISVKDTSA--TTALELVAGERLYNVVVDTEVTGK--KLLERGELKRRytiIPLNK 580
Cdd:COG4913   459 ELPF-----------------VGELIEVRPEEErwRGAIERVLGGFALTLLVPPEHYAAalRWVNRLHLRGR---LVYER 518
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  581 ISARCIAPETLRVAQN-LVGpdnvhvalsLVEYKP-ELQKAMEFVFGTTFV---CDNMDNAKKVafdkrimTRTVTLGGD 655
Cdd:COG4913   519 VRTGLPDPERPRLDPDsLAG---------KLDFKPhPFRAWLEAELGRRFDyvcVDSPEELRRH-------PRAITRAGQ 582
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  656 VFDPHGTLSGGARSQAAS-----------ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmktE 724
Cdd:COG4913   583 VKGNGTRHEKDDRRRIRSryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---D 659
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  725 EADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdAQKKLDCAKTK 804
Cdd:COG4913   660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDR 735
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  805 ADASSKKmkekqqEVEAITLELEELKREHtsykQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ-KEVIT 883
Cdd:COG4913   736 LEAAEDL------ARLELRALLEERFAAA----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETA 805
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  884 AQDTVIKA--KYAEV---------AKHKEQ-----NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWiNAERHL 947
Cdd:COG4913   806 DLDADLESlpEYLALldrleedglPEYEERfkellNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF-GPGRYL 884
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1046-1144 1.02e-11

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: 64.19  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1046 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKEN---LTELSGGQRSLVALSLILsmlLFKPaPIYILDEVDAALDLS 1122
Cdd:cd00267    39 STLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRigyVPQLSGGQRQRVALARAL---LLNP-DLLLLDEPTSGLDPA 114
                          90       100
                  ....*....|....*....|...
gi 110347418 1123 HTQNIGQMLRTHF-THSQFIVVS 1144
Cdd:cd00267   115 SRERLLELLRELAeEGRTVIIVT 137
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
668-912 4.10e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.40  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  668 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDA 747
Cdd:PRK03918  196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEE 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  748 LKKTIEESEETLKNTKEIQRKAEE---------KYEVLENKMKNAEAERERELKDAQKKLdcaktkadassKKMKEKQQE 818
Cdd:PRK03918  271 LKKEIEELEEKVKELKELKEKAEEyiklsefyeEYLDELREIEKRLSRLEEEINGIEERI-----------KELEEKEER 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  819 VEAITLELEELKREHTSYKQQLEAVNEAiKSYESQIEVMAAEVA-KNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 897
Cdd:PRK03918  340 LEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
                         250
                  ....*....|....*
gi 110347418  898 KHKEQNNDSQLKIKE 912
Cdd:PRK03918  419 KEIKELKKAIEELKK 433
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-126 6.42e-11

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


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 65.56  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    2 HIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVSI 81
Cdd:COG1195     1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110347418   82 TFDNSDKKqsplgFEVhdEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:COG1195    72 EVERDGRE-----VRL--GLGLSR----GGKKRVRINGKPVRRLS 105
AAA_23 pfam13476
AAA domain;
6-196 6.72e-11

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 62.90  E-value: 6.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:pfam13476    1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    84 DNSDKKQSplgFEVHDEITVTRQVVIGGRNKYL-INGVNANNTRVQDLFCSvgLNVNNPHFLIM-QGRITKVLNMKPPEI 161
Cdd:pfam13476   79 ENNDGRYT---YAIERSRELSKKKGKTKKKEILeILEIDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKEKKER 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 110347418   162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK 196
Cdd:pfam13476  154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
257-509 8.05e-11

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 65.17  E-value: 8.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  257 QDKVIKLQEELSENDKKIKALNHEIEELEKRKdKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLAceeskrkELEK 336
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  337 NMVEDSKTLAAKEKEVKKItdgLHALQEASNKDAEALaaaqqhfnavsagLSSNEDGAEATLAGQMMACKNDISKAQTEA 416
Cdd:COG4942    91 EIAELRAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  417 -KQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEM-KKLNYEENKEESLLEKRRQLSRDIGRLKE 494
Cdd:COG4942   155 lRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEA 234
                         250
                  ....*....|....*
gi 110347418  495 TYEALLARFPNLRFA 509
Cdd:COG4942   235 EAAAAAERTPAAGFA 249
PTZ00121 PTZ00121
MAEBL; Provisional
242-937 8.22e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 8.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  242 AEDtkVRSAEELKEMQDkVIKLQEELSENDKKIKALNHEIEELEKRKdketggILRSLEDAL-AEAQRVNTKSQSAFDLK 320
Cdd:PTZ00121 1124 AED--ARKAEEARKAED-ARKAEEARKAEDAKRVEIARKAEDARKAE------EARKAEDAKkAEAARKAEEVRKAEELR 1194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  321 KknlaCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAvsaGLSSNEDGAEATLAG 400
Cdd:PTZ00121 1195 K----AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE---EIRKFEEARMAHFAR 1267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  401 QMMACKNDISKAQTEAKQAQMKLKHAQ----------QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE-------A 463
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaeekkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaaeA 1347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  464 EMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvKDTSATTALEL 543
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-----------------AEEDKKKADEL 1410
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  544 VAGERLYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAmefv 623
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKK--------------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---- 1472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  624 fgttfvcdnmDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELA 703
Cdd:PTZ00121 1473 ----------DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  704 GLKNTAEKYR---QLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIqrKAEEKYEVLENKM 780
Cdd:PTZ00121 1543 EEKKKADELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKAEEAKI 1620
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  781 KNAEAERERELKdaqKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMA-- 858
Cdd:PTZ00121 1621 KAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKke 1697
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  859 AEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND--SQLKIKELDHNISKHKREAEDGAAKVSKMLK 936
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777

                  .
gi 110347418  937 D 937
Cdd:PTZ00121 1778 E 1778
PTZ00121 PTZ00121
MAEBL; Provisional
667-1030 1.29e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKtEEADLLQTKLQQssyhkqQEELD 746
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEE------KKKAD 1434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  747 ALKKTIEESeetlKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDCAKtKADASSKKMKEKQQEVEAITLEL 826
Cdd:PTZ00121 1435 EAKKKAEEA----KKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAA 1506
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  827 EELKREHTSYKQQLEAVNEAIKSYEsqiEVMAAEVAKNKESVNKAqEEVTKQKEVITAQDTvikaKYAEVAKHKEQNNDS 906
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAE---EAKKADEAKKAEEKKKA-DELKKAEELKKAEEK----KKAEEAKKAEEDKNM 1578
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  907 QLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmR 986
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---------KIKAEELKKAEEEKKKVEQLKKKEAEEKK-K 1648
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 110347418  987 AMNVLTEAEERYNDLMKKKRIVENDKSKI--LTTIEDLDQKKNQAL 1030
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
23-130 3.21e-10

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: 62.22  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   23 FDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASNlqDLVykngQAGITKASVSITFDNSDK-----KQSPLGFEV 97
Cdd:cd03241    19 FEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEeeakaLLLELGIED 86
                          90       100       110
                  ....*....|....*....|....*....|...
gi 110347418   98 HDEITVTRQVVIGGRNKYLINGVNANNTRVQDL 130
Cdd:cd03241    87 DDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1-499 3.35e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrasnLQDLVYKngqaGITKAS 78
Cdd:PRK02224    1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   79 VSITFdnsdkkqSPLGFEVH---------DEITVTRQVVIGGRNkyLINGVNANNTRVQDLfcsvgLNVNNPHFL----I 145
Cdd:PRK02224   70 IELWF-------EHAGGEYHierrvrlsgDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  146 MQGRITKVLNMKPPEILSMIEEAAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------L 192
Cdd:PRK02224  136 RQGEVNKLINATPSDRQDMIDDLLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  193 KEIKTILE--EEITPTIQKLKEERSSYLE-YQKVMREIEHLSRLYIAYQFLLAEDTKVRS--AEELKEMQDKVIKLQEEL 267
Cdd:PRK02224  216 AELDEEIEryEEQREQARETRDEADEVLEeHEERREELETLEAEIEDLRETIAETEREREelAEEVRDLRERLEELEEER 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  268 SE-------NDKKIKALNHEIEELEKRKDketgGILRSLEDALAEAQRVNTKSQS----AFDLKKKNLACEEsKRKELEK 336
Cdd:PRK02224  296 DDllaeaglDDADAEAVEARREELEDRDE----ELRDRLEECRVAAQAHNEEAESlredADDLEERAEELRE-EAAELES 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  337 NMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHfnavSAGLSSNEDGA---EATLAGQMMACKNDISKAq 413
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF----LEELREERDELrerEAELEATLRTARERVEEA- 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  414 tEAKQAQMKLKHAQQELKnkqaevkkmDSGyrkDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLS---RDIG 490
Cdd:PRK02224  446 -EALLEAGKCPECGQPVE---------GSP---HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIE 512

                  ....*....
gi 110347418  491 RLKETYEAL 499
Cdd:PRK02224  513 RLEERREDL 521
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-882 7.78e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGqagiTKASVS 80
Cdd:PRK03918    1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG----SGTEIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   81 ITFDNSDKKqsplgfevhdeITVTRQVVIGgrNKYLINGVNANNTRVQDLFCS------VGLNVNNPHFLIMQGRITKVL 154
Cdd:PRK03918   75 LKFEKNGRK-----------YRIVRSFNRG--ESYLKYLDGSEVLEEGDSSVRewverlIPYHVFLNAIYIRQGEIDAIL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  155 nmkppeilsmieEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEitptIQKLKEERSSYLEYQKVMREiehlsrly 234
Cdd:PRK03918  142 ------------ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKE-------- 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  235 iayqfllAEDTKVRSAEELKEMQDKVIKLQEEL---SENDKKIKALNHEIEELEKRKDKETGGiLRSLEDALAEAQrvnt 311
Cdd:PRK03918  198 -------KEKELEEVLREINEISSELPELREELeklEKEVKELEELKEEIEELEKELESLEGS-KRKLEEKIRELE---- 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  312 ksqsafdlkkKNLACEESKRKELEKNmVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNE 391
Cdd:PRK03918  266 ----------ERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  392 DgaeatlagqMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDsGYRKDQEALEAVKRLKEKLEAEMKKLNYE 471
Cdd:PRK03918  335 E---------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIE 404
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  472 EnKEESLLEKRRQLSRDIGRLKETYEALlarfpnlrfaykdpeKNWNRNCvkglvaslisvkdtsattalelvagerlyn 551
Cdd:PRK03918  405 E-EISKITARIGELKKEIKELKKAIEEL---------------KKAKGKC------------------------------ 438
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  552 vvvdtEVTGKKLLE--RGELKRRYTiIPLNKISA---------RCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAM 620
Cdd:PRK03918  439 -----PVCGRELTEehRKELLEEYT-AELKRIEKelkeieekeRKLRKELRELEKVLKKESELIKLKELAEQLKELEEKL 512
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  621 EFVfgttfvcdNMDNAKKVAFDKRIMTRtvtlggdvfdphgtLSGGARSQAASILTKFQELKDVQDELRIKENELRALEE 700
Cdd:PRK03918  513 KKY--------NLEELEKKAEEYEKLKE--------------KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  701 ELAGLkntaekyrqLKQQWEMKTEEADLLQTKLQQ-SSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENK 779
Cdd:PRK03918  571 ELAEL---------LKELEELGFESVEELEERLKElEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  780 MKnaeaERERELKDAQKKLDcaktkadasskkmkekQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAA 859
Cdd:PRK03918  642 LE----ELRKELEELEKKYS----------------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
                         890       900
                  ....*....|....*....|....*....
gi 110347418  860 EVAKNK------ESVNKAQEEVTKQKEVI 882
Cdd:PRK03918  702 ELEEREkakkelEKLEKALERVEELREKV 730
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
248-913 8.11e-10

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: 63.60  E-value: 8.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   248 RSAEELK-EMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGgILRSLEDALAEAQRVNTKSQSAFD----LKKK 322
Cdd:pfam15921  138 QSQEDLRnQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEG-VLQEIRSILVDFEEASGKKIYEHDsmstMHFR 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   323 NLACEESK-RKELEKNmvedsktLAAKEKEVKKITDGLHALQEASNKDAEALAaaQQHFNAVSAGLSSNEDgaeatlagQ 401
Cdd:pfam15921  217 SLGSAISKiLRELDTE-------ISYLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEV--------E 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   402 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQA----EVKKMDSGYRKDQEALEAVKRLKE-KLEAEMKKLNYEENKEE 476
Cdd:pfam15921  280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELT 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   477 SLLEKRRQLSRDIGRLKETYEALLA----RFPNLRFAYKDPEKNWNRNC-------------------VKGLVASLISVK 533
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMK 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   534 D----------------------TSATTALELVAGERLYNVVvdTEVTGKKL-LERGELKrrytiipLNKISARCIAPET 590
Cdd:pfam15921  440 SecqgqmerqmaaiqgkneslekVSSLTAQLESTKEMLRKVV--EELTAKKMtLESSERT-------VSDLTASLQEKER 510
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   591 LRVAQNL-VGPDNVHVALSLVEYKpELQKAMEFVFGTTFVCD----NMDNAKKVAfdkRIMTRTVTLGGDVFDPHGTLSG 665
Cdd:pfam15921  511 AIEATNAeITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEalklQMAEKDKVI---EILRQQIENMTQLVGQHGRTAG 586
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   666 GARSQAASI----------LTKFQELKDVQDElRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLL-QTKLQ 734
Cdd:pfam15921  587 AMQVEKAQLekeindrrleLQEFKILKDKKDA-KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnEVKTS 665
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   735 QSSYHKQQEELDALKKTI----EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDA---QKKLDCAKTKADA 807
Cdd:pfam15921  666 RNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDA 745
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   808 SSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDT 887
Cdd:pfam15921  746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
                          730       740
                   ....*....|....*....|....*.
gi 110347418   888 VIKAKYAEVAKHKEQNNdsqLKIKEL 913
Cdd:pfam15921  826 IIQRQEQESVRLKLQHT---LDVKEL 848
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
668-1025 9.77e-10

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 62.92  E-value: 9.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   668 RSQAASILTKFQELKDvqdELRIKENELRALEEELAGLKNTAEKYRQ----LKQQWEMKTEEADLLQTklqqssyhkqqe 743
Cdd:pfam10174  281 KSHSKFMKNKIDQLKQ---ELSKKESELLALQTKLETLTNQNSDCKQhievLKESLTAKEQRAAILQT------------ 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   744 ELDALKKTIEESEETL-KNTKEIQRKAEE--------------------KYEVLENKMKN-AEAERERE-----LKDAQK 796
Cdd:pfam10174  346 EVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirdlkdmldvkerKINVLQKKIENlQEQLRDKDkqlagLKERVK 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   797 KLDCAKTKADASSKKMKEKQQEVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV 875
Cdd:pfam10174  426 SLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   876 TKQKEVITAQDTVIKAKYAEVAKHKEQ--------------------NNDSQLKIKELDHNISKHKREAEDGAAKVSKML 935
Cdd:pfam10174  506 SSLASSGLKKDSKLKSLEIAVEQKKEEcsklenqlkkahnaeeavrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLL 585
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   936 ------------KDYDWINAE----RHLFGQPNSAYDFKTNNPKEagqRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYN 999
Cdd:pfam10174  586 gilrevenekndKDKKIAELEsltlRQMKEQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
                          410       420
                   ....*....|....*....|....*.
gi 110347418  1000 DLMKKKRIVENDKSKILTTIEDLDQK 1025
Cdd:pfam10174  663 ALEKTRQELDATKARLSSTQQSLAEK 688
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
677-839 1.35e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.48  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  677 KFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQ-QSSYHKQQEELDALKKTIEES 755
Cdd:COG4717    79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEELEERLEEL 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  756 EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTS 835
Cdd:COG4717   159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238

                  ....
gi 110347418  836 YKQQ 839
Cdd:COG4717   239 AALE 242
recF PRK00064
recombination protein F; Reviewed
1-123 2.96e-09

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 60.17  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVS 80
Cdd:PRK00064    1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110347418   81 ITFDNSdkkqsplGFEVHDEITVTRQvvigGRNKYLINGVNAN 123
Cdd:PRK00064   72 GRVEKG-------GRELPLGLEIDKK----GGRKVRINGEPQR 103
PTZ00121 PTZ00121
MAEBL; Provisional
160-925 3.76e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  160 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKVMREIEHLSRLYIAYQ 238
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARK 1171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  239 fllAEDTK----------VRSAEELKEMQDKVIKLQEELSENDKKIkalnheiEELEKRKDKETGGILRSLEDALAEAqr 308
Cdd:PTZ00121 1172 ---AEDAKkaeaarkaeeVRKAEELRKAEDARKAEAARKAEEERKA-------EEARKAEDAKKAEAVKKAEEAKKDA-- 1239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  309 vntksqsafdlkkknlacEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEasnKDAEALAAAQQHFNAVSAGLS 388
Cdd:PTZ00121 1240 ------------------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKAEEKKKADEAKKA 1298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  389 SNEDGAEatlagqmmacknDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKL 468
Cdd:PTZ00121 1299 EEKKKAD------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  469 NYEENKEESLLEKRRQLSRDIGRLKETYEAllarfpnLRFAYKDPEKnwnrncvkglvASLISVKDTSATTALELVAGER 548
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEA-------KKKAEEDKKK-----------ADELKKAAAAKKKADEAKKKAE 1428
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  549 LYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciaPETLRVAQNLV-GPDNVHVALSLVEYKPELQKAMEFVFGTT 627
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKK---------------AEEAKKAEEAKkKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  628 FVCDNMDNAKKVAFDKRIMTRTVTlgGDVFDPHGTLSGGARSQAASILTKFQELKDVqDELRiKENELRALEEelaglKN 707
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELK-KAEELKKAEE-----KK 1564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  708 TAEKYRQLKQQWEMKTEEADLLQT--KLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLEnKMKNAEA 785
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEA 1643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  786 ERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNK 865
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKA 1718
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAE 925
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
3-95 6.97e-09

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


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 56.84  E-value: 6.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03276     1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
                          90
                  ....*....|...
gi 110347418   83 FDNSDKKQSPLGF 95
Cdd:cd03276    75 LKNQGLDANPLCV 87
COG4637 COG4637
Predicted ATPase [General function prediction only];
3-97 7.38e-09

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 59.17  E-value: 7.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL--LGISNLSQVRASN--LQDLVYKNGQAGITKAS 78
Cdd:COG4637     2 ITRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITEPIR 78
                          90
                  ....*....|....*....
gi 110347418   79 VSITFDNSDkkQSPLGFEV 97
Cdd:COG4637    79 LELEFAEED--ERDLRYEL 95
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
3-109 1.33e-08

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: 56.46  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASNLQDLVYKngqaGITKASVSI 81
Cdd:cd03240     1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
                          90       100
                  ....*....|....*....|....*...
gi 110347418   82 TFDNSDKKQsplgFEVHDEITVTRQVVI 109
Cdd:cd03240    76 AFENANGKK----YTITRSLAILENVIF 99
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
1-84 3.09e-08

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: 57.32  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLqdlvYKNGQAGITKASVS 80
Cdd:COG3593     1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDF----YLGDDPDLPEIEIE 74

                  ....
gi 110347418   81 ITFD 84
Cdd:COG3593    75 LTFG 78
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
744-898 4.99e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 55.32  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  744 ELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKkmkekQQEVE 820
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-----NKEYE 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347418  821 AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 898
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
689-860 5.83e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  689 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKL----QQSSYHKQQEELDALKKTIEESEETLKNTKE 764
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  765 IQRKAEEKYEVLENKMkNAEAERERELKDAQKKLDCAKTKADASSKK-MKEKQQEVEAITLELEELKREHTSYKQQLEAV 843
Cdd:COG4717   147 RLEELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEEL 225
                         170
                  ....*....|....*..
gi 110347418  844 NEAIKSYESQIEVMAAE 860
Cdd:COG4717   226 EEELEQLENELEAAALE 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
669-1142 6.14e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  669 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYH---KQQEEL 745
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEEL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  746 DALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKK---------------------------- 797
Cdd:COG4717   202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlfl 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  798 ----LDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQE 873
Cdd:COG4717   282 vlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  874 EV------TKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 947
Cdd:COG4717   362 ELqleeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  948 fgqpnsaydfktnnpKEAGQRLQKL-QEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:COG4717   442 ---------------EELEEELEELrEELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1027 NQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEgqtvldGLEFKVALGNTWKENLTELSGGQRSLVALSL---ILSMLL 1103
Cdd:COG4717   507 EEYREERLPPVLERASEYFSRLTDGRYRLIRIDE------DLSLKVDTEDGRTRPVEELSRGTREQLYLALrlaLAELLA 580
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 110347418 1104 FKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIV 1142
Cdd:COG4717   581 GEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIY 618
PTZ00121 PTZ00121
MAEBL; Provisional
677-1026 1.65e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  677 KFQELKDVQDELRIKENELRALEEelagLKNTAEKYRQlKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESE 756
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  757 ETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADA-SSKKMKEKQQEVEAITLE---------- 825
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEekkkadelkk 1553
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  826 ------------LEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQKEVITAQDTVI 889
Cdd:PTZ00121 1554 aeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKK 1633
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  890 KAKYAEVAKHKEQNNDSQLKIKELDHNISKH--KREAEDGAAKVSKMLKDYDwinAERHlfgqpnsaydfKTNNPKEAGQ 967
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEE---DEKK-----------AAEALKKEAE 1699
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418  968 RLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
678-1029 1.70e-07

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 55.47  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   678 FQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmkteeadllqtklqqsSYHKQQEELDALKKTIEESEE 757
Cdd:pfam05622   96 VLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVE----------------TYKKKLEDLGDLRRQVKLLEE 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   758 tlKNTKEIQRKAEekyevLENKMKNAEAER------ERELKDAQKKLDCAKTKADA---SSKKMKEK----QQEVEAITL 824
Cdd:pfam05622  160 --RNAEYMQRTLQ-----LEEELKKANALRgqletyKRQVQELHGKLSEESKKADKlefEYKKLEEKlealQKEKERLII 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   825 E-------LEELKREHTSYKQQLEAVNEAIKSYESqIEVMAAEV--AKNKESVNKAQEEvtkQKEVITAQDTVIKAKYAE 895
Cdd:pfam05622  233 ErdtlretNEELRCAQLQQAELSQADALLSPSSDP-GDNLAAEImpAEIREKLIRLQHE---NKMLRLGQEGSYRERLTE 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   896 VAKH-----------KEQNNDSQLKIKELDHNISKHKRE-------AEDGAAKVSKMLKDYDWINaERHLFGQPNSAYdF 957
Cdd:pfam05622  309 LQQLledanrrknelETQNRLANQRILELQQQVEELQKAlqeqgskAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQ-I 386
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418   958 KTNNPKEAGQRLQKLQEMKEKL-GRNVNMRAMnvlteaEERYndlmkkKRIVENDKSKILTtiedLDQKKNQA 1029
Cdd:pfam05622  387 EELEPKQDSNLAQKIDELQEALrKKDEDMKAM------EERY------KKYVEKAKSVIKT----LDPKQNPA 443
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
664-1031 1.82e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.89  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   664 SGGARSQAASILTkfqELKDVQDELRIKEN----ELRALEEELAGLKNtaeKYRQLKQQWEMKTEE---------ADLLQ 730
Cdd:pfam15921  287 ASSARSQANSIQS---QLEIIQEQARNQNSmymrQLSDLESTVSQLRS---ELREAKRMYEDKIEElekqlvlanSELTE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   731 TKLQQSSYHKQQEELD-ALKKTIEESEetlKNTKEIQRKAEEKYEVLENKMKNAeaererelkdaqkkldcakTKADASS 809
Cdd:pfam15921  361 ARTERDQFSQESGNLDdQLQKLLADLH---KREKELSLEKEQNKRLWDRDTGNS-------------------ITIDHLR 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   810 KKMKEKQQEVEAITLELEELKRE-HTSYKQQLEAVNEAIKSYEsQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA---- 884
Cdd:pfam15921  419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESsert 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   885 ----------QDTVIKAKYAEVAKHKEQNNdsqLKIKELDH--NISKHKR--EAEDGAAKVSKMLKD------YDWINAE 944
Cdd:pfam15921  498 vsdltaslqeKERAIEATNAEITKLRSRVD---LKLQELQHlkNEGDHLRnvQTECEALKLQMAEKDkvieilRQQIENM 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   945 RHLFGQPNSAYDF----KTNNPKEAGQRLQKLQEMK-EKLGRNVNMRamnvltEAEERYNDLMKKKRIVENDKSKILTTI 1019
Cdd:pfam15921  575 TQLVGQHGRTAGAmqveKAQLEKEINDRRLELQEFKiLKDKKDAKIR------ELEARVSDLELEKVKLVNAGSERLRAV 648
                          410
                   ....*....|..
gi 110347418  1020 EDLDQKKNQALN 1031
Cdd:pfam15921  649 KDIKQERDQLLN 660
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
681-926 2.14e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  681 LKDVQDELRIKENELR-ALEEE---LAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKK 750
Cdd:PRK02224  312 VEARREELEDRDEELRdRLEECrvaAQAHNEEAESLRedadDLEERAEELREEAAELESELEeaREAVEDRREEIEELEE 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  751 TIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAEAERERELKDAQKKLDCAKTKADASskKMKEKQQEVEaitlele 827
Cdd:PRK02224  392 EIEELRERFGDAPVDLGNAEDFLEELReerDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVE------- 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  828 elKREHTsykqqleavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTV----IKAKYAE--VAKHKE 901
Cdd:PRK02224  463 --GSPHV----------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleERREDLEelIAERRE 530
                         250       260
                  ....*....|....*....|....*
gi 110347418  902 QNNDSQLKIKELDHNISKHKREAED 926
Cdd:PRK02224  531 TIEEKRERAEELRERAAELEAEAEE 555
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
675-944 3.03e-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: 54.64  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   675 LTKFQELKDVQDELRIKENELRALEEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKKTI 752
Cdd:TIGR04523  359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETI 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   753 EESEETLKNTKEIQRKAEEKYEVLENKMKnaeaERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523  436 IKNNSEIKDLTNQDSVKELIIKNLDNTRE----SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   833 HTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ--KEVITAQDTVIKAKYAEVAKHKEQNNDSQLKI 910
Cdd:TIGR04523  512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
                          250       260       270
                   ....*....|....*....|....*....|....
gi 110347418   911 KELDHNISKHKREAEDGAAKVSKMLKDYDWINAE 944
Cdd:TIGR04523  592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
986-1144 3.54e-07

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 53.08  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  986 RAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKdfgsIFSTLLPGANAMLAPPEGQTVL 1065
Cdd:COG3950    97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVRE----ALNKLLPDFKDIRIDRDPGRLV 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1066 ----DGLEFkvalgntwkeNLTELSGGQRSLVAL--SLILSMLLFKPAP--------IYILDEVDAALDLSHTQNIGQML 1131
Cdd:COG3950   173 ildkNGEEL----------PLNQLSDGERSLLALvgDLARRLAELNPALenplegegIVLIDEIDLHLHPKWQRRILPDL 242
                         170
                  ....*....|...
gi 110347418 1132 RTHFTHSQFIVVS 1144
Cdd:COG3950   243 RKIFPNIQFIVTT 255
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
680-897 3.74e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  680 ELKDVQDELRIKENELRALEEELAGLKNTAEkyrQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETL 759
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  760 KNTKEIQRKAEEKYEVLE------------------NKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG3883    89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  822 ITLELEELKREHTSYKQQLEAvneAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 897
Cdd:COG3883   169 AKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
3-90 4.67e-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: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASNLQDLVyKNGQagiTKASVS 80
Cdd:cd03277     3 IVRIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIE 74
                          90
                  ....*....|.
gi 110347418   81 IT-FDNSDKKQ 90
Cdd:cd03277    75 IElYGNPGNIQ 85
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
662-892 5.02e-07

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 54.46  E-value: 5.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   662 TLSGGARS---QAASILTKFQE-LKDVQDELRIKENELRALEEELAGLKNTAekyrqlKQQWEMKTEEADLLQTKLQQ-- 735
Cdd:pfam12128  262 HLHFGYKSdetLIASRQEERQEtSAELNQLLRTLDDQWKEKRDELNGELSAA------DAAVAKDRSELEALEDQHGAfl 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   736 ----SSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDcaktkadaSSKK 811
Cdd:pfam12128  336 dadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK---EQNNRDIAGIKDKLA--------KIRE 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   812 MKEKQQEVEAITLE-LE-ELKREHtsyKQQLEAVNEAIKSYESQIE--------VMAAE-----VAKNKESVNKAQEEVT 876
Cdd:pfam12128  405 ARDRQLAVAEDDLQaLEsELREQL---EAGKLEFNEEEYRLKSRLGelklrlnqATATPelllqLENFDERIERAREEQE 481
                          250
                   ....*....|....*..
gi 110347418   877 K-QKEVITAQDTVIKAK 892
Cdd:pfam12128  482 AaNAEVERLQSELRQAR 498
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
692-870 6.22e-07

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 53.49  E-value: 6.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   692 ENELRALEEELAgLKNTAEKYRQLKQQWEMKTeeadlLQTKLQ--QSSYHKQQEELDALKKTIEESEEtlkNTKEIQRKA 769
Cdd:pfam05667  309 TNEAPAATSSPP-TKVETEEELQQQREEELEE-----LQEQLEdlESSIQELEKEIKKLESSIKQVEE---ELEELKEQN 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   770 EEKYEVLENKMKNAEaererELKDAQKKLDCAKTKADASSKKMKEKQQEVEA----ITLELEELKREHTSYKQQLEAVNE 845
Cdd:pfam05667  380 EELEKQYKVKKKTLD-----LLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLE 454
                          170       180
                   ....*....|....*....|....*
gi 110347418   846 AIKSYESQIEVMAAEvAKNKESVNK 870
Cdd:pfam05667  455 EIKELREKIKEVAEE-AKQKEELYK 478
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
709-905 6.86e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  709 AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKnTKEIQRKAEEKYEVLENKMKNAEAERE 788
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLA-AQEQKKQAEEAAKQAALKQKQAEEAAA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  789 RELKDAQKKLDCAKTKADASSKKMKE---KQQEVEAITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK 865
Cdd:PRK09510  140 KAAAAAKAKAEAEAKRAAAAAKKAAAeakKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAEAEAKKKAAAEAKKK 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110347418  866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND 905
Cdd:PRK09510  219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
679-821 6.99e-07

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: 51.85  E-value: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  679 QELKDVQDELRIKENELRALEEELAGLKntaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQ----QEELDALKKTIEE 754
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLKRRISD 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  755 SEETLKNTKEIQRKAEEKYEVLENKMknaeAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:COG1579   108 LEDEILELMERIEELEEELAELEAEL----AELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
422-934 1.03e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  422 KLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  502 RFPNLRFAYKD-PEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVV--------DTEVTGKKLLERGELKRR 572
Cdd:PRK03918  274 EIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleeKEERLEELKKKLKELEKR 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  573 YTIIP-----LNKISARCIAPETLRVAQNLVGPDNVHVALSLVE-YKPELQKAMEFVFGTTFVCDNMDNAKKVAFD--KR 644
Cdd:PRK03918  354 LEELEerhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkAKEEIEEEISKITARIGELKKEIKELKKAIEelKK 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  645 IMTRTVTLGGDVFDPH-GTLSGGARSQAASILTKFQELKDVQDELRIKENELRAL---EEELAGLKNTAEKYRQLK---- 716
Cdd:PRK03918  434 AKGKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEeklk 513
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  717 ----QQWEMKTEEADLLQTKL-----QQSSYHKQQEELDALKKTIEESEETLKNT--------KEIQRKAEEKYEVLENK 779
Cdd:PRK03918  514 kynlEELEKKAEEYEKLKEKLiklkgEIKSLKKELEKLEELKKKLAELEKKLDELeeelaellKELEELGFESVEELEER 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  780 MKNAE---------AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTsyKQQLEAVNEAIKSY 850
Cdd:PRK03918  594 LKELEpfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLEL 671
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  851 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVitaqdtviKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGA-A 929
Cdd:PRK03918  672 SRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlS 743

                  ....*
gi 110347418  930 KVSKM 934
Cdd:PRK03918  744 KVGEI 748
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
663-911 1.29e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  663 LSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLkntAEKYRQLKQQWEMKTEEADLLQTKLQQssyhkQQ 742
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAA-----LE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  743 EELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSK---KMKEKQQEV 819
Cdd:COG4942    83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  820 EAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKH 899
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
                         250
                  ....*....|..
gi 110347418  900 KEQNNDSQLKIK 911
Cdd:COG4942   243 TPAAGFAALKGK 254
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-63 1.69e-06

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 51.15  E-value: 1.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418    1 MHIKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQ 63
Cdd:COG3950     1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
8-89 1.78e-06

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: 50.35  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:cd03279     8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82

                  ....*.
gi 110347418   84 DNSDKK 89
Cdd:cd03279    83 QLGGKK 88
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
734-932 1.94e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  734 QQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSK 810
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIralEQELAALEAELAELEKEIAELRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  811 KMKEKQQEVEAITLELEELKREHT-------------------------SYKQQLEAVNEAIKSYESQIEVMAAEVAKNK 865
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  866 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 932
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
3-126 1.96e-06

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: 50.76  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVykngQAGITKASVSIT 82
Cdd:cd03242     1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISAV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 110347418   83 FDNSdkkqsplGFEVHDEITVTRqvviGGRNKYLINGVNANNTR 126
Cdd:cd03242    72 LERQ-------GGELALELTIRS----GGGRKARLNGIKVRRLS 104
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
665-892 3.52e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  665 GGARSQAASILTKFQE-LKDVQDELRIKENE-----LRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqsSY 738
Cdd:PRK02224  172 SDARLGVERVLSDQRGsLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLE-----EH 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  739 HKQQEELDALKKTIEESEETLkntkeiqRKAEEKYEVLENKMKNAEAERErELKDAQKKL--DCAKTKADAsskkmkekq 816
Cdd:PRK02224  247 EERREELETLEAEIEDLRETI-------AETEREREELAEEVRDLRERLE-ELEEERDDLlaEAGLDDADA--------- 309
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  817 qevEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV-TKQKEVITAQDTVIKAK 892
Cdd:PRK02224  310 ---EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaELESELEEAREAVEDRR 383
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
670-934 4.38e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 50.89  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   670 QAASILTKFQeLKDVQDELRIKENELRaleEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQQssYHKQQEELD-AL 748
Cdd:pfam05557    1 RAELIESKAR-LSQLQNEKKQMELEHK---RARIELEK---KASALKRQLDRESDRNQELQKRIRL--LEKREAEAEeAL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   749 KKTIEESEETLKNTKEIQRKAEEKYEVLEnkmknaeaererelkDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 828
Cdd:pfam05557   72 REQAELNRLKKKYLEALNKKLNEKESQLA---------------DAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   829 LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVikAKYAEVAKHKEQNNDSQL 908
Cdd:pfam05557  137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL--ARIPELEKELERLREHNK 214
                          250       260
                   ....*....|....*....|....*.
gi 110347418   909 KIKELDHNISKHKREAEDGAAKVSKM 934
Cdd:pfam05557  215 HLNENIENKLLLKEEVEDLKRKLERE 240
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
678-880 4.39e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  678 FQELKDVQDELRIKENELRALEEELAGLKNT----AEKYRQLKQQWEMKTEEADLLQTKL-----QQSSYHKQQEELDAL 748
Cdd:COG1340    35 NEELKELAEKRDELNAQVKELREEAQELREKrdelNEKVKELKEERDELNEKLNELREELdelrkELAELNKAGGSIDKL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  749 KKTIEESEETLKN---TKEIQRKAEEKYEVLENKMKNAEAERE--RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAIT 823
Cdd:COG1340   115 RKEIERLEWRQQTevlSPEEEKELVEKIKELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELH 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  824 LELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:COG1340   195 EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
422-879 5.97e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  422 KLKHAQQELKNKQAEVKKmdsgYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEE------SLLEKRRQLSRDIGRLKET 495
Cdd:COG4717    72 ELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAELPER 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  496 YEALLARFPNLRFaykdpeknwnrncvkgLVASLISVKDTSATTALELVAGERLYNVVVDTEVTgKKLLERGELKRRYTI 575
Cdd:COG4717   148 LEELEERLEELRE----------------LEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAE 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  576 IpLNKISARCIAPETLRvaQNLVGPDNVHVALSLVEykpELQKAMEFVFGTTFVCDnmdnakKVAFDKRIMTRTVTLGGD 655
Cdd:COG4717   211 L-EEELEEAQEELEELE--EELEQLENELEAAALEE---RLKEARLLLLIAAALLA------LLGLGGSLLSLILTIAGV 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  656 VFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGL--------KNTAEKYRQLKQQWEMKTEEAD 727
Cdd:COG4717   279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQELLREAEE 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  728 lLQTKLQQSSYHKQQEELdaLKKTIEESEETLK---NTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQK-----KLD 799
Cdd:COG4717   359 -LEEELQLEELEQEIAAL--LAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeELE 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  800 CAKTKADASSKKMKEKQQEVEAITLELEELKREHTsykqqLEAVNEAIKSYESQIEVMAAEVAKNK---ESVNKAQEEVT 876
Cdd:COG4717   436 ELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKlalELLEEAREEYR 510

                  ...
gi 110347418  877 KQK 879
Cdd:COG4717   511 EER 513
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
674-853 6.59e-06

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 50.00  E-value: 6.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   674 ILTKFQELKDVQDELRIKENELRALEEELAglkntAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIE 753
Cdd:pfam05262  182 VVEALREDNEKGVNFRRDMTDLKERESQED-----AKRAQQLKEELDKKQIDADKAQQKADFA-----QDNADKQRDEVR 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   754 ESEETLKNTKEIQR--KAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKR 831
Cdd:pfam05262  252 QKQQEAKNLPKPADtsSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKRE 331
                          170       180
                   ....*....|....*....|..
gi 110347418   832 EHTSYKQQLEAVNEAIKSYESQ 853
Cdd:pfam05262  332 PVAEDLQKTKPQVEAQPTSLNE 353
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
679-880 7.70e-06

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 50.34  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWemktEEADLLQTKLQQssyhkqqeELDALKKTI------ 752
Cdd:COG3096   903 DAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADY----LQAKEQQRRLKQ--------QIFALSEVVqrrphf 970
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  753 --EESEETLKNTKEIQrkaeekyEVLENKMKNAEAERER---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVE 820
Cdd:COG3096   971 syEDAVGLLGENSDLN-------EKLRARLEQAEEARREareQLRQAQAQYSqynqvlaSLKSSRDAKQQTLQELEQELE 1043
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347418  821 AITL----ELEELKREHTS-YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:COG3096  1044 ELGVqadaEAEERARIRRDeLHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
738-1028 8.96e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  738 YHKQQEELDALKKTIEESEETLKntKEIQRKAEekyevLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQq 817
Cdd:PRK03918  160 YENAYKNLGEVIKEIKRRIERLE--KFIKRTEN-----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  818 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVnkaqEEVTKQKEVitaqdtviKAKYAEVA 897
Cdd:PRK03918  232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEK--------AEEYIKLS 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  898 KHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnSAYDFKTNNPKEAGQRLQKLQEMKE 977
Cdd:PRK03918  300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERHELYEEAKAKKE 372
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110347418  978 KLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 1028
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
180-1026 9.15e-06

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.05  E-value: 9.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   180 AAQKTIEKKEAKLKEIKTILE--EEITPTIQKLKEE----RSSYLEYQKVMREIEH-LSRLYIAYQFLLAEDTKVRSAEe 252
Cdd:TIGR00606  235 SSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEikalKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHNHQRT- 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   253 LKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA-EAQRVNTKSQSAFDLKKKNLACE---- 327
Cdd:TIGR00606  314 VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGPFSErqik 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   328 ----------ESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEat 397
Cdd:TIGR00606  394 nfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-- 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   398 lagqmmacknDISKAQTEAKQAQMKLKHAQqelKNKQAEVKKMDSGYRKDQEAleAVKRLKEKLEAEMKKLNYEENKEES 477
Cdd:TIGR00606  472 ----------RILELDQELRKAERELSKAE---KNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHTTTRTQ 536
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   478 LL-------EKRRQLSRDIGRLKETYEALLARFPNLR-----FAYKDPEKNWNRNCVKGLVASLISV--------KDTSA 537
Cdd:TIGR00606  537 MEmltkdkmDKDEQIRKIKSRHSDELTSLLGYFPNKKqledwLHSKSKEINQTRDRLAKLNKELASLeqnknhinNELES 616
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   538 TTALELVAGERLYNVV--VDTEVTGKKLLERGElKRRYTIIPLNKISARCIAPETLRVAQNlvgPDNVHVALSLVEYKPE 615
Cdd:TIGR00606  617 KEEQLSSYEDKLFDVCgsQDEESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVFQTEAE 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   616 LQKamefvfgttfVCDNMDNAKKVAFDKriMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQdelrikeNEL 695
Cdd:TIGR00606  693 LQE----------FISDLQSKLRLAPDK--LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-------NKL 753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLqqSSYHKQQEELDALKKTIEE------SEETLKNTKEIQRKA 769
Cdd:TIGR00606  754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV--TIMERFQMELKDVERKIAQqaaklqGSDLDRTVQQVNQEK 831
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   770 EEKYEVLENKMKNAE------AERERELKDAQKKLDCAKTKADASSKKMKEKQQ---EVEAITLELEELKREHTSYKQQL 840
Cdd:TIGR00606  832 QEKQHELDTVVSKIElnrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQD 911
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   841 EAVNEAIKSYESQIEVMaaeVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKE-QNNDSQLKIKELDHNISK 919
Cdd:TIGR00606  912 SPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEE 988
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   920 HKREAEDGAAKVSKMLKDYDwINAERHLFGQPNSAYDFKTNnpkeagqrlqKLQEMKEKLGRNVNMRAMNVLTEAEERYN 999
Cdd:TIGR00606  989 CEKHQEKINEDMRLMRQDID-TQKIQERWLQDNLTLRKREN----------ELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
                          890       900
                   ....*....|....*....|....*..
gi 110347418  1000 DLMKKKRIVENDKSKILTTIEDLDQKK 1026
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQKGYEKEI 1084
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
680-855 1.02e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  680 ELKDVQDELRIKENELRALEEELAGLKNTAEKYRQlkqqwEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 759
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  760 KNTKEiqrkaeekYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREhtsY 836
Cdd:COG1579    86 RNNKE--------YEALQKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---L 154
                         170
                  ....*....|....*....
gi 110347418  837 KQQLEAVNEAIKSYESQIE 855
Cdd:COG1579   155 EAELEELEAEREELAAKIP 173
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1053-1133 1.08e-05

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 47.85  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1053 NAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03225   103 NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLK 178

                  .
gi 110347418 1133 T 1133
Cdd:cd03225   179 K 179
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
679-864 1.13e-05

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 49.47  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDEL---RIKENELRALEEELAGLKntaekyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEeldalKKTIEES 755
Cdd:pfam09726  402 QDIKKLKAELqasRQTEQELRSQISSLTSLE------RSLKSELGQLRQENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   756 EETLKNTKEiQRKAEEKYEVLENKMKnaeaeRERELKDAQKKLDCAKTKAD-ASSKKMKEKQQEVEAITLEL-----EEL 829
Cdd:pfam09726  471 EKRLKAEQE-ARASAEKQLAEEKKRK-----KEEEATAARAVALAAASRGEcTESLKQRKRELESEIKKLTHdiklkEEQ 544
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 110347418   830 KREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 864
Cdd:pfam09726  545 IRELEIKVQELRKYKESEKDTEVLMSALSAMQDKN 579
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
2-100 1.25e-05

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


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 48.89  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    2 HIKSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITK 76
Cdd:COG1106     1 MLISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEP 80
                          90       100
                  ....*....|....*....|....
gi 110347418   77 ASVSITFdNSDKKQSPLGFEVHDE 100
Cdd:COG1106    81 SEFEILF-LLDGVRYEYGFELDKE 103
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
776-939 1.28e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.00  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  776 LENKMKNAEAERE---RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAV--NEAIKSY 850
Cdd:COG1579    15 LDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  851 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDsqlKIKELDHNISKHKREAEDGAAK 930
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAK 171
                         170
                  ....*....|
gi 110347418  931 VSK-MLKDYD 939
Cdd:COG1579   172 IPPeLLALYE 181
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
742-878 1.32e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.00  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  742 QEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-----RERELKDAQKKLDCAKTKADASSKKMKEKQ 816
Cdd:COG1579    37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQKEIESLKRRISDLEDEILELM 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347418  817 QEveaitleLEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:COG1579   117 ER-------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
668-1168 1.35e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  668 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSSYHKQQEELDA 747
Cdd:PRK03918  320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEE 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  748 LKKTIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAE-------------------AERERELKDAQKKLdcakTKA 805
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKEL----KEI 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  806 DASSKKMKEKQQEVEAITLELEELKREHTSYKQqLEAVNEAIKSYE-SQIEVMAAEVAKNKESVNKAQ------------ 872
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgeikslkkelek 550
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  873 -EEVTKQKEVITAQDTVIKAKYAEVAK-----------------------HKEQNN--DSQLKIKELDHNISKHKREAED 926
Cdd:PRK03918  551 lEELKKKLAELEKKLDELEEELAELLKeleelgfesveeleerlkelepfYNEYLElkDAEKELEREEKELKKLEEELDK 630
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  927 GAAKVSKMLKDYDWINAERHLFGQPNSAYDF--KTNNPKEAGQRLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKK 1004
Cdd:PRK03918  631 AFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKA 709
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1005 KRIVENDKsKILTTIEDLDQK----KNQALNIAWQKVNKDFGSIFSTLLPGANAmlappegQTVLDGLEFKVALGNTW-- 1078
Cdd:PRK03918  710 KKELEKLE-KALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYS-------GVRVKAEENKVKLFVVYqg 781
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1079 -KENLTELSGGQRSLVALS--LILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNAN 1154
Cdd:PRK03918  782 kERPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELKDAAD 861
                         570
                  ....*....|....
gi 110347418 1155 VLFKTKFVDGVSTV 1168
Cdd:PRK03918  862 YVIRVSLEGGVSKV 875
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
632-1026 1.50e-05

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: 49.33  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   632 NMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELrikenelraLEEELAGLKNTAEK 711
Cdd:pfam05483  308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---------LRTEQQRLEKNEDQ 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   712 YRQLKQQWEMKTEEADLLqTKLQQSsyhkQQEELDALKKTIEESEETLKNTKEIQRKAEEkYEVLENKMKNAEAEREREL 791
Cdd:pfam05483  379 LKIITMELQKKSSELEEM-TKFKNN----KEVELEELKKILAEDEKLLDEKKQFEKIAEE-LKGKEQELIFLLQAREKEI 452
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   792 KDAQKKLDCAKTKADASSKKMKEKQQEVE--------------AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVM 857
Cdd:pfam05483  453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   858 AAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLK----IKELDHNISKHKREAEDGAAKVSK 933
Cdd:pfam05483  533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQIENKNKNIEE 612
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   934 MLKDYDWINAERHLFGQPNSAYDFKTNNPK-EAGQRLQKLQEMKEKLGRNVNMRAMnvlteAEERYNDLMKKKRIVENDK 1012
Cdd:pfam05483  613 LHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKI-----SEEKLLEEVEKAKAIADEA 687
                          410
                   ....*....|....
gi 110347418  1013 SKILTTIEDLDQKK 1026
Cdd:pfam05483  688 VKLQKEIDKRCQHK 701
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
147-489 1.73e-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: 49.35  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   147 QGRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTIEKKEAKLKEIKTILE-EEITPTIQKLKEE-RSSYLEYQKVM 224
Cdd:pfam15921  266 QDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSElREAKRMYEDKI 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   225 REIEHlsrlyiayQFLLA--EDTKVRS-----AEELKEMQDKvikLQEELSENDKKIKALNHEIEELEKRKDKETGG--- 294
Cdd:pfam15921  345 EELEK--------QLVLAnsELTEARTerdqfSQESGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   295 ---ILRSLEDALAEAQRVNT-----KSQSAFDLKKKnLACEESKRKELEKnmvedSKTLAAKEKEVKKItdgLHALQEAS 366
Cdd:pfam15921  414 idhLRRELDDRNMEVQRLEAllkamKSECQGQMERQ-MAAIQGKNESLEK-----VSSLTAQLESTKEM---LRKVVEEL 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   367 NKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMKLKHAQQE---LKNKQAEVKKMDSG 443
Cdd:pfam15921  485 TAKKMTLESSERTVSDLTASLQEKERAIEATNA--------EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ 556
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 110347418   444 YRKDQEALEAvkrLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDI 489
Cdd:pfam15921  557 MAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
668-882 2.28e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  668 RSQAASILTKFQELKDVQDELRIKENELRaleEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEelda 747
Cdd:COG1340    63 REKRDELNEKVKELKEERDELNEKLNELR---EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE---- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  748 lKKTIEESEEtLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELE 827
Cdd:COG1340   136 -KELVEKIKE-LEKELEKAKKALEKNEKLKELRAELKELRK-EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  828 ELKREHTSYKQQLEAVNEAIKSYESQI-----EVMAAEVAKNKESVNKAQEEVTKQKEVI 882
Cdd:COG1340   213 ELHKEIVEAQEKADELHEEIIELQKELrelrkELKKLRKKQRALKREKEKEELEEKAEEI 272
PRK11281 PRK11281
mechanosensitive channel MscK;
720-916 2.46e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 48.75  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  720 EMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEES-EETLKNTKEIQR-KAEEKYEVLE--NKMKNAE-----AERERE 790
Cdd:PRK11281   57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAELEAlKDDNDEETREtlSTLSLRQlesrlAQTLDQ 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  791 LKDAQKKLDCA-------KTKADASSKKMKEKQQEVEAITLELEELKRE---------------------HTSYKQQLEA 842
Cdd:PRK11281  137 LQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGgkalrpsqrvllqaeqallnaQNDLQRKSLE 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347418  843 VNEAIKS-YESQIEVMAAEVAKNKESVNKAQEEVTkQKEVITAQDTVIKAKYAEVAKHKEQNNdsqLKIKELDHN 916
Cdd:PRK11281  217 GNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAIN-SKRLTLSEKTVQEAQSQDEAARIQANP---LVAQELEIN 287
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1081-1143 2.52e-05

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 46.27  E-value: 2.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418 1081 NLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:cd03214    94 PFNELSGGERQRV----LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
684-892 2.86e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.63  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   684 VQDELRIKENELRALEEELAGLKNTAE----KYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEEldalkktieeseetl 759
Cdd:pfam01576  880 LQDEKRRLEARIAQLEEELEEEQSNTEllndRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE--------------- 944
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   760 KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQ 839
Cdd:pfam01576  945 RQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQ 1024
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418   840 LEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQ---EEVTKQKEVITAQDTVIKAK 892
Cdd:pfam01576 1025 AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQrelDDATESNESMNREVSTLKSK 1080
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
679-1033 3.44e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDELRIKENELRALEEELAGlknTAEKYRQLKQQWEMKTEEADLLQTKLQQSS--YHKQQEELDALKKTIEESE 756
Cdd:pfam15921  419 RELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKemLRKVVEELTAKKMTLESSE 495
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   757 ETLKntkEIQRKAEEKYEVLEnkMKNAEAERERELKDAQ-KKLDCAKTKADasskKMKEKQQEVEAITLELEELKREHTS 835
Cdd:pfam15921  496 RTVS---DLTASLQEKERAIE--ATNAEITKLRSRVDLKlQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEI 566
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   836 YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTvikakyaevakhkeqnndsqlKIKELDH 915
Cdd:pfam15921  567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA---------------------KIRELEA 625
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   916 NISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmramNVLTEAE 995
Cdd:pfam15921  626 RVSDLELEKVKLVNAGSERLRAVKDIKQER----------DQLLNEVKTSRNELNSLSEDYEVLKRNFR----NKSEEME 691
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 110347418   996 ERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIA 1033
Cdd:pfam15921  692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
679-923 3.55e-05

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: 48.18  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDEL----RIKENELRALEEELAGLKNTAEKYrqLKQQWEMKTE--EADLLQTKLQQSS------YHKQQEELD 746
Cdd:pfam05483  432 EELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHY--LKEVEDLKTEleKEKLKNIELTAHCdkllleNKELTQEAS 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   747 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKM---------KEKQ- 816
Cdd:pfam05483  510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENArsieyevlkKEKQm 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   817 -----------QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQK-- 879
Cdd:pfam05483  590 kilenkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfeEIIDNYQKEIEDKKis 669
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 110347418   880 ------EVITAQDTVIKAkyaeVAKHKEQNNDSQLKIKELDHNISKHKRE 923
Cdd:pfam05483  670 eeklleEVEKAKAIADEA----VKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
742-1017 3.61e-05

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: 48.04  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   742 QEELDA-LKKTIEESEETLKNTKEIQRKAEEKYEVLENKmKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR00618  151 QGEFAQfLKAKSKEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   821 AITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTviKAKYAEVAKHK 900
Cdd:TIGR00618  230 HLREALQQTQQSHAYLTQKREAQEEQ-----LKKQQLLKQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAV 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   901 EQNNDsqlKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYD-FKTNNPKEAGQRLQKLQEMKEkl 979
Cdd:TIGR00618  303 TQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTL-- 377
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 110347418   980 gRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILT 1017
Cdd:TIGR00618  378 -TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
687-926 3.68e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.41  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  687 ELRIKENELRALEEELAGLKN--TAEKYRQ--LKQQWEMKTEEADLLQTKLQQSSYH--------KQQEELDALKKTIEE 754
Cdd:COG3096   279 ERRELSERALELRRELFGARRqlAEEQYRLveMARELEELSARESDLEQDYQAASDHlnlvqtalRQQEKIERYQEDLEE 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  755 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERER---ELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITLELEE 828
Cdd:COG3096   359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksQLADYQQALDVQQTRAIQyqqAVQALEKARALCGLPDLTPEN 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  829 LKREHTSYKQQLEAVNEAIKSYESQIEVmaAEVAKNK-----ESVNKAQEEVTKQ------KEVIT---------AQDTV 888
Cdd:COG3096   439 AEDYLAAFRAKEQQATEEVLELEQKLSV--ADAARRQfekayELVCKIAGEVERSqawqtaRELLRryrsqqalaQRLQQ 516
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 110347418  889 IKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAED 926
Cdd:COG3096   517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
677-1020 3.88e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   677 KFQELKDVQDELRIKENELRALEEELAGLKNTAEK--YRQLKQQWEMKTEEADLLQTKLQQS--SYHKQQEELDALKKTI 752
Cdd:TIGR04523  272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNnkIISQLNEQISQLKKEL 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   753 EESEetlKNTKEIQRKAEEKYEVLEnKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523  352 TNSE---SENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   833 HTSYKQQLEAVNEAIKSYES---------------------QIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKA 891
Cdd:TIGR04523  428 IERLKETIIKNNSEIKDLTNqdsvkeliiknldntresletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   892 KYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNS------AYDFKTNNPKEA 965
Cdd:TIGR04523  508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqTQKSLKKKQEEK 587
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418   966 GQRLQKLQEMKEKLGRNVNMRAMNV------LTEAEERYNDLMKKKRIVENDKSKILTTIE 1020
Cdd:TIGR04523  588 QELIDQKEKEKKDLIKEIEEKEKKIsslekeLEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
23-376 4.10e-05

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 47.76  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   23 FDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASnlQDLVyKNGQAgitKASVSITFDNSDKKQ-----SPLGFEV 97
Cdd:COG0497    20 FGPGLTVLTGETGAGKSILLDALGLLLG------GRAD--ASLV-RHGAD---KAEVEAVFDLSDDPPlaawlEENGLDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   98 HD-EITVTRQVVIGGRNKYLINGVNANNTRVQDLFcsvglnvnnpHFLI-MQG-----RItkvlnMKPPEILSMIEEAAG 170
Cdd:COG0497    88 DDgELILRREISADGRSRAFINGRPVTLSQLRELG----------ELLVdIHGqhehqSL-----LDPDAQRELLDAFAG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  171 TR--MYEYKkiAAQKTIEKKEAKLKEIKTILEEeitptiqklKEERSSYLEYQkvMREIEHLSRLYIAYQFLLAEDTKVR 248
Cdd:COG0497   153 LEelLEEYR--EAYRAWRALKKELEELRADEAE---------RARELDLLRFQ--LEELEAAALQPGEEEELEEERRRLS 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  249 SAEELKEmqdKVIKLQEELSEND----KKIKALNHEIEELEkRKDKETGGILRSLEDALAEAQ----------------- 307
Cdd:COG0497   220 NAEKLRE---ALQEALEALSGGEggalDLLGQALRALERLA-EYDPSLAELAERLESALIELEeaaselrryldslefdp 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  308 ----RVNTKSQSAFDLKKKN-------LACEESKRKELEK--NMVEDSKTLAAKEKEVKKITDGL-HALQEASNKDAEAL 373
Cdd:COG0497   296 erleEVEERLALLRRLARKYgvtveelLAYAEELRAELAEleNSDERLEELEAELAEAEAELLEAaEKLSAARKKAAKKL 375

                  ...
gi 110347418  374 AAA 376
Cdd:COG0497   376 EKA 378
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
740-841 4.90e-05

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 44.10  E-value: 4.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   740 KQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEV 819
Cdd:pfam13863    3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
                           90       100
                   ....*....|....*....|..
gi 110347418   820 EAITLELEELKREHTSYKQQLE 841
Cdd:pfam13863   83 KKLTAQIEELKSEISKLEEKLE 104
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
181-308 5.34e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  181 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKVMREIEH--------LSRLYIAYQFLLAEDTKV 247
Cdd:COG3206   187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418  248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQR 308
Cdd:COG3206   267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
3-472 5.63e-05

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


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 47.42  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    3 IKSII-LEGFKSYAQRTEVNGFDPLfNAITGLNGSGK---SNILDSICfllgisnlsqvrasnlqdlvyKNGQAGITKAS 78
Cdd:COG4694     2 ITKIKkLKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE---------------------LGDTSSEVIAE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   79 VSITFDNSDKKQSPLGF-------EVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLfcSVGLNVNNPHFLIMQGRIT 151
Cdd:COG4694    60 FEIEAGGSAPNPSVRVFnrdfveeNLRSGEEIKGIFTLGEENIELEEEIEELEKEIEDL--KKELDKLEKELKEAKKALE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  152 KVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEK-------------KEAKLKEIKTILEEEITPTIQKLKEERSSYL 218
Cdd:COG4694   138 KLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSAlksssedelkeklKLLKEEEPEPIAPITPLPDLKALLSEAETLL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  219 EYQKVMREIEHLSRLyiayQFLLAEDTKVRSAEELKEMQDKVI------KLQEEL---------SENDKKIKALNHEIEE 283
Cdd:COG4694   218 EKSAVSSAIEELAAL----IQNPGNSDWVEQGLAYHKEEEDDTcpfcqqELAAERiealeayfdDEYEKLLAALKDLLEE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  284 LEKRKDKETGGILRSLEDALAEA-QRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAakeKEVKKITDGLHAL 362
Cdd:COG4694   294 LESAINALSALLLEILRTLLPSAkEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELL---DELNDLIAALNAL 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  363 QEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAGQmmacKNDISKAQTEAKQAQmKLKHAQQELKNKQAEVKKmds 442
Cdd:COG4694   371 IEEHNAKIANLKAEKE--EARKKLEAHELAELKEDLSRY----KAEVEELIEELKTIK-ALKKALEDLKTEISELEA--- 440
                         490       500       510
                  ....*....|....*....|....*....|
gi 110347418  443 gyrkdqeALEAVKRLKEKLEAEMKKLNYEE 472
Cdd:COG4694   441 -------ELSSVDEAADEINEELKALGFDE 463
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
743-947 5.63e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  743 EELDALKKTIEESEETLKNTKEIQRKAEEkyevLENKMKNAEAERErELKDAQKKLDCAKTKADASsKKMKEKQQEVEAI 822
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELE-ELREELEKLEKLLQLLPLY-QELEALEAELAEL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  823 TLELEELKREHTSYKQQLEavneaiksyesQIEVMAAEVAKNKESVNKAQEEVTKQKEvitaqdtvikakyAEVAKHKEQ 902
Cdd:COG4717   145 PERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATE-------------EELQDLAEE 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110347418  903 NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 947
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
263-503 6.44e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  263 LQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRvntksqsafdlkKKNLACEESKRKELEKNMVEDS 342
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKE--------LEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELE 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  343 KTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMK 422
Cdd:COG3206   226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELA--------ELSARYTPNHPDVIA 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  423 LKHAQQELKNK-QAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMKKLNyeenkeeSLLEKRRQLSRDIGRLKETYE 497
Cdd:COG3206   296 LRAQIAALRAQlQQEAQRILASLEAELEALQAreasLQAQLAQLEARLAELP-------ELEAELRRLEREVEVARELYE 368

                  ....*.
gi 110347418  498 ALLARF 503
Cdd:COG3206   369 SLLQRL 374
46 PHA02562
endonuclease subunit; Provisional
711-945 6.48e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.93  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  711 KYRQLKQQWEMKTEEADLLQTKLQqsSYHKQQEELDAlkktieeseetlKNTKEIQRKaEEKYEVLENKMKNAEAERErE 790
Cdd:PHA02562  175 KIRELNQQIQTLDMKIDHIQQQIK--TYNKNIEEQRK------------KNGENIARK-QNKYDELVEEAKTIKAEIE-E 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  791 LKDaqKKLDCAKTKADASSKkMKEKQQEVEAITLELEELKREHTSY---------KQQLEAVNEAIKSYESQIevmaAEV 861
Cdd:PHA02562  239 LTD--ELLNLVMDIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKL----KEL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  862 AKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWI 941
Cdd:PHA02562  312 QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391

                  ....
gi 110347418  942 NAER 945
Cdd:PHA02562  392 VKTK 395
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
669-912 7.10e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  669 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ--EEL 745
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDElNAQVKELREEAQELREKRDELNEKVKELKEERDElnEKL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  746 DALKKTIEESEETLKNTKEIQR---KAEEKYEVLENKMKNA----EAERE--RELKDAQKKLDCAKtKADASSKKMKEKQ 816
Cdd:COG1340    88 NELREELDELRKELAELNKAGGsidKLRKEIERLEWRQQTEvlspEEEKElvEKIKELEKELEKAK-KALEKNEKLKELR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  817 QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEV 896
Cdd:COG1340   167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
                         250
                  ....*....|....*.
gi 110347418  897 AKHKEQNNDSQLKIKE 912
Cdd:COG1340   247 KKLRKKQRALKREKEK 262
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
698-821 7.50e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  698 LEEELAGLkntAEKYRQLKQQW---EMKTEEADLLQTKLQQSsYHKQQEELDALKKTIEES-EETLKNTKEiqRKAEEKY 773
Cdd:PRK00409  518 LNELIASL---EELERELEQKAeeaEALLKEAEKLKEELEEK-KEKLQEEEDKLLEEAEKEaQQAIKEAKK--EADEIIK 591
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110347418  774 EVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 821
Cdd:PRK00409  592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
mukB PRK04863
chromosome partition protein MukB;
679-885 9.22e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  679 QELKDVQDELRIKENELRALEEElagLKNTAEKYRQLKQQW---------------EMKTEEADLLQTKLQQSSYHKQ-- 741
Cdd:PRK04863  837 AELRQLNRRRVELERALADHESQ---EQQQRSQLEQAKEGLsalnrllprlnlladETLADRVEEIREQLDEAEEAKRfv 913
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  742 --------------------QEELDALKKTIEESEETLKNTKE--------IQRKAEEKY--------------EVLENK 779
Cdd:PRK04863  914 qqhgnalaqlepivsvlqsdPEQFEQLKQDYQQAQQTQRDAKQqafaltevVQRRAHFSYedaaemlaknsdlnEKLRQR 993
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  780 MKNAEAERER---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVEAITL----ELEELKREHTS-YKQQLEAVN 844
Cdd:PRK04863  994 LEQAEQERTRareQLRQAQAQLAqynqvlaSLKSSYDAKRQMLQELKQELQDLGVpadsGAEERARARRDeLHARLSANR 1073
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 110347418  845 EAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 885
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
679-880 1.05e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 45.02  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEA-DLLQTKLQQ-SSYHKQQEELDALKKTIEES- 755
Cdd:pfam00261    8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeERLAEALEKlEEAEKAADESERGRKVLENRa 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   756 ----------EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdaqkkldcAKTKADASSKKMKEKQQEVEAIT-- 823
Cdd:pfam00261   88 lkdeekmeilEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-----------AEERAELAESKIVELEEELKVVGnn 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418   824 ---LELEELK---REHtSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 880
Cdd:pfam00261  157 lksLEASEEKaseRED-KYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
242-446 1.11e-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: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAE----AQRVNTKSQSAF 317
Cdd:COG4942    46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-ELRAELEAQKEELAEllraLYRLGRQPPLAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  318 DLKKKNLAcEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAT 397
Cdd:COG4942   125 LLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 110347418  398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK 446
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-507 1.58e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  171 TRMYEYKKIAAQKTIEKKEAKLKEI---KTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKv 247
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR- 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  248 rsAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK--------RKDKETGGILRSLEDALAE--AQRVNTKSQSAF 317
Cdd:PRK03918  451 --KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeselIKLKELAEQLKELEEKLKKynLEELEKKAEEYE 528
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  318 DLKKK---------NLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLS 388
Cdd:PRK03918  529 KLKEKliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  389 SNEDGAEATLAgQMMACKNDISKAQTE------------AKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKR 456
Cdd:PRK03918  609 DAEKELEREEK-ELKKLEEELDKAFEElaetekrleelrKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110347418  457 LKEKLEAEMKKLnyEENKEEslLEKRRQLSRDIGRLKETYEALLARFPNLR 507
Cdd:PRK03918  688 RREEIKKTLEKL--KEELEE--REKAKKELEKLEKALERVEELREKVKKYK 734
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
161-503 1.61e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  161 ILSMIEEAAGTRMYEY------KKIAAQKTIEKKEAKLKEIKTILEE--EITPTIQKLKEE----RSSYLEYQKVMREIE 228
Cdd:COG4717    43 IRAMLLERLEKEADELfkpqgrKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEEleelEAELEELREELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  229 HLSRLYIAYQFLLAEDTKVRS----AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA 304
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAElperLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  305 EAQRVNTKSQSAFDLKKKNLaceESKRKELEKnmVEDSKTLAAKEKEVKKITDGLHALqeasnkdaeALAAAQQHFNAVS 384
Cdd:COG4717   203 ELQQRLAELEEELEEAQEEL---EELEEELEQ--LENELEAAALEERLKEARLLLLIA---------AALLALLGLGGSL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  385 AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKK-----MDSGYRKDQEALEAVKRLKE 459
Cdd:COG4717   269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELLELLDRIEE 348
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 110347418  460 --KLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARF 503
Cdd:COG4717   349 lqELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1062-1143 1.97e-04

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 44.02  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1062 QTVLDGLEFKVALGNtwkENLtelSGGQRSLVALSLILsmllFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFI 1141
Cdd:cd03244   123 ESLPGGLDTVVEEGG---ENL---SVGQRQLLCLARAL----LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVL 192

                  ..
gi 110347418 1142 VV 1143
Cdd:cd03244   193 TI 194
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
679-856 2.07e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLlQTKLQQ--SSYHKQQEELDALKKTIEESE 756
Cdd:COG3206   226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAElsARYTPNHPDVIALRAQIAALR 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  757 EtlkntkEIQRKAEEKYEVLENKMKNAEAeRERELKDAQKKLDcaktkadASSKKMKEKQQEVEAITLELEELKREHTSY 836
Cdd:COG3206   305 A------QLQQEAQRILASLEAELEALQA-REASLQAQLAQLE-------ARLAELPELEAELRRLEREVEVARELYESL 370
                         170       180
                  ....*....|....*....|
gi 110347418  837 KQQLEAVNEAIKSYESQIEV 856
Cdd:COG3206   371 LQRLEEARLAEALTVGNVRV 390
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
199-507 2.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  199 LEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE---DTKVRSAEELKEMQDKVIKLQEELSENDKKIK 275
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  276 ALNHEIEELEKRKDK-ETGGILRSLEDALAEAQRV------------NTKSQSAFDLKKKNLAC-----------EESKR 331
Cdd:COG4717   217 EAQEELEELEEELEQlENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFlvlgllallflLLARE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  332 KELEKNMVEDSKTLAAKE----KEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEdgAEATLAGQMMACKN 407
Cdd:COG4717   297 KASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLEELEQEIAA 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  408 DISKAQTEAKQA-QMKLKHAQ--QELKNKQAEVKKMDSGYRKDQEALEAV---KRLKEKLEAEMKKLNYEENKEESLLEK 481
Cdd:COG4717   375 LLAEAGVEDEEElRAALEQAEeyQELKEELEELEEQLEELLGELEELLEAldeEELEEELEELEEELEELEEELEELREE 454
                         330       340
                  ....*....|....*....|....*...
gi 110347418  482 RRQLSRDIGRLKE--TYEALLARFPNLR 507
Cdd:COG4717   455 LAELEAELEQLEEdgELAELLQELEELK 482
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
680-912 2.72e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  680 ELKDVQDELRIKENELRALEEELAGLKNTaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 759
Cdd:NF033838  175 ELEIAESDVEVKKAELELVKEEAKEPRDE-EKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  760 KNTKEIQRKAEEKYEVL---------ENKMKNAEA------------ERERELKDAQKKLDCAKTKADASSKKMKEKQQE 818
Cdd:NF033838  254 ATSEQDKPKRRAKRGVLgepatpdkkENDAKSSDSsvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPT 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  819 VEAITLELEELKREHTSYKQQLEAVNEAIKSyesqievmaaevAKNKESVNKAQEEVTKQKEVITAQDTVI--KAKYAEV 896
Cdd:NF033838  334 NTYKTLELEIAESDVKVKEAELELVKEEAKE------------PRNEEKIKQAKAKVESKKAEATRLEKIKtdRKKAEEE 401
                         250
                  ....*....|....*.
gi 110347418  897 AKHKEQNNDsqlKIKE 912
Cdd:NF033838  402 AKRKAAEED---KVKE 414
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1081-1120 2.81e-04

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 43.94  E-value: 2.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 110347418 1081 NLTELSGGQRSLVALSLILSmllfKPAPIYILDEVDAALD 1120
Cdd:cd03237   112 EVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLD 147
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
677-934 2.89e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   677 KFQELKdvQDELRiKENELRALEEELAGLKNTAEKYRQLK---------QQWEMKTE-EADLLQTKLQQSSYHKQQEELD 746
Cdd:pfam17380  292 KFEKME--QERLR-QEKEEKAREVERRRKLEEAEKARQAEmdrqaaiyaEQERMAMErERELERIRQEERKRELERIRQE 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   747 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLEL 826
Cdd:pfam17380  369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   827 EELKREHTSYKQQLeavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTK--QKEVITAQDTVIKAKYAEVAKHKEQnN 904
Cdd:pfam17380  449 ERVRLEEQERQQQV----ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEM-E 523
                          250       260       270
                   ....*....|....*....|....*....|
gi 110347418   905 DSQLKIKEldhniSKHKREAEDGAAKVSKM 934
Cdd:pfam17380  524 ERQKAIYE-----EERRREAEEERRKQQEM 548
PRK12704 PRK12704
phosphodiesterase; Provisional
689-885 2.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  689 RIKENELRALEEELAGL----KNTAEKYRQLKQQwEMKtEEADLLQTKLQQSsYHKQQEELDALKKTIEESEETLKNTKE 764
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALL-EAK-EEIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  765 IQRKAEEKyevLENKMKNAEaERERELKDAQKKLDcaktkadassKKMKEKQQEVEAITleleELKREhtsykqqlEAVN 844
Cdd:PRK12704  104 LLEKREEE---LEKKEKELE-QKQQELEKKEEELE----------ELIEEQLQELERIS----GLTAE--------EAKE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110347418  845 EAIKSYESQIEVMAAEVAKNKEsvNKAQEEVTKQKEVITAQ 885
Cdd:PRK12704  158 ILLEKVEEEARHEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
201-926 3.17e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.21  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   201 EEITPTIQKLKEERSSYLEyqkVMREIEHLSRLYIAYQFLLAEDTKVRSA------EEL----KEMQDKVIKLQEELSEN 270
Cdd:pfam12128  237 MKIRPEFTKLQQEFNTLES---AELRLSHLHFGYKSDETLIASRQEERQEtsaelnQLLrtldDQWKEKRDELNGELSAA 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   271 DKKIKALNHEIEELEKRKdketggilRSLEDALAEaqrvntksQSAFDLKKknlacEESKRKELEkNMVEDSKTLAAKEK 350
Cdd:pfam12128  314 DAAVAKDRSELEALEDQH--------GAFLDADIE--------TAAADQEQ-----LPSWQSELE-NLEERLKALTGKHQ 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   351 EVKKITDGLHALQEASNKDaeALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQEL 430
Cdd:pfam12128  372 DVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   431 KNKQAEV----------KKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN-YEENKEESLLEKRRQLSRDIGRLKETYEAL 499
Cdd:pfam12128  450 KLRLNQAtatpelllqlENFDERIERAREEQEAANAEVERLQSELRQARkRRDQASEALRQASRRLEERQSALDELELQL 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   500 LARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGER-LYNVVVD---TEVTGKKLLERgELKRRyti 575
Cdd:pfam12128  530 FPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnLYGVKLDlkrIDVPEWAASEE-ELRER--- 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   576 iplnkisaRCIAPETLRVAQNLVGPDNVHVALSLVEYKpELQKAMEfvFGTTFVCDNMDNAKKVAFDKRIMTRTVTlggd 655
Cdd:pfam12128  606 --------LDKAEEALQSAREKQAAAEEQLVQANGELE-KASREET--FARTALKNARLDLRRLFDEKQSEKDKKN---- 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   656 vfdphgtlsggaRSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQ---WEMKTEEADLLQTK 732
Cdd:pfam12128  671 ------------KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvveGALDAQLALLKAAI 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   733 LQQSSYHKQQeeLDALKKtieeseetlKNTKEIQRKAEEKYEVlenkmknaeAERERELKDAQKKL-DCAKTKADASSKK 811
Cdd:pfam12128  739 AARRSGAKAE--LKALET---------WYKRDLASLGVDPDVI---------AKLKREIRTLERKIeRIAVRRQEVLRYF 798
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   812 --MKEK-QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmaaevaKNKESVNKAQEEVTkqkEVITAQDTV 888
Cdd:pfam12128  799 dwYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE-------MERKASEKQQVRLS---ENLRGLRCE 868
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 110347418   889 IKaKYAEVAKHKEqNNDSQLKIKE----LDHNISKHKREAED 926
Cdd:pfam12128  869 MS-KLATLKEDAN-SEQAQGSIGErlaqLEDLKLKRDYLSES 908
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1079-1144 3.41e-04

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 42.76  E-value: 3.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418 1079 KENLteLSGGQRSLVALSLilsMLLfKPAPIYILDEVDAALDlSHTQN-IGQMLRTHFTHSQFIVVS 1144
Cdd:cd03228    93 RENI--LSGGQRQRIAIAR---ALL-RDPPILILDEATSALD-PETEAlILEALRALAKGKTVIVIA 152
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
708-936 3.55e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 45.04  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  708 TAEKYRQLKQQWEMKTEEADLLQTKLQQSSYhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKyevlenKMKNAEAER 787
Cdd:PTZ00108 1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMW---LEDLDKFEEALEEQEEVEEKEIAKEQRLKSK------TKGKASKLR 1170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  788 ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEaiksyESQIEVMAAEVAKNKES 867
Cdd:PTZ00108 1171 KPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDD-----EEQKTKPKKSSVKRLKS 1245
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  868 VNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLK 936
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGsKPSSPTKKKVKKRLE 1315
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
144-468 3.86e-04

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 44.79  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  144 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 212
Cdd:PRK10246  152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  213 ERSSYLEYQKVM-REIEHLSRLYIAYQFLLAEDTKVRSA-EELKEMQDKVIKLqeELSENDKKIKALNHEIEELEKRkdk 290
Cdd:PRK10246  231 EEKQLLTAQQQQqQSLNWLTRLDELQQEASRRQQALQQAlAAEEKAQPQLAAL--SLAQPARQLRPHWERIQEQSAA--- 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  291 etggilrsLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK------EVKkitdGLHALQE 364
Cdd:PRK10246  306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnELA----GWRAQFS 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  365 ASNKDAEALAAAQQHFNAVSAGLS---------SNEDGAEA--------TLAGQMMACKNDISKAQTEAKQAQMKLKHAQ 427
Cdd:PRK10246  374 QQTSDREQLRQWQQQLTHAEQKLNalpaitltlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 110347418  428 QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEkLEAEMKKL 468
Cdd:PRK10246  454 QEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
182-392 4.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  182 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE----DTKVRSAE---- 251
Cdd:COG4913   606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaelEAELERLDassd 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  252 ELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggilrsLEDALAEAQRVNTKSQSAFDLKKKNLaceeskR 331
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LEQAEEELDELQDRLEAAEDLARLEL------R 748
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418  332 KELEKnMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNA--------VSAGLSSNED 392
Cdd:COG4913   749 ALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADLESLPE 816
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-462 5.00e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  175 EYKKIAAQ-KTIEKKEAKLKEIKTILEEEIT--PTIQKLKEERSSYLEYQKVMREI--EHLSRLYIAYQFLLAEDTKVRS 249
Cdd:PRK03918  460 ELKRIEKElKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYEKLKEKLIKLKG 539
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  250 --------AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKsqsafdlkK 321
Cdd:PRK03918  540 eikslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA--------E 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQeaSNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagq 401
Cdd:PRK03918  612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEE----- 684
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418  402 mmackndISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE 462
Cdd:PRK03918  685 -------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1082-1132 5.15e-04

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 43.08  E-value: 5.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110347418 1082 LTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:PRK11231  136 LTDLSGGQRQRA----FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1084-1144 5.28e-04

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 43.09  E-value: 5.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347418 1084 ELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLRT-HFTHSQFIVVS 1144
Cdd:COG1122   134 ELSGGQKQRVAIAGVLAM---EP-EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVT 191
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
667-945 5.38e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   667 ARSQAASILTKfQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSsyHKQQEELD 746
Cdd:TIGR00618  201 LRSQLLTLCTP-CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE----AQEEQLKKQQLLKQL--RARIEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   747 ALKKTIEESEETL-------------KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMK 813
Cdd:TIGR00618  274 AQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   814 EK--QQEVEAITLELEELKREHT------SYKQQLEAVNEAIKSYESQIEVMAAEVAknKESVNKAQEEVTKQKEVITAQ 885
Cdd:TIGR00618  354 EIhiRDAHEVATSIREISCQQHTltqhihTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKK 431
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418   886 DTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLKDYDWINAER 945
Cdd:TIGR00618  432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQETRKKAVV 492
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
785-945 5.47e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  785 AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 864
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  865 KESVNKAQ------------EEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 932
Cdd:COG3883    99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
                         170
                  ....*....|...
gi 110347418  933 KMLKDYDWINAER 945
Cdd:COG3883   179 EQEALLAQLSAEE 191
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
180-378 5.74e-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: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  180 AAQKTIEKKEAKLKEIKtileEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaedtkvrsaEELKEMQDK 259
Cdd:COG4942    17 AQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALE----------------------RRIAALARR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  260 VIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI-------------------------------------------- 295
Cdd:COG4942    71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparre 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  296 -LRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALA 374
Cdd:COG4942   151 qAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                  ....
gi 110347418  375 AAQQ 378
Cdd:COG4942   231 RLEA 234
46 PHA02562
endonuclease subunit; Provisional
682-900 6.03e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  682 KDVQDELRIKENELRALEEELAGLKNTAEkyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ-----EELDALKKTIEESE 756
Cdd:PHA02562  177 RELNQQIQTLDMKIDHIQQQIKTYNKNIE--EQRKKNGENIARKQNKYDELVEEAKTIKAEieeltDELLNLVMDIEDPS 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  757 ETLK--NTKEIQRKAE-----------EKYEVLENKMKNAEAERER------ELKDAQKKLDCAKTKADasskKMKEKQQ 817
Cdd:PHA02562  255 AALNklNTAAAKIKSKieqfqkvikmyEKGGVCPTCTQQISEGPDRitkikdKLKELQHSLEKLDTAID----ELEEIMD 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  818 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKqkevitaqdtvIKAKYAEVA 897
Cdd:PHA02562  331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK-----------IVKTKSELV 399

                  ...
gi 110347418  898 KHK 900
Cdd:PHA02562  400 KEK 402
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
665-880 6.07e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  665 GGARSQAASILTKFQELKDVQDELRikeNELRALEEELAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQQSSYHK 740
Cdd:PRK02224  338 QAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRReeieELEEEIEELRERFGDAPVDLGNAEDFL 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  741 Q--QEELDALKKTIEESEETLKNTKEIQRKAE----------------------------EKYEVLENKMKNAEAERER- 789
Cdd:PRK02224  415 EelREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEv 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  790 --------ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEV 861
Cdd:PRK02224  495 eerleraeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
                         250
                  ....*....|....*....
gi 110347418  862 AknkeSVNKAQEEVTKQKE 880
Cdd:PRK02224  575 A----ELNSKLAELKERIE 589
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
641-874 6.23e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.13  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  641 FDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENeLRALEEELAGLKNTAEKYRQlkqqwe 720
Cdd:cd22656    63 FKDDTYPSIVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQD------ 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  721 mkteEADLLQTKLQ--QSSYHKQQEELDALKKTI------EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELK 792
Cdd:cd22656   136 ----KAAKVVDKLTdfENQTEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIA 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  793 DAQKKLDcAKTKADASSKKMKEK----QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmAAEVAKNKesV 868
Cdd:cd22656   212 DDEAKLA-AALRLIADLTAADTDldnlLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIP--AAILAKLE--L 286

                  ....*.
gi 110347418  869 NKAQEE 874
Cdd:cd22656   287 EKAIEK 292
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
679-862 6.45e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  679 QELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWE---MKTEEADLLQTKLQQSSYHKQQEELDALKKTIEE 754
Cdd:COG3883    51 EEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARalyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  755 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHT 834
Cdd:COG3883   131 DADLLEELKADKAELEAKKAELEAKLAELEALKA-ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
                         170       180
                  ....*....|....*....|....*...
gi 110347418  835 SYKQQLEAVNEAIKSYESQIEVMAAEVA 862
Cdd:COG3883   210 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
PRK12704 PRK12704
phosphodiesterase; Provisional
677-812 6.52e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  677 KFQELK-DVQDELRIKENELRALEEELaglkntAEKYRQLKQQWE-MKTEEADLLQtklQQSSYHKQQEELDALKKTIEE 754
Cdd:PRK12704   65 EIHKLRnEFEKELRERRNELQKLEKRL------LQKEENLDRKLElLEKREEELEK---KEKELEQKQQELEKKEEELEE 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418  755 SEETLKntKEIQR-----KAEEKYEVLENKMKNAEAERERELKDAQKKldcAKTKADASSKKM 812
Cdd:PRK12704  136 LIEEQL--QELERisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEE---AKEEADKKAKEI 193
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
242-467 8.22e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  242 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--------LEALQAEIDKLQAEIAEAEAEIEERR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  322 KNLACE-----ESKRKELEKNMVEDSKTLAAkekevkkITDGLHALQEASNKDAEALAAAQQhfnavsaglssnedgAEA 396
Cdd:COG3883    86 EELGERaralyRSGGSVSYLDVLLGSESFSD-------FLDRLSALSKIADADADLLEELKA---------------DKA 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418  397 TLAGQmmacKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKK 467
Cdd:COG3883   144 ELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
27-301 8.30e-04

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.76  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    27 FNAITGLNGSGKSNILDSICFLLGIsnlsqvrASNLQDLVYKNGQAGITKASVSITFDNSDKKqsPLGFEVHdeitvtrq 106
Cdd:pfam13304    1 INVLIGPNGSGKSNLLEALRFLADF-------DALVIGLTDERSRNGGIGGIPSLLNGIDPKE--PIEFEIS-------- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   107 vviggrnKYLINGVNAnntrvqdlfcSVGLNVNNPHFLimqgritkvlnmkppEILSMIEEAAGTRMYEYKKIAaqKTIE 186
Cdd:pfam13304   64 -------EFLEDGVRY----------RYGLDLEREDVE---------------EKLSSKPTLLEKRLLLREDSE--EREP 109
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   187 KKEAKLKEIKTILEEEItpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEE 266
Cdd:pfam13304  110 KFPPEAEELRLGLDVEE--RIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR 187
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 110347418   267 LS----ENDKKIKALNHEIEELEKRKDKETGGILRSLED 301
Cdd:pfam13304  188 LVrglkLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN 226
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
674-909 8.42e-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: 43.47  E-value: 8.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   674 ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAE--KYRQLKQQWEMKTEEADLL----QTKLQQSSYHKQQEELDA 747
Cdd:TIGR04523   49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlNDKLKKNKDKINKLNSDLSkinsEIKNDKEQKNKLEVELNK 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   748 LKKTIEESEETL-KNTKEIQRKAEE------KYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASS------KK 811
Cdd:TIGR04523  129 LEKQKKENKKNIdKFLTEIKKKEKEleklnnKYNDLKKQKEELENELnllEKEKLNIQKNIDKIKNKLLKLElllsnlKK 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   812 MKEKQQEVEAITLELEE----LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI---TA 884
Cdd:TIGR04523  209 KIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIkelEK 288
                          250       260
                   ....*....|....*....|....*
gi 110347418   885 QDTVIKAKYAEVAKHKEQNNDSQLK 909
Cdd:TIGR04523  289 QLNQLKSEISDLNNQKEQDWNKELK 313
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
175-350 8.65e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   175 EYKKIAAQKTIE----KKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQ----KVMREIEHLSRLYI-------AYQF 239
Cdd:pfam17380  338 EQERMAMEREREleriRQEERKRELERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVKIleeerqrKIQQ 417
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   240 LLAEDTKVRSAEElKEMQDKVIKLQEELSENDKKIK----ALNHEIEEL----EKRKDKETGGILRSLEDALAEAQRVNT 311
Cdd:pfam17380  418 QKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRleeqERQQQVERLrqqeEERKRKKLELEKEKRDRKRAEEQRRKI 496
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 110347418   312 KSQSaFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK 350
Cdd:pfam17380  497 LEKE-LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
724-1006 9.28e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   724 EEADLLQTKLQ-QSSYHKQQEE--------LDALKKTIEESEETLKNTKEIQRKaeekyevLENKMKNAEAERERELKDA 794
Cdd:pfam12128  604 ERLDKAEEALQsAREKQAAAEEqlvqangeLEKASREETFARTALKNARLDLRR-------LFDEKQSEKDKKNKALAER 676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   795 QKKLDCAKTKADASSKKMKEKQQEVEAitlELEELKREHTSYKQQ-LEAVNEAIKSYESQIevmaaevaknkesvnkaqe 873
Cdd:pfam12128  677 KDSANERLNSLEAQLKQLDKKHQAWLE---EQKEQKREARTEKQAyWQVVEGALDAQLALL------------------- 734
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   874 evtkqKEVITAQDTVIKAKyaevAKHKEQNNDSQLKIKELD-HNISKHKREAEDGAAKVSKMLKD----YDWINAERHLF 948
Cdd:pfam12128  735 -----KAAIAARRSGAKAE----LKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRrqevLRYFDWYQETW 805
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110347418   949 GQPNSAYDFKTNNPKEAGQRLQ---KLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKR 1006
Cdd:pfam12128  806 LQRRPRLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
PRK12704 PRK12704
phosphodiesterase; Provisional
775-895 9.34e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  775 VLENKMKNAEAERERELKDAQKKLDCAKtkadasSKKMKEKQQEVEAITLELEelkREHTSYKQQLEAVNEAIKSYESQI 854
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENL 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110347418  855 EVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAE 895
Cdd:PRK12704   99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
mukB PRK04863
chromosome partition protein MukB;
687-864 9.64e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  687 ELRIKENELRALEEELAGLKNT--AEKYR--QLKQQWEMKTEEADLLQTKLQQSSYHKQ---------------QEELDA 747
Cdd:PRK04863  280 ERRVHLEEALELRRELYTSRRQlaAEQYRlvEMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqekieryQADLEE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  748 LKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAererELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITL 824
Cdd:PRK04863  360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS----QLADYQQALDVQQTRAIQyqqAVQALERAKQLCGLPDL 435
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110347418  825 ELEELKREHTSYKQQLEAVNEAIKSYESQIEVmaAEVAKN 864
Cdd:PRK04863  436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSV--AQAAHS 473
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
803-945 9.91e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  803 TKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKEsvnkAQEEVTKQKEvi 882
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKE-- 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347418  883 taqdtvIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAER 945
Cdd:COG1579    91 ------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
667-873 1.07e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  667 ARSQAASILTKF--QELKDVQDELRIKENELRALEEElAGLKNTAEKYRQLKQQweMKTEEADLLQTKLQQSSYHKQQEE 744
Cdd:COG3206   168 LRREEARKALEFleEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAA 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  745 LDALKKTIEESEETLKNTKEIQRkaeekyevLENKMKNAEAERER----------ELKDAQKKLdcaktkADASSKKMKE 814
Cdd:COG3206   245 LRAQLGSGPDALPELLQSPVIQQ--------LRAQLAELEAELAElsarytpnhpDVIALRAQI------AALRAQLQQE 310
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSY---ESQIEVMAAEVAKNKES----VNKAQE 873
Cdd:COG3206   311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELyeslLQRLEE 376
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
696-945 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKYEV 775
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  776 LENKMKNAEAERER---ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA-----VNEAI 847
Cdd:COG4372   106 LQEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeAEQAL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  848 KSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEV-AKHKEQNNDSQLKIKELDHNISKHKREAED 926
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlSALLDALELEEDKEELLEEVILKEIEELEL 265
                         250
                  ....*....|....*....
gi 110347418  927 GAAKVSKMLKDYDWINAER 945
Cdd:COG4372   266 AILVEKDTEEEELEIAALE 284
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
251-420 1.11e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETggilRSLEDALAEAQR-----------VNTKSQSAFDL 319
Cdd:COG3883    44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR----EELGERARALYRsggsvsyldvlLGSESFSDFLD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  320 KKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG3883   120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
                         170       180
                  ....*....|....*....|.
gi 110347418  400 GQMMACKNDISKAQTEAKQAQ 420
Cdd:COG3883   200 ELEAELAAAEAAAAAAAAAAA 220
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
807-931 1.19e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  807 ASSKKMKEKQQEVEAITLELEELKREhtsYKQQLEAVNEAIKSYESQIEVMAaevaknKESVNKAQEEVtkqKEVITAQD 886
Cdd:PRK00409  527 ELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEKEA------QQAIKEAKKEA---DEIIKELR 594
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110347418  887 TVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 931
Cdd:PRK00409  595 QLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
1-298 1.47e-03

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


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 42.59  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418     1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSIcfllgisnlsqvrasnlqDLVYKNGQAGITKASVS 80
Cdd:pfam13175    1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEAL------------------DIFLNNKEKFFEDDFLV 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418    81 ITFDNSDKKQSPLgFEVHDEITVTRQVVI-----GGRNKYLINGVNANNTRvQDLFCSVGLNVNNPHFLIMQGRITKVLN 155
Cdd:pfam13175   61 LYLKDVIKIDKED-LNIFENISFSIDIEIdveflLILFGYLEIKKKYLCLA-SKGKAKEYEKTLHPKGANKADLLLELKI 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   156 MKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEakLKEIKTILEEEITPTIQKLKEE--RSSYLEYQKVMREIEHLSRL 233
Cdd:pfam13175  139 SDLKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYE--LPSLKEEFLNSEKEEIKVDKEDlkKLINELEKSINYHENVLENL 216
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347418   234 YIAYQFLLAE-DTKVRSAEELKEMQDKVI--KLQEELSENDKKIKALNHEIEELeKRKDKETGGILRS 298
Cdd:pfam13175  217 QIKKLLISADrNASDEDSEKINSLLGALKqrIFEEALQEELELTEKLKETQNKL-KEIDKTLAEELKN 283
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1066-1120 1.50e-03

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 42.78  E-value: 1.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 110347418  1066 DGLEFKVAlgntwkENLTELSGGQRSLVALSlilsMLLFKPAPIYILDEVDAALD 1120
Cdd:TIGR02203  457 LGLDTPIG------ENGVLLSGGQRQRLAIA----RALLKDAPILILDEATSALD 501
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1085-1134 1.52e-03

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 41.31  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 110347418 1085 LSGGQRSLVALSLilsmLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTH 1134
Cdd:COG4133   132 LSAGQKRRVALAR----LLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
COG5022 COG5022
Myosin heavy chain [General function prediction only];
248-499 1.53e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  248 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-----RKDKETGGILRSLEDA--LAEAQRVNTKSQSAFDLK 320
Cdd:COG5022   786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikreKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLK 865
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  321 KKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHA-LQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG5022   866 KETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESeIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEG 945
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  400 GQMMACKNDISKAQTEAKQaqmKLKHAQQELKNkqaEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLL 479
Cdd:COG5022   946 PSIEYVKLPELNKLHEVES---KLKETSEEYED---LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK 1019
                         250       260
                  ....*....|....*....|...
gi 110347418  480 EKRRQLSR---DIGRLKETYEAL 499
Cdd:COG5022  1020 ELPVEVAElqsASKIISSESTEL 1042
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
794-870 1.62e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  794 AQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNK 870
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
801-878 1.72e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110347418  801 AKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
PTZ00121 PTZ00121
MAEBL; Provisional
667-1005 1.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELaGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELD 746
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAF-GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  747 ALK--KTIEESEETLKNTK-------EIQRKAEEKYEVlENKMKNAEAERERELKDAQ--KKLDCAKTKAD---ASSKKM 812
Cdd:PTZ00121 1141 KAEeaRKAEDAKRVEIARKaedarkaEEARKAEDAKKA-EAARKAEEVRKAEELRKAEdaRKAEAARKAEEerkAEEARK 1219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  813 KEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYES--------QIEVMAAEVAKNKESVNKAQE-----EVTKQK 879
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarmahfarRQAAIKAEEARKADELKKAEEkkkadEAKKAE 1299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  880 EVITAQDTVIKAKYAEVAKH-KEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFK 958
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 110347418  959 TNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKK 1005
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1081-1132 1.82e-03

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 41.57  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110347418 1081 NLTELSGGQRSLVAlsliLSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:COG1120   134 PVDELSGGERQRVL----IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLR 181
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1062-1114 1.84e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 39.94  E-value: 1.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110347418  1062 QTVLDGLEFKVALGNTWKENLTELSGGQRSLVAlsliLSMLLFKPAPIYILDE 1114
Cdd:pfam00005   99 EEALEKLGLGDLADRPVGERPGTLSGGQRQRVA----IARALLTKPKLLLLDE 147
PRK01156 PRK01156
chromosome segregation protein; Provisional
681-902 2.08e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  681 LKDVQDELRIKENEL----RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESE 756
Cdd:PRK01156  185 IDYLEEKLKSSNLELenikKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS--SLEDMKNRYESEIKTAE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  757 ETLKNTKEIQRK---AEEKYEVLENKMKNAEAERERE----------LKDAQKKLDCAKTKADASSKKMKE--------- 814
Cdd:PRK01156  263 SDLSMELEKNNYykeLEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVlqkdyndyi 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  815 -KQQEVEAITLELEELKREHTSYK---QQLEAVNEAIKSYESQIEVMAAEVAK-------NKESVNKAQEEVTKQKEVIT 883
Cdd:PRK01156  343 kKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEilkiqeiDPDAIKKELNEINVKLQDIS 422
                         250
                  ....*....|....*....
gi 110347418  884 AQDTVIKAKYAEVAKHKEQ 902
Cdd:PRK01156  423 SKVSSLNQRIRALRENLDE 441
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
679-811 2.09e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDELRIKENELRALEEELAglkNTAEKYRQLKQQWEMKTEEAdllqtKLQQSSYHKQQEELDALKKTIEESEET 758
Cdd:TIGR02794   80 AEKQRAAEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQKQAEEA-----KAKQAAEAKAKAEAEAERKAKEEAAKQ 151
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110347418   759 LKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKK 811
Cdd:TIGR02794  152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1064-1132 2.38e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 40.59  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418 1064 VLDGLEFkVALGNTWKENLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03235   113 VDEALER-VGLSELADRQIGELSGGQQQRV----LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
679-882 2.42e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   679 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQE------ELDALKKTI 752
Cdd:TIGR04523  426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEK 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   753 EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-------------------RERELKDAQKKLDCAKTKADASSKKMK 813
Cdd:TIGR04523  506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisdledelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQE 585
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418   814 EKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI 882
Cdd:TIGR04523  586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1059-1143 2.67e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 40.85  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1059 PEGQTVLDGLE-FKVALgNTWKENLTELSGGQRSLVALsliLSMLLFKPApIYILDEVDAALDLSHTQNIGQMLrTHFTH 1137
Cdd:PRK10247  112 PDPAIFLDDLErFALPD-TILTKNIAELSGGEKQRISL---IRNLQFMPK-VLLLDEITSALDESNKHNVNEII-HRYVR 185

                  ....*.
gi 110347418 1138 SQFIVV 1143
Cdd:PRK10247  186 EQNIAV 191
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1084-1143 2.75e-03

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 40.54  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418 1084 ELSGGQRSLVALsliLSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:COG4136   133 TLSGGQRARVAL---LRALLAEPRAL-LLDEPFSKLDAALRAQFREFVFEQIRQRGIPAL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
239-481 3.07e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  239 FLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKetggilrsLEDALAEAQRvntksqsafd 318
Cdd:COG3883     4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQA---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  319 lkkknlaceesKRKELEKNMVEDSKTLAAKEKEVKKItdgLHALQEASNK--------DAEALAAAQQHFNAVSAGLSSN 390
Cdd:COG3883    66 -----------EIDKLQAEIAEAEAEIEERREELGER---ARALYRSGGSvsyldvllGSESFSDFLDRLSALSKIADAD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  391 EDgaeatLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNY 470
Cdd:COG3883   132 AD-----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
                         250
                  ....*....|.
gi 110347418  471 EENKEESLLEK 481
Cdd:COG3883   207 AAEAAAAAAAA 217
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
408-482 3.61e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347418  408 DISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKR 482
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
177-425 3.65e-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: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   177 KKIAAQKTIEKKEAKLKEIKtILEEEITPTIQKLkEERSSYLEYQKVmreiehlsrlyiayQFLLAEDTKVRSAEELKEM 256
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFK-ILKDKKDAKIREL-EARVSDLELEKV--------------KLVNAGSERLRAVKDIKQE 654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   257 QDKVIKlQEELSENDKKIKALNHEI---------EELEKRKDK-------------ETGGILRSLEDALAEAQRVNTKSQ 314
Cdd:pfam15921  655 RDQLLN-EVKTSRNELNSLSEDYEVlkrnfrnksEEMETTTNKlkmqlksaqseleQTRNTLKSMEGSDGHAMKVAMGMQ 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   315 SAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDA---EALAAAQQHFNAVSAGLSSNE 391
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVANMEVAL 813
                          250       260       270
                   ....*....|....*....|....*....|....
gi 110347418   392 DGAEAtlagQMMACKNDISKAQTEAkqAQMKLKH 425
Cdd:pfam15921  814 DKASL----QFAECQDIIQRQEQES--VRLKLQH 841
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
689-885 3.77e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   689 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEE--LDALKKTIEESEETLKNTKEIQ 766
Cdd:TIGR02794   54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQaaKQAEEKQKQAEEAKAKQAAEAK 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   767 RKAEEKYEVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSKKMKEKQQEVEAitlelEELKREHTSYKQQLEAv 843
Cdd:TIGR02794  134 AKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-----EEAKAKAEAAKAKAAA- 207
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 110347418   844 nEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 885
Cdd:TIGR02794  208 -EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
251-501 3.86e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   251 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-RKDKETGG--ILRSLEDALAEAQRVNTKSQSAFD------LKK 321
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeLTNSESENseKQRELEEKQNEIEKLKKENQSYKQeiknleSQI 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   322 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE---ATL 398
Cdd:TIGR04523  394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtqlKVL 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   399 AGQMMACKNDISKAQTEAKQAQ---MKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEK----LEAEMKKLNYE 471
Cdd:TIGR04523  474 SRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdLEDELNKDDFE 553
                          250       260       270
                   ....*....|....*....|....*....|
gi 110347418   472 ENKEEsLLEKRRQLSRDIGRLKETYEALLA 501
Cdd:TIGR04523  554 LKKEN-LEKEIDEKNKEIEELKQTQKSLKK 582
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
692-842 4.05e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.21  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  692 ENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqssyhkQQEELDALK------KTIEESEETLKNTKEI 765
Cdd:COG0497   154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRF---------QLEELEAAAlqpgeeEELEEERRRLSNAEKL 224
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347418  766 QRKAEEKYEVLENKMKNAEAererELKDAQKKLDcaktKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA 842
Cdd:COG0497   225 REALQEALEALSGGEGGALD----LLGQALRALE----RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
688-878 4.79e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   688 LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEAdllqtklQQSSYHKQQEELDALKKTIEESEETLKNTKEIQR 767
Cdd:pfam13868    1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEK-------EEERRLDEMMEEERERALEEEEEKEEERKEERKR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   768 KAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYK----QQLEAV 843
Cdd:pfam13868   74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREE 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 110347418   844 NEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 878
Cdd:pfam13868  154 DERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
741-900 4.94e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.60  E-value: 4.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   741 QQEELDALKKTIEEseetlknTKEIQRKAEEKyevleNKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 820
Cdd:TIGR02794   56 QQQKKPAAKKEQER-------QKKLEQQAEEA-----EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   821 AITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK--ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 898
Cdd:TIGR02794  124 AKAKQAAEAKAKAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKaeEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAK 202

                   ..
gi 110347418   899 HK 900
Cdd:TIGR02794  203 AK 204
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
696-855 5.23e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.50  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   696 RALEEELAGLKNTAEKYRQLKQQWEMKTEEadlLQTKLQQssyhkQQEELDALKKTIEESE---ETLKNTKEIQRKAEEK 772
Cdd:pfam13851   29 KSLKEEIAELKKKEERNEKLMSEIQQENKR---LTEPLQK-----AQEEVEELRKQLENYEkdkQSLKNLKARLKVLEKE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   773 -------YEVLENKMKNAEAER-------ERELKDAQKKLDCaktKADASSKKMKEKQQEVEAITLELEELKR----EHT 834
Cdd:pfam13851  101 lkdlkweHEVLEQRFEKVERERdelydkfEAAIQDVQQKTGL---KNLLLEKKLQALGETLEKKEAQLNEVLAaanlDPD 177
                          170       180
                   ....*....|....*....|.
gi 110347418   835 SYKQQLEAVNEAIKSYESQIE 855
Cdd:pfam13851  178 ALQAVTEKLEDVLESKNQLIK 198
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
256-477 6.46e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.58  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   256 MQDKVIKLQEELSENDKKIKALNHEIEELEKrKDKETGGILRSLEDALAEAQRVntksqsafdlkkknlacEESKRKELE 335
Cdd:pfam10174  399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQT-DSSNTDTALTTLEEALSEKERI-----------------IERLKEQRE 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418   336 KNMVEDSKTLAAKEKEVKKITDGLHALQ-EASNKDAEALAAAQQHFNAVSAGLssNEDGAEATLAGQMMACKNDISKAQT 414
Cdd:pfam10174  461 REDRERLEELESLKKENKDLKEKVSALQpELTEKESSLIDLKEHASSLASSGL--KKDSKLKSLEIAVEQKKEECSKLEN 538
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347418   415 EAKQAQM-------------KLKHAQQELKNKQAEVKKMDSGYRKDQEAL---EAVKRLKEKLEAEMKKLNYEENKEES 477
Cdd:pfam10174  539 QLKKAHNaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESLTLRQMKEQN 617
PRK01156 PRK01156
chromosome segregation protein; Provisional
667-884 6.66e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  667 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTaekyrqlkqQWEMKTEEADLLQTKLQQSSYHKQQEELD 746
Cdd:PRK01156  527 ARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---------SWLNALAVISLIDIETNRSRSNEIKKQLN 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  747 ALKKTIEESEETLKNTKEIQ----RKAEEKYEVLENKMKNAEaERERELKDAQKKLDCAKTKadasSKKMKEKQQEVEAI 822
Cdd:PRK01156  598 DLESRLQEIEIGFPDDKSYIdksiREIENEANNLNNKYNEIQ-ENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEI 672
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347418  823 TLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA 884
Cdd:PRK01156  673 TSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
241-370 8.61e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  241 LAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVNTKSQSAFDLK 320
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV--------EELEAELEEKDERIERLERELSEA 453
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110347418  321 KKNLACEESKRKELEK--NMVED-SKTLAAKEKEVKKITDGLHALQEASNKDA 370
Cdd:COG2433   454 RSEERREIRKDREISRldREIERlERELEEERERIEELKRKLERLKELWKLEH 506
COG5022 COG5022
Myosin heavy chain [General function prediction only];
688-866 8.81e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  688 LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTE-EADLLQTKLQQSSYHK---------------QQEELDALKKT 751
Cdd:COG5022   805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKkrfsllkketiylqsAQRVELAERQL 884
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  752 IEESEE--TLKNTKEIQRKAEEKY----------EVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSK------ 810
Cdd:COG5022   885 QELKIDvkSISSLKLVNLELESEIielkkslssdLIENLEFKTELIARLKKLLnniDLEEGPSIEYVKLPELNKlheves 964
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  811 KMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 866
Cdd:COG5022   965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
27-49 9.36e-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: 37.99  E-value: 9.36e-03
                          10        20
                  ....*....|....*....|...
gi 110347418   27 FNAITGLNGSGKSNILDSICFLL 49
Cdd:cd00267    27 IVALVGPNGSGKSTLLRAIAGLL 49
growth_prot_Scy NF041483
polarized growth protein Scy;
663-866 9.44e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.19  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  663 LSGGARSQAASILTKFQELKDVQDELRIKENELRAlEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhkqq 742
Cdd:NF041483  420 LKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA-EAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADA----- 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  743 EELDALKKTieESE----ETLKNTKEIQRKAEEKYEvlenkMKNAEAERERelKDAQKKLDCAKTKADASSKKMKEK-QQ 817
Cdd:NF041483  494 DELRSTATA--ESErvrtEAIERATTLRRQAEETLE-----RTRAEAERLR--AEAEEQAEEVRAAAERAARELREEtER 564
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 110347418  818 EVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 866
Cdd:NF041483  565 AIAARQAEAaEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETE 614
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
190-473 9.65e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  190 AKLKEIKTI-LEEEITPTIQKLKE----------ERSSYLEYQKVMREIEHLSRL------YIAYQFLLAE---DTKVRS 249
Cdd:PRK05771    4 VRMKKVLIVtLKSYKDEVLEALHElgvvhiedlkEELSNERLRKLRSLLTKLSEAldklrsYLPKLNPLREekkKVSVKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  250 AEELKEMQDkviklqEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVntksqSAFDLKKKNLAcees 329
Cdd:PRK05771   84 LEELIKDVE------EELEKIEKEIKELEEEISELENEI--------KELEQEIERLEPW-----GNFDLDLSLLL---- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347418  330 krkeleknmveDSKTLAAKEKEVKKiTDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacKNDI 409
Cdd:PRK05771  141 -----------GFKYVSVFVGTVPE-DKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELK------KLGF 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347418  410 SKAQT-EAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK-DQEALEAVKRLKEKLEAEMKKLNYEEN 473
Cdd:PRK05771  203 ERLELeEEGTPSELIREIKEELEEIEKERESLLEELKElAKKYLEELLALYEYLEIELERAEALSK 268
 
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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