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Conserved domains on  [gi|2796428067|ref|WP_373151603|]
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MULTISPECIES: ATP-binding protein [Bacteroidaceae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
197-555 1.70e-12

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 70.87  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  197 LEQLAKEIASKK---SAIKDELKGIPGRIDSVRDAMPESE--------DWAVLEKEIADKKEKIKDIDSQLADKSKQIEA 265
Cdd:TIGR02169  676 LQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  266 EFKAKSELQKQIGNKKLAKSQRENEIrqnaNKSYHDVLDNiskleyQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlr 345
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLN--- 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  346 gkfyaidaetlqypegaficptcKRELEVEDIQAKQQELQDNFNLNKANRlKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02169  823 -----------------------RLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEELEAALR 878
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  426 QLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENQLKaeakpidttELKEAKATLSEAIDELNKKL 505
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELERKIE---------ELEAQIEKKRKRLS---------ELKAKLEALEEELSEIEDPK 940
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  506 GKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFL-VQDFQ---------KEKDNKLME 555
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaIQEYEevlkrldelKEKRAKLEE 1000
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-97 1.17e-10

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


:

Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 61.56  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGkpilhlvhSVTG 84
Cdd:COG0419     2 LLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEA--------SVEL 73
                          90
                  ....*....|...
gi 2796428067  85 VLSINGRDVELQR 97
Cdd:COG0419    74 EFEHGGKRYRIER 86
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-555 1.70e-12

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: 70.87  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  197 LEQLAKEIASKK---SAIKDELKGIPGRIDSVRDAMPESE--------DWAVLEKEIADKKEKIKDIDSQLADKSKQIEA 265
Cdd:TIGR02169  676 LQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  266 EFKAKSELQKQIGNKKLAKSQRENEIrqnaNKSYHDVLDNiskleyQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlr 345
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLN--- 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  346 gkfyaidaetlqypegaficptcKRELEVEDIQAKQQELQDNFNLNKANRlKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02169  823 -----------------------RLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEELEAALR 878
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  426 QLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENQLKaeakpidttELKEAKATLSEAIDELNKKL 505
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELERKIE---------ELEAQIEKKRKRLS---------ELKAKLEALEEELSEIEDPK 940
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  506 GKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFL-VQDFQ---------KEKDNKLME 555
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaIQEYEevlkrldelKEKRAKLEE 1000
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-97 1.17e-10

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 61.56  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGkpilhlvhSVTG 84
Cdd:COG0419     2 LLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEA--------SVEL 73
                          90
                  ....*....|...
gi 2796428067  85 VLSINGRDVELQR 97
Cdd:COG0419    74 EFEHGGKRYRIER 86
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-539 6.19e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADtnFNIKTLGEDGKPILhlvhSVTGV 85
Cdd:PRK03918    3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKG--LKKDDFTRIGGSGT----EIELK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  86 LSINGRDVELQRNyvekwgSGVNAGVLQNHAtefyLNGVKLKTKKEYDAEVAAILPEDVFrmiTNPLYFptmkAQDQKAM 165
Cdd:PRK03918   77 FEKNGRKYRIVRS------FNRGESYLKYLD----GSEVLEEGDSSVREWVERLIPYHVF---LNAIYI----RQGEIDA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 166 LLE-------MAGNVTN-EEVANINPKFQELISLISGRtLEQLAKEIAS------KKSAIKDELKGIPGRIDSVRDAMPE 231
Cdd:PRK03918  140 ILEsdesrekVVRQILGlDDYENAYKNLGEVIKEIKRR-IERLEKFIKRtenieeLIKEKEKELEEVLREINEISSELPE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 232 -SEDWAVLEKEIAD---KKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKL------AKSQRENEIRQNANK---- 297
Cdd:PRK03918  219 lREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleEKVKELKELKEKAEEyikl 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 298 -----SYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDaetlqypegaficptcKREL 372
Cdd:PRK03918  299 sefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE----------------ERHE 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 373 EVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKG--------N 444
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcG 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 445 MPEEQDTQKIILSDPTwLSLSN------EIVDLENQLKAEAKPIDTTELKEAK----ATLSEAIDELNKKLGKRDtIERS 514
Cdd:PRK03918  443 RELTEEHRKELLEEYT-AELKRiekelkEIEEKERKLRKELRELEKVLKKESEliklKELAEQLKELEEKLKKYN-LEEL 520
                         570       580
                  ....*....|....*....|....*
gi 2796428067 515 NKVIEDLEDRRDKNNEALAEQERLE 539
Cdd:PRK03918  521 EKKAEEYEKLKEKLIKLKGEIKSLK 545
AAA_23 pfam13476
AAA domain;
9-214 1.03e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 58.28  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   9 LILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTlgedGKPILHLVHSVTGVLSI 88
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVK----GDIRIGLEGKGKAYVEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  89 NGRDVELQRNYVEKWGSGVNagvlQNHATEFYLNGVKLKTKKEYDAEVAAILPEDvFRMITNPLYFPtmkaQDQKAMLLE 168
Cdd:pfam13476  77 TFENNDGRYTYAIERSRELS----KKKGKTKKKEILEILEIDELQQFISELLKSD-KIILPLLVFLG----QEREEEFER 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2796428067 169 MAgnvTNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDE 214
Cdd:pfam13476 148 KE---KKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-539 1.95e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   1 MKevfLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLfgkdstnradtnfnIKTLGEDGKPIlhlvh 80
Cdd:COG4717     1 MK---IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------LERLEKEADEL----- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  81 svtgvLSINGRDVELQRNYVEKWGSgvnagvlqnhatefylngvKLKTKKEYDAEVAAilpedvfrmitnplyfptmkAQ 160
Cdd:COG4717    59 -----FKPQGRKPELNLKELKELEE-------------------ELKEAEEKEEEYAE--------------------LQ 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 161 DQKAMLlemagnvtNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMpesedwavleK 240
Cdd:COG4717    95 EELEEL--------EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL----------E 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 241 EIADKKEKIKDIDSQLADKSKQIEAEFKAKSElqkqignkklaksQRENEIRQNAnksyhdvlDNISKLEYQVKSKDAEI 320
Cdd:COG4717   157 ELRELEEELEELEAELAELQEELEELLEQLSL-------------ATEEELQDLA--------EELEELQQRLAELEEEL 215
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 321 SRKQEEHSRIKANIEALNNDLE----------------------VLRGKFYAIDAETLQYPEGAFIC---------PTCK 369
Cdd:COG4717   216 EEAQEELEELEEELEQLENELEaaaleerlkearlllliaaallALLGLGGSLLSLILTIAGVLFLVlgllallflLLAR 295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 370 RELEVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSN----EKEILVHNINEC---- 441
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeelEEELQLEELEQEiaal 375
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 442 --KGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKAEAKPI-------DTTELKEAKATLSEAIDELNKKLGK-RDTI 511
Cdd:COG4717   376 laEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealDEEELEEELEELEEELEELEEELEElREEL 455
                         570       580
                  ....*....|....*....|....*...
gi 2796428067 512 ERSNKVIEDLEDRRDKnNEALAEQERLE 539
Cdd:COG4717   456 AELEAELEQLEEDGEL-AELLQELEELK 482
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
5-64 3.89e-05

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: 46.44  E-value: 3.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   5 FLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFN 64
Cdd:pfam13175   2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVL 61
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
6-143 6.20e-05

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: 45.37  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKdSTNRAdtnfNIKTLGEDGKPilhlVHSVTGV 85
Cdd:cd03242     1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK-SHRTS----RDKELIRWGAE----EAKISAV 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  86 LSINGRDVELQRNYVEKWGSGVNagvlqnhatefyLNGVKLKTKKEYDAEVAAIL--PED 143
Cdd:cd03242    72 LERQGGELALELTIRSGGGRKAR------------LNGIKVRRLSDLLGVLNAVWfaPED 119
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-555 1.70e-12

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: 70.87  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  197 LEQLAKEIASKK---SAIKDELKGIPGRIDSVRDAMPESE--------DWAVLEKEIADKKEKIKDIDSQLADKSKQIEA 265
Cdd:TIGR02169  676 LQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  266 EFKAKSELQKQIGNKKLAKSQRENEIrqnaNKSYHDVLDNiskleyQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlr 345
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLN--- 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  346 gkfyaidaetlqypegaficptcKRELEVEDIQAKQQELQDNFNLNKANRlKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02169  823 -----------------------RLTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGKKEELEEELEELEAALR 878
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  426 QLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENQLKaeakpidttELKEAKATLSEAIDELNKKL 505
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELERKIE---------ELEAQIEKKRKRLS---------ELKAKLEALEEELSEIEDPK 940
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  506 GKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFL-VQDFQ---------KEKDNKLME 555
Cdd:TIGR02169  941 GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLaIQEYEevlkrldelKEKRAKLEE 1000
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5-538 9.56e-11

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: 65.46  E-value: 9.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067    5 FLKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLfGKDSTN--RADTNFNIKTLGEDGKPILHLVhS 81
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTtINFDKGITGIVGPNGCGKSNIVDAIRWVL-GEQSAKalRGGKMEDVIFNGSETRKPLSLA-E 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   82 VTGVLS-INGRDVELQRNYVEkwgsgVNAGVLQNHATEFYLNGVKLKTKKEYD--------AEVAAILPEDVFRMITNPl 152
Cdd:TIGR02168   79 VELVFDnSDGLLPGADYSEIS-----ITRRLYRDGESEYFINGQPCRLKDIQDlfldtglgKRSYSIIEQGKISEIIEA- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  153 yfptmKAQDQKAMLLEMAG---------------NVTNEEVANINPKFQELislisGRTLEQLAK--EIASKKSAIKDEL 215
Cdd:TIGR02168  153 -----KPEERRAIFEEAAGiskykerrketerklERTRENLDRLEDILNEL-----ERQLKSLERqaEKAERYKELKAEL 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  216 KGIpgridsvrdampeseDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQnA 295
Cdd:TIGR02168  223 REL---------------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-L 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  296 NKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEgaficptcKRELEVE 375
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------ELESLEA 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  376 DIQAKQQELQdnfnlNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPE---EQDTQ 452
Cdd:TIGR02168  359 ELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkKLEEA 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  453 KIILSDPTWLSLSNEIVDLENQLKA--EAKPIDTTELKEAKATLSEAIDELNKKLGKRDTIERsnkVIEDLEDRRDKNNE 530
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERleEALEELREELEEAEQALDAAERELAQLQARLDSLER---LQENLEGFSEGVKA 510

                   ....*...
gi 2796428067  531 ALAEQERL 538
Cdd:TIGR02168  511 LLKNQSGL 518
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
6-97 1.17e-10

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 61.56  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGkpilhlvhSVTG 84
Cdd:COG0419     2 LLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEA--------SVEL 73
                          90
                  ....*....|...
gi 2796428067  85 VLSINGRDVELQR 97
Cdd:COG0419    74 EFEHGGKRYRIER 86
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-556 1.48e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 64.70  E-value: 1.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067    5 FLKKLILKNFKKIQDLTV-EFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTN-RADTNFNIKTLGEDGKPILHLvhSV 82
Cdd:TIGR02169    1 YIERIELENFKSFGKKKViPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAmRAERLSDLISNGKNGQSGNEA--YV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   83 TGVLSINGR-----DVELQRNYVEKwgsgvnagvlQNHATEFYLNGVKLkTKKEYDAEVAA--ILPE--------DVFRM 147
Cdd:TIGR02169   79 TVTFKNDDGkfpdeLEVVRRLKVTD----------DGKYSYYYLNGQRV-RLSEIHDFLAAagIYPEgynvvlqgDVTDF 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  148 ITnplyfptMKAQDQKAMLLEMAG---------NVTNE-EVANINPKFQELISLISGRTLEQLAKE--IASKKSAIKDEL 215
Cdd:TIGR02169  148 IS-------MSPVERRKIIDEIAGvaefdrkkeKALEElEEVEENIERLDLIIDEKRQQLERLRREreKAERYQALLKEK 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  216 KGIPG--RIDSVRDAMPESEDwavLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkklaKSQRENEIRQ 293
Cdd:TIGR02169  221 REYEGyeLLKEKEALERQKEA---IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLR 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  294 nANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGkfyaidaetlqypegaficptckrelE 373
Cdd:TIGR02169  292 -VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER--------------------------E 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  374 VEDIQAKQQELQDnfnlnkanRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQK 453
Cdd:TIGR02169  345 IEEERKRRDKLTE--------EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  454 iilsdptwlSLSNEIVDLENQLK-AEAKpidtteLKEAKATLSEAIDELNKKLGKRDTIersnkvIEDLEDRRDKNNEAL 532
Cdd:TIGR02169  417 ---------RLSEELADLNAAIAgIEAK------INELEEEKEDKALEIKKQEWKLEQL------AADLSKYEQELYDLK 475
                          570       580
                   ....*....|....*....|....
gi 2796428067  533 AEQERLEFLVQDFQKEKDNKLMER 556
Cdd:TIGR02169  476 EEYDRVEKELSKLQRELAEAEAQA 499
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
6-539 6.19e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADtnFNIKTLGEDGKPILhlvhSVTGV 85
Cdd:PRK03918    3 IEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKG--LKKDDFTRIGGSGT----EIELK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  86 LSINGRDVELQRNyvekwgSGVNAGVLQNHAtefyLNGVKLKTKKEYDAEVAAILPEDVFrmiTNPLYFptmkAQDQKAM 165
Cdd:PRK03918   77 FEKNGRKYRIVRS------FNRGESYLKYLD----GSEVLEEGDSSVREWVERLIPYHVF---LNAIYI----RQGEIDA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 166 LLE-------MAGNVTN-EEVANINPKFQELISLISGRtLEQLAKEIAS------KKSAIKDELKGIPGRIDSVRDAMPE 231
Cdd:PRK03918  140 ILEsdesrekVVRQILGlDDYENAYKNLGEVIKEIKRR-IERLEKFIKRtenieeLIKEKEKELEEVLREINEISSELPE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 232 -SEDWAVLEKEIAD---KKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKL------AKSQRENEIRQNANK---- 297
Cdd:PRK03918  219 lREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleEKVKELKELKEKAEEyikl 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 298 -----SYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDaetlqypegaficptcKREL 372
Cdd:PRK03918  299 sefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE----------------ERHE 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 373 EVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKG--------N 444
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcG 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 445 MPEEQDTQKIILSDPTwLSLSN------EIVDLENQLKAEAKPIDTTELKEAK----ATLSEAIDELNKKLGKRDtIERS 514
Cdd:PRK03918  443 RELTEEHRKELLEEYT-AELKRiekelkEIEEKERKLRKELRELEKVLKKESEliklKELAEQLKELEEKLKKYN-LEEL 520
                         570       580
                  ....*....|....*....|....*
gi 2796428067 515 NKVIEDLEDRRDKNNEALAEQERLE 539
Cdd:PRK03918  521 EKKAEEYEKLKEKLIKLKGEIKSLK 545
AAA_23 pfam13476
AAA domain;
9-214 1.03e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 58.28  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   9 LILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTlgedGKPILHLVHSVTGVLSI 88
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVK----GDIRIGLEGKGKAYVEI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  89 NGRDVELQRNYVEKWGSGVNagvlQNHATEFYLNGVKLKTKKEYDAEVAAILPEDvFRMITNPLYFPtmkaQDQKAMLLE 168
Cdd:pfam13476  77 TFENNDGRYTYAIERSRELS----KKKGKTKKKEILEILEIDELQQFISELLKSD-KIILPLLVFLG----QEREEEFER 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2796428067 169 MAgnvTNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDE 214
Cdd:pfam13476 148 KE---KKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
239-540 1.33e-09

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: 61.61  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  239 EKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRqNANKSYHDVLDNISKLEYQVKSKDA 318
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  319 EISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEGAFicptcKRELEVEDIQAKQQELQDNFnLNKANRLKA 398
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-----ALREALDELRAELTLLNEEA-ANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  399 VQNEGKEKAAKVEELKKQcsiiqatITQLSNEKEILVHNINECKGNMPEEQDtqkiilsdptwlslsnEIVDLENQLKAE 478
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELES----------------ELEALLNERASL 885
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  479 AKPIDttELKEAKATLSEAIDELNKKLGK--------RDTIERSNKVIEDLEDRRDKNNEALAEQERLEF 540
Cdd:TIGR02168  886 EEALA--LLRSELEELSEELRELESKRSElrreleelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
5-58 3.70e-09

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: 58.86  E-value: 3.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2796428067   5 FLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAfLWLLFGKDSTNR 58
Cdd:COG3593     2 KLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEA-LRLLLGPSSSRK 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-563 1.37e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  272 ELQKQIGNKKLAKSQRENEIR--------QNANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEV 343
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  344 LRGKFYAIDAetlqypegaficptckrelEVEDIQAKQQELQDnfnlnkanRLKAVQNEGKEKAAKVEELKKQCSIIQAT 423
Cdd:TIGR02168  286 LQKELYALAN-------------------EISRLEQQKQILRE--------RLANLERQLEELEAQLEELESKLDELAEE 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  424 ITQLSNEKEILVHNINECKGNMPEEQDT-----QKIILSDPTWLSLSNEIVDLENQLKAEAKPIDT-----TELKEAKAT 493
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAEleeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERlearlERLEDRRER 418
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796428067  494 LSEAIDELNKKLGKRD------TIERSNKVIEDLEDRRDKNNEALAE-QERLEFLVQDFQKEKD--NKLMERINGMFSL 563
Cdd:TIGR02168  419 LQQEIEELLKKLEEAElkelqaELEELEEELEELQEELERLEEALEElREELEEAEQALDAAERelAQLQARLDSLERL 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-539 1.95e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   1 MKevfLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLfgkdstnradtnfnIKTLGEDGKPIlhlvh 80
Cdd:COG4717     1 MK---IKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML--------------LERLEKEADEL----- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  81 svtgvLSINGRDVELQRNYVEKWGSgvnagvlqnhatefylngvKLKTKKEYDAEVAAilpedvfrmitnplyfptmkAQ 160
Cdd:COG4717    59 -----FKPQGRKPELNLKELKELEE-------------------ELKEAEEKEEEYAE--------------------LQ 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 161 DQKAMLlemagnvtNEEVANINPKFQELISLISGRTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMpesedwavleK 240
Cdd:COG4717    95 EELEEL--------EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL----------E 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 241 EIADKKEKIKDIDSQLADKSKQIEAEFKAKSElqkqignkklaksQRENEIRQNAnksyhdvlDNISKLEYQVKSKDAEI 320
Cdd:COG4717   157 ELRELEEELEELEAELAELQEELEELLEQLSL-------------ATEEELQDLA--------EELEELQQRLAELEEEL 215
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 321 SRKQEEHSRIKANIEALNNDLE----------------------VLRGKFYAIDAETLQYPEGAFIC---------PTCK 369
Cdd:COG4717   216 EEAQEELEELEEELEQLENELEaaaleerlkearlllliaaallALLGLGGSLLSLILTIAGVLFLVlgllallflLLAR 295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 370 RELEVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSN----EKEILVHNINEC---- 441
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeelEEELQLEELEQEiaal 375
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 442 --KGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKAEAKPI-------DTTELKEAKATLSEAIDELNKKLGK-RDTI 511
Cdd:COG4717   376 laEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealDEEELEEELEELEEELEELEEELEElREEL 455
                         570       580
                  ....*....|....*....|....*...
gi 2796428067 512 ERSNKVIEDLEDRRDKnNEALAEQERLE 539
Cdd:COG4717   456 AELEAELEQLEEDGEL-AELLQELEELK 482
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-431 2.15e-08

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: 57.77  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  184 KFQELISLISGRTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPESE-DWAVLEKEIADKKEKIKDIDSQLADKSKQ 262
Cdd:TIGR02169  776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  263 IEAEFKAKSELQKQIGNKKLAKSQREneirqnanKSYHDVLDNISKLEYQVKskdaEISRKQEEhsrIKANIEALNNDLE 342
Cdd:TIGR02169  856 IENLNGKKEELEEELEELEAALRDLE--------SRLGDLKKERDELEAQLR----ELERKIEE---LEAQIEKKRKRLS 920
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  343 VLRGKFYAIDAETLQY-PEGAFICPTCKRELEVEDIQAKQQELQDNFNLNKANRLKAVQ---------NEGKEKAAKVEE 412
Cdd:TIGR02169  921 ELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQeyeevlkrlDELKEKRAKLEE 1000
                          250
                   ....*....|....*....
gi 2796428067  413 LKKQcsiIQATITQLSNEK 431
Cdd:TIGR02169 1001 ERKA---ILERIEEYEKKK 1016
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
196-557 1.38e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 196 TLEQLAKEIASKKSAIKDELKGIPGRIDSVR-DAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQ 274
Cdd:PRK02224  311 AVEARREELEDRDEELRDRLEECRVAAQAHNeEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 275 KQIgnkklaksqRENEirqnanKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEvlrgkfyaiDAE 354
Cdd:PRK02224  391 EEI---------EELR------ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE---------EAE 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 355 TLQyPEGAfiCPTCKRELE-------VEDIQAKQQELQDNFNlnkanRLKAVQNEGKEKAAKVEELKKQcsiiQATITQL 427
Cdd:PRK02224  447 ALL-EAGK--CPECGQPVEgsphvetIEEDRERVEELEAELE-----DLEEEVEEVEERLERAEDLVEA----EDRIERL 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 428 SNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDLENqlKAEAKPIDTTELKEAKATLSEAIDELNKKLGK 507
Cdd:PRK02224  515 EERREDLEELIAERRETIEEKRERAE---------ELRERAAELEA--EAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2796428067 508 -RDTIERSNKV------IEDLEDRRDKNNEALAEQERLEflvqDFQKEKDNKLMERI 557
Cdd:PRK02224  584 lKERIESLERIrtllaaIADAEDEIERLREKREALAELN----DERRERLAEKRERK 636
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
8-551 2.19e-07

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: 54.20  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067    8 KLILKNFKKIQDL-TVEFTDKNTF--ICGGNGTGKTTLQDAFLWLLFGK-----------DSTNRADTNFNIKTLGEDGK 73
Cdd:TIGR00618    5 RLTLKNFGSYKGThTIDFTALGPIflICGKTGAGKTTLLDAITYALYGKlprrsevirslNSLYAAPSEAAFAELEFSLG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   74 PILHLVHSVTGVlSINGRDVEL--QRNYVEKWGSGVNAGVLQNHATEFYLNGVKLKTKKeydAEVAAILPEDVFRMITNP 151
Cdd:TIGR00618   85 TKIYRVHRTLRC-TRSHRKTEQpeQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKT---FTRVVLLPQGEFAQFLKA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  152 LyfPTMKAQ--------DQKAMLLEMAGNVTNEEVANINpKFQELISLISgRTLEQLAKEIASKKSAIKDELKgipgRID 223
Cdd:TIGR00618  161 K--SKEKKEllmnlfplDQYTQLALMEFAKKKSLHGKAE-LLTLRSQLLT-LCTPCMPDTYHERKQVLEKELK----HLR 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  224 SVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKK-----LAKSQRENEIRQNANKS 298
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplAAHIKAVTQIEQQAQRI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  299 YHDVLDNISKLE--------YQVKSKDAEISRK-------QEEHSRIKAN------------------IEALNNDLEVLR 345
Cdd:TIGR00618  313 HTELQSKMRSRAkllmkraaHVKQQSSIEEQRRllqtlhsQEIHIRDAHEvatsireiscqqhtltqhIHTLQQQKTTLT 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  346 GKFYAIDAETLQY-PEGAFICPTCKRELEV----------EDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELK 414
Cdd:TIGR00618  393 QKLQSLCKELDILqREQATIDTRTSAFRDLqgqlahakkqQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  415 KQCSIIQATITQLSNEKEILVHNINECKGNMPE--------EQDTQKIILSDPT----------WLSLSNEIVDLENQLK 476
Cdd:TIGR00618  473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgscihpNPARQDIDNPGPLtrrmqrgeqtYAQLETSEEDVYHQLT 552
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796428067  477 AEAKpidttELKEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDN 551
Cdd:TIGR00618  553 SERK-----QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
195-355 3.80e-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: 51.46  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 195 RTLEQLAkEIASKKSAIKDELKGIPGRIDSVRDampeseDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQ 274
Cdd:COG1579     7 RALLDLQ-ELDSELDRLEHRLKELPAELAELED------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 275 KQIGNkklAKSQRE-----NEIRQNANKsyhdvldnISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFY 349
Cdd:COG1579    80 EQLGN---VRNNKEyealqKEIESLKRR--------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148

                  ....*.
gi 2796428067 350 AIDAET 355
Cdd:COG1579   149 EELAEL 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
233-548 5.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 233 EDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkkLAKSQRENEIRQnanksyhdvldNISKLEyq 312
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL----EEAQAEEYELLA-----------ELARLE-- 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 313 vkskdAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQypegaficptckRELEVEDIQAKQQELQDNFNLNK 392
Cdd:COG1196   302 -----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEE------------LEEELEEAEEELEEAEAELAEAE 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 393 ANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHnineckgnmpEEQDTQKIIlsdptwlSLSNEIVDLE 472
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA----------EEALLERLE-------RLEEELEELE 427
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067 473 NQLKAEAKPIDTTELKEAKATLSEAiDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQDFQKE 548
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
5-64 8.32e-07

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: 8.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796428067   5 FLKKLILKNFKKIQDLTVEFTDKN--TFICGGNGTGKTTLQDAfLWLLFGKDSTNRADTNFN 64
Cdd:COG3950     2 RIKSLTIENFRGFEDLEIDFDNPPrlTVLVGENGSGKTTLLEA-IALALSGLLSRLDDVKFR 62
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
176-527 1.23e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 176 EEVANINPKFQELISLISGRtLEQLAKEIASKKSAIkDELKGIPGRIDSVRDAMPESEDWAVLE------KEIADKKEKI 249
Cdd:PRK03918  394 EELEKAKEEIEEEISKITAR-IGELKKEIKELKKAI-EELKKAKGKCPVCGRELTEEHRKELLEeytaelKRIEKELKEI 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 250 KDIDSQLADKSKQIEAEFKAKSELQKqigNKKLAKSQRENEIR---------QNANKSYHDVLDNISKLEYQVKSKDAEI 320
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIK---LKELAEQLKELEEKlkkynleelEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 321 SRKQEehsrIKANIEALNNDLEVLRGKFYAIDAETLqypEGAFICptckreleVEDIQAKQQELQDNFNlnKANRLKAVQ 400
Cdd:PRK03918  549 EKLEE----LKKKLAELEKKLDELEEELAELLKELE---ELGFES--------VEELEERLKELEPFYN--EYLELKDAE 611
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 401 NEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKiilsDPTWLSLSNEIVDLENQLKAEAK 480
Cdd:PRK03918  612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL----REEYLELSRELAGLRAELEELEK 687
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2796428067 481 PIDttelkEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDK 527
Cdd:PRK03918  688 RRE-----EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-516 1.33e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  197 LEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPESE----DWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSE 272
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  273 LQKQIGNKKLAKSQRENEIR------QNANKSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRg 346
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE- 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  347 kfyaIDAETLQypegaficptckRELEVEDIQAKQQELQdnfnLNKAN-RLKAVQNEGKEKAAKVEELKKQCSIIQATIT 425
Cdd:TIGR02168  866 ----ELIEELE------------SELEALLNERASLEEA----LALLRsELEELSEELRELESKRSELRRELEELREKLA 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  426 QLSNEKEILVHNINECKGNMPEE-QDTQKIILS-----DPTWLSLSNEIVDLENQLKA----------EAKPIDT----- 484
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERLSEEySLTLEEAEAlenkiEDDEEEARRRLKRLENKIKElgpvnlaaieEYEELKErydfl 1005
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2796428067  485 ----TELKEAKATLSEAIDELNKKLGKR--DTIERSNK 516
Cdd:TIGR02168 1006 taqkEDLTEAKETLEEAIEEIDREARERfkDTFDQVNE 1043
COG4637 COG4637
Predicted ATPase [General function prediction only];
6-49 2.30e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 50.31  E-value: 2.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFIcGGNGTGKTTLQDAFLWL 49
Cdd:COG4637     2 ITRIRIKNFKSLRDLELPLGPLTVLI-GANGSGKSNLLDALRFL 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
197-432 2.39e-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: 50.15  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKKSAIKDELKgipgRIDSVRDAMpesedwAVLEKEIADKKEKIKDIDSQLADKSKQIEaefkaksELQKQ 276
Cdd:COG4942    29 LEQLQQEIAELEKELAALKK----EEKALLKQL------AALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 277 IGNKKLAKSQRENEIRQNANKSYhdVLDNISKLEYQVKSKDA-EISRKQEEHSRI----KANIEALNNDLEVLRGKFYAI 351
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFlDAVRRLQYLKYLaparREQAEELRADLAELAALRAEL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 352 DAETLQypegaficptcKRELEVEdIQAKQQELQDNFNlNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEK 431
Cdd:COG4942   170 EAERAE-----------LEALLAE-LEEERAALEALKA-ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236

                  .
gi 2796428067 432 E 432
Cdd:COG4942   237 A 237
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
5-578 2.76e-06

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: 50.74  E-value: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067    5 FLKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGEDGKPILHLvhSVT 83
Cdd:pfam02463    1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSA--EVE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   84 GVLSINGRDVelqrnYVEKWGSGVNAGVLQNHATEFYLNGvKLKTKKEYdaevaAILPEDVFRMITNPlyfptmkaqdqk 163
Cdd:pfam02463   79 ITFDNEDHEL-----PIDKEEVSIRRRVYRGGDSEYYING-KNVTKKEV-----AELLESQGISPEAY------------ 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  164 aMLLEMAGNVTNeeVANINPKFQELISLISGRTLEQLAKEIASKKSA-IKDELKGIPGRIDSVRDAMPESEDWAVLEKEI 242
Cdd:pfam02463  136 -NFLVQGGKIEI--IAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKEQAKKALEY 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  243 ADKKEKIKDIDS-QLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKSKDAEIS 321
Cdd:pfam02463  213 YQLKEKLELEEEyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  322 RKQEEHSRIKANIEALNNDLEvlrgkfyaidaetlqypegaficptckRELEVEDIQAKQQELQDNFNLNKANRLKAVQN 401
Cdd:pfam02463  293 KEEEELKSELLKLERRKVDDE---------------------------EKLKESEKEKKKAEKELKKEKEEIEELEKELK 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  402 EGKEKAAKVEELKKQCSiiqatitQLSNEKEILVHNINECKGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKAEAKP 481
Cdd:pfam02463  346 ELEIKREAEEEEEEELE-------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  482 IDTTELKEAKATLSEAIDELNKKLGKRDTIERSNkvIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLM-ERINGM 560
Cdd:pfam02463  419 DLLKEEKKEELEILEEEEESIELKQGKLTEEKEE--LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLlSRQKLE 496
                          570
                   ....*....|....*...
gi 2796428067  561 FSLVKFSFISEKLNGNEA 578
Cdd:pfam02463  497 ERSQKESKARSGLKVLLA 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-421 2.87e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  184 KFQELISLISGR------TLEQLAKEIASKKS----AIKDELKGIPGRIDSVRDAMPESEDWAV-LEKEIADKKEKIKDI 252
Cdd:TIGR02169  255 KLTEEISELEKRleeieqLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKL 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  253 DSQLADKSKQIEAEFKAKSELQKQIGNKK--LAKSQRENEIRQNANKSYHDVLDN----ISKLEYQVKSKDAEISRKQEE 326
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKeeLEDLRAELEEVDKEFAETRDELKDyrekLEKLKREINELKRELDRLQEE 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  327 HSRIKANIEALNNDLEVLRGKFYAIDAETLqypegAFICPTCKRELEVEDIQAKQQELQDNFnLNKANRLKAVQNEGKEK 406
Cdd:TIGR02169  415 LQRLSEELADLNAAIAGIEAKINELEEEKE-----DKALEIKKQEWKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKL 488
                          250
                   ....*....|....*
gi 2796428067  407 AAKVEELKKQCSIIQ 421
Cdd:TIGR02169  489 QRELAEAEAQARASE 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
240-505 6.73e-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: 48.99  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 240 KEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIG--NKKLAKSQREneirqnanksyhdvldnISKLEYQVKSKD 317
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARR-----------------IRALEQELAALE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDaetlQYPEGAFIcptckreLEVEDIQ--AKQQELQDNFNLNKANR 395
Cdd:COG4942    83 AELAELEKEIAELRAELEAQKEELAELLRALYRLG----RQPPLALL-------LSPEDFLdaVRRLQYLKYLAPARREQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 396 LKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKiilsdptwlSLSNEIVDL---E 472
Cdd:COG4942   152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA---------ELAAELAELqqeA 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2796428067 473 NQLKAEAKPIDTTELKEAKATLSEAIDELNKKL 505
Cdd:COG4942   223 EELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
5-64 3.89e-05

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: 46.44  E-value: 3.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   5 FLKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFN 64
Cdd:pfam13175   2 KIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVL 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
172-416 4.32e-05

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: 46.97  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  172 NVTNEEVANINPKFQELISLISgrTLEQLAKEIASKKSAIKDELKGIPGRIDSVRDAMPE-SEDWAVLEKEIADKKEKIK 250
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIE--ELEAQIEQLKEELKALREALDELRAELTLLNEEAANlRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  251 DIDSQLADKSKQIEA-------EFKAKSELQKQIgNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKSKDAEISRK 323
Cdd:TIGR02168  842 DLEEQIEELSEDIESlaaeieeLEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  324 QEEHSRIKANIEALNNDLEVLRGKFyaidAETLQYPEGAFICPTCKRELEVEDIQAKQQELQdnfnlNKANRLKAVQ--- 400
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQERL----SEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----NKIKELGPVNlaa 991
                          250
                   ....*....|....*..
gi 2796428067  401 -NEGKEKAAKVEELKKQ 416
Cdd:TIGR02168  992 iEEYEELKERYDFLTAQ 1008
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
246-557 4.58e-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: 46.64  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 246 KEKIKDIDSQLADKSKQIEAEFKAKSELqkQIGNKKLAkSQRENEIRQNANK-SYHDVLDNISKLEYQVKSKDAEISRKQ 324
Cdd:pfam05483  98 EAELKQKENKLQENRKIIEAQRKAIQEL--QFENEKVS-LKLEEEIQENKDLiKENNATRHLCNLLKETCARSAEKTKKY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 325 E-EHSRIKANIEALNNDLEVLRGKFYAIDAETlqypEGAFICPTCKRELEVEDIQAKQQELQDNFN-------------L 390
Cdd:pfam05483 175 EyEREETRQVYMDLNNNIEKMILAFEELRVQA----ENARLEMHFKLKEDHEKIQHLEEEYKKEINdkekqvsllliqiT 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 391 NKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKIILSD-----PTWLSLS 465
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlqiatKTICQLT 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 466 NEI-VDLENQLKAEAK-PIDTTELKEAKATLSEAIDELNKKLGKRD------TIERSNKVIEDLEDRRDKNNEALAEQER 537
Cdd:pfam05483 331 EEKeAQMEELNKAKAAhSFVVTEFEATTCSLEELLRTEQQRLEKNEdqlkiiTMELQKKSSELEEMTKFKNNKEVELEEL 410
                         330       340
                  ....*....|....*....|
gi 2796428067 538 LEFLVQDFQKEKDNKLMERI 557
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKI 430
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
304-544 5.11e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  304 DNISKLEyqvkSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYA-----------IDAETLQypegaficptckrel 372
Cdd:COG4913    607 DNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswdeIDVASAE--------------- 667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  373 evEDIQAKQQELQDnfnLNKAN-RLKAVQNEGKEKAAKVEELKKQcsiiqatITQLSNEKEILVHNINECKgnmpEEQDT 451
Cdd:COG4913    668 --REIAELEAELER---LDASSdDLAALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAE----EELDE 731
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  452 QKIILSDPTWLSLSNEIVDLENQLKAEAkpiDTTELKEAKATLSEAIDELNKKLGK-----RDTIERSNKVIEDLEDRRD 526
Cdd:COG4913    732 LQDRLEAAEDLARLELRALLEERFAAAL---GDAVERELRENLEERIDALRARLNRaeeelERAMRAFNREWPAETADLD 808
                          250
                   ....*....|....*....
gi 2796428067  527 KNNEALAE-QERLEFLVQD 544
Cdd:COG4913    809 ADLESLPEyLALLDRLEED 827
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
373-556 5.19e-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: 46.71  E-value: 5.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  373 EVEDIQAKQQELQDNFNLNKANRLKaVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQ 452
Cdd:pfam01576   97 EKKKMQQHIQDLEEQLDEEEAARQK-LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  453 KIIlsdpTWLSLSNE--IVDLENQLKAEAK------------PIDTTELKEAKATLSEAIDELNKKLGKRDtiERSNKVI 518
Cdd:pfam01576  176 KSL----SKLKNKHEamISDLEERLKKEEKgrqelekakrklEGESTDLQEQIAELQAQIAELRAQLAKKE--EELQAAL 249
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2796428067  519 EDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMER 556
Cdd:pfam01576  250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR 287
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
6-143 6.20e-05

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: 45.37  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKdSTNRAdtnfNIKTLGEDGKPilhlVHSVTGV 85
Cdd:cd03242     1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK-SHRTS----RDKELIRWGAE----EAKISAV 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  86 LSINGRDVELQRNYVEKWGSGVNagvlqnhatefyLNGVKLKTKKEYDAEVAAIL--PED 143
Cdd:cd03242    72 LERQGGELALELTIRSGGGRKAR------------LNGIKVRRLSDLLGVLNAVWfaPED 119
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
238-520 7.23e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQnANKSYHDVLDNISKLEYQVKSKD 317
Cdd:TIGR00606  540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELESKE 618
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  318 AEISRKQE-------------EHSRIKANIEALNNDLEVLRGKFYAIDAETLQ-YPEGAFICPTCKRELEVE-DIQAKQQ 382
Cdd:TIGR00606  619 EQLSSYEDklfdvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQlTDENQSCCPVCQRVFQTEaELQEFIS 698
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  383 ELQdNFNLNKANRLKAVQNEGKEKAAKVEEL----KKQCSIIQ---ATITQLSNEKEILVHNINECKGNMpEEQDTQ--- 452
Cdd:TIGR00606  699 DLQ-SKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQSIIDlkeKEIPELRNKLQKVNRDIQRLKNDI-EEQETLlgt 776
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796428067  453 --------KIILSDPTWLS-LSNEIVDLENQLKAEAKPIDTTELKEAKATLSEAIDELNKKLGK-RDTIERSNKVIED 520
Cdd:TIGR00606  777 impeeesaKVCLTDVTIMErFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQD 854
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
1-62 1.14e-04

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: 43.80  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796428067   1 MKEVflkKLILKNF---KKIQdlTVEFTD---KNTF-ICGGNGTGKTTLQDAFLWLLFGKDSTNRADTN 62
Cdd:cd03279     1 MKPL---KLELKNFgpfREEQ--VIDFTGldnNGLFlICGPTGAGKSTILDAITYALYGKTPRYGRQEN 64
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
6-74 1.29e-04

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: 43.07  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796428067   6 LKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKD-STNRADtnfNIKTLGEDGKP 74
Cdd:cd03239     1 IKQITLKNFKSYRDETvVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAaKLRRGS---LLFLAGGGVKA 68
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
201-416 2.05e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 201 AKEIASKKSAIKDELKGIPGRIDSVRDAMPE-SEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEaefkaksELQKQIGn 279
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE-------ERREELG- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 280 kKLAKSQRENEIRQNA------NKSYHDVLDNISKLEyQVKSKDAEI----SRKQEEHSRIKANIEALNNDLEVLRGKfy 349
Cdd:COG3883    90 -ERARALYRSGGSVSYldvllgSESFSDFLDRLSALS-KIADADADLleelKADKAELEAKKAELEAKLAELEALKAE-- 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796428067 350 aidAETLQypegaficptckreLEVEDIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQ 416
Cdd:COG3883   166 ---LEAAK--------------AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-50 2.11e-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: 2.11e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2796428067    5 FLKKLILKN---FKKIQdlTVEFTDKNTFICGGNGTGKTTLQDAFLWLL 50
Cdd:COG4913      2 RLQRLQLINwgtFDGVH--TIDFDGRGTLLTGDNGSGKSTLLDAIQTLL 48
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
6-430 3.99e-04

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


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 43.57  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLI-LKNFKKIQDLTV-EFTDKNTFICGGNGTGKTTLQDAFLwLLFGKDSTNRADTNFNIKTLGEDGKP--------- 74
Cdd:COG4694     2 ITKIKkLKNVGAFKDFGWlAFFKKLNLIYGENGSGKSTLSRILR-SLELGDTSSEVIAEFEIEAGGSAPNPsvrvfnrdf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  75 ---ILHLVHSVTGVLSINGRDVELQrNYVEKwgsgvNAGVLQNHATEFylnGVKLKTKKEYDAEVAAILpEDVFRMITNP 151
Cdd:COG4694    81 veeNLRSGEEIKGIFTLGEENIELE-EEIEE-----LEKEIEDLKKEL---DKLEKELKEAKKALEKLL-EDLAKSIKDD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 152 L--YFPTMKAQDQKAMLLEMAGNVTNEEVANINPKFQEL----------------ISLISGRTLEQLAKEIASKKSAIKD 213
Cdd:COG4694   151 LkkLFASSGRNYRKANLEKKLSALKSSSEDELKEKLKLLkeeepepiapitplpdLKALLSEAETLLEKSAVSSAIEELA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 214 ELKGIPGRIDSVRDAMPESEDWAV------LEKEIADKKEKIKD-IDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQ 286
Cdd:COG4694   231 ALIQNPGNSDWVEQGLAYHKEEEDdtcpfcQQELAAERIEALEAyFDDEYEKLLAALKDLLEELESAINALSALLLEILR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 287 RENEIRQNANKSYHDVLDN-ISKLEYQVKSKDAEISRK-----QEEHSRIKANIEALNNDLEvlrgkfyAIDAETLQYPE 360
Cdd:COG4694   311 TLLPSAKEDLKAALEALNAlLETLLAALEEKIANPSTSidlddQELLDELNDLIAALNALIE-------EHNAKIANLKA 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796428067 361 GAFICPTCKRELEVEDIQAKQQELQDNFN--LNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNE 430
Cdd:COG4694   384 EKEEARKKLEAHELAELKEDLSRYKAEVEelIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEE 455
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
6-70 5.18e-04

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: 41.82  E-value: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067   6 LKKLILKNFKKIQD-LTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRADTNFNIKTLGE 70
Cdd:cd03240     1 IDKLSIRNIRSFHErSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIRE 66
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
6-56 6.97e-04

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: 41.30  E-value: 6.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2796428067   6 LKKLILKNFKKIQDLT-VEFTDKNTFICGGNGTGKTTLQDAFLWLLfGKDST 56
Cdd:cd03278     1 LKKLELKGFKSFADKTtIPFPPGLTAIVGPNGSGKSNIIDAIRWVL-GEQSA 51
PRK11637 PRK11637
AmiB activator; Provisional
242-324 8.72e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.37  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 242 IADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIgnkklaKSQrENEIRQnANKSYHDVLDNISKLEYQVKSKDAEIS 321
Cdd:PRK11637   42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQL------KKQ-EEAISQ-ASRKLRETQNTLNQLNKQIDELNASIA 113

                  ...
gi 2796428067 322 RKQ 324
Cdd:PRK11637  114 KLE 116
46 PHA02562
endonuclease subunit; Provisional
246-510 1.14e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 246 KEKIKDIDSQLADKSKQIeaefkakSELQKQIG-NKKLAKSQRE--NEIRQNANKSYHDVLDNIskleyqvKSKDAEISR 322
Cdd:PHA02562  173 KDKIRELNQQIQTLDMKI-------DHIQQQIKtYNKNIEEQRKknGENIARKQNKYDELVEEA-------KTIKAEIEE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 323 KQEEHSRIKANIEALNNDLEVLRGKFYAIDA--ETLQ-----YPEGAfICPTCKRELEVEDiqAKQQELQDNfNLNKANR 395
Cdd:PHA02562  239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSkiEQFQkvikmYEKGG-VCPTCTQQISEGP--DRITKIKDK-LKELQHS 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 396 LKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKgnmpeeqDTQKIIlsdptwlslsneivdleNQL 475
Cdd:PHA02562  315 LEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK-------KVKAAI-----------------EEL 370
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2796428067 476 KAEaKPIDTTELKEAKATLSEAIDELNKKLGKRDT 510
Cdd:PHA02562  371 QAE-FVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
PRK01156 PRK01156
chromosome segregation protein; Provisional
6-558 1.42e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067   6 LKKLILKNFKKIQDLTVEFTDKNTFICGGNGTGKTTLQDAFLWLLFGKDSTNRadtnfnIKTLGEDGKPIL-------HL 78
Cdd:PRK01156    3 IKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEK------IEDMIKKGKNNLevelefrIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  79 VHSVTGVLSINGRDVELQRN-YVEKWGSGVNAGVLQ----------NHATEFYLNGVKLKtKKEYDAEVAAILPE--DVF 145
Cdd:PRK01156   77 GHVYQIRRSIERRGKGSRREaYIKKDGSIIAEGFDDttkyieknilGISKDVFLNSIFVG-QGEMDSLISGDPAQrkKIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 146 RMITNplyfptMKAQDQKAMLLEMAGNVTNEEVANINPKFQELISLISgrTLEQLAKEIASKKSAIKDELKGIPGRIDSV 225
Cdd:PRK01156  156 DEILE------INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL--ELENIKKQIADDEKSHSITLKEIERLSIEY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 226 RDAMPES-------EDWAVLEKEIADKKEKIKDIDSQLADKSKQIeAEFKAKSELQKQIGNKKLAKSQreNEIRQnanks 298
Cdd:PRK01156  228 NNAMDDYnnlksalNELSSLEDMKNRYESEIKTAESDLSMELEKN-NYYKELEERHMKIINDPVYKNR--NYIND----- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 299 YHDVLDNISKLEYQVKSKDAEISRKQEEHSRIkANIEALNNDLEVLRGKFYAIDAETLQYPEGAFICPTCKRELE----- 373
Cdd:PRK01156  300 YFKYKNDIENKKQILSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIEslkkk 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 374 VEDIQAKQQELQDNFNLNKANRL---KAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINE---------C 441
Cdd:PRK01156  379 IEEYSKNIERMSAFISEILKIQEidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvC 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 442 KGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKA-EAKPIDTTELKE--AKATLSEAIDELNKKLGKRDTIERSNKVI 518
Cdd:PRK01156  459 GTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDiDEKIVDLKKRKEylESEEINKSINEYNKIESARADLEDIKIKI 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 2796428067 519 EDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMERIN 558
Cdd:PRK01156  539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS 578
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
238-552 2.13e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 41.20  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFK-AKSELQKQIGNKKLAKSQR------------ENEIRQNANKSYH-DVL 303
Cdd:pfam13166 101 LKKEIKDHEEKLDAAEANLQKLDKEKEKLEAdFLDECWKKIKRKKNSALSEalngfkyeanfkSRLLREIEKDNFNaGVL 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 304 DNISKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLR---GKFYAIDaETLQYP--------------EGAFICP 366
Cdd:pfam13166 181 LSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQkviGKSSAIE-ELIKNPdladwveqglelhkAHLDTCP 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 367 TCKRELEvediQAKQQELQDNFNlnkaNRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMP 446
Cdd:pfam13166 260 FCGQPLP----AERKAALEAHFD----DEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAE 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 447 EEQDTQKiilsdptwlslSNEIVdLENQLKAEAKPIDTTELKEAKATLSEAIDELNkklgkrDTIERSNKVIEDLEDRRD 526
Cdd:pfam13166 332 VLNSQLD-----------GLRRA-LEAKRKDPFKSIELDSVDAKIESINDLVASIN------ELIAKHNEITDNFEEEKN 393
                         330       340
                  ....*....|....*....|....*.
gi 2796428067 527 KNNEALaEQERLEFLVQDFQKEKDNK 552
Cdd:pfam13166 394 KAKKKL-RLHLVEEFKSEIDEYKDKY 418
PRK09039 PRK09039
peptidoglycan -binding protein;
236-353 2.35e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 236 AVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEiRQNANKSYHDVLDNISKLEYQVKS 315
Cdd:PRK09039   42 FFLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAE-RSRLQALLAELAGAGAAAEGRAGE 120
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2796428067 316 KDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDA 353
Cdd:PRK09039  121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEA 158
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-561 2.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 197 LEQLAKEIASKKSAIKdELKGIPGRIDSVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQ 276
Cdd:PRK03918  261 IRELEERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 277 IG--NKKLAKSQRENEIRQNANKSYHDV---LDNISKLEYQVKSKDAE-ISRKQEEHSRIKANIEALNNDLEVLRGKFYA 350
Cdd:PRK03918  340 LEelKKKLKELEKRLEELEERHELYEEAkakKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKK 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 351 IDAE---TLQYPEGA-FICPTCKRELEVEDiqakQQELQDNFNLnkanRLKAVQNEGKEKAAKVEELKKQCSIIQATITQ 426
Cdd:PRK03918  420 EIKElkkAIEELKKAkGKCPVCGRELTEEH----RKELLEEYTA----ELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 427 LSN--------------EKEILVHNINECKGNMPE-EQDTQKIILSDPTWLSLS---NEIVDLENQLKAEAKPIDTTE-- 486
Cdd:PRK03918  492 ESEliklkelaeqlkelEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEee 571
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 487 LKEAKATLSE----AIDELNKKLG------------------KRDTIERSNKVIEDLEDRRDKNNEALAEQERLEFLVQD 544
Cdd:PRK03918  572 LAELLKELEElgfeSVEELEERLKelepfyneylelkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
                         410
                  ....*....|....*..
gi 2796428067 545 FQKEKDNKLMERINGMF 561
Cdd:PRK03918  652 LEKKYSEEEYEELREEY 668
PRK12704 PRK12704
phosphodiesterase; Provisional
237-409 2.73e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 237 VLEKEIADKKEKIKDI--DSQLADKSKQIEAEFKAKSELQKQignkklaKSQRENEIRQNANKsyhdvldnISKLEYQVK 314
Cdd:PRK12704   28 IAEAKIKEAEEEAKRIleEAKKEAEAIKKEALLEAKEEIHKL-------RNEFEKELRERRNE--------LQKLEKRLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 315 SKDAEISRKQEEHSRIKANIEALNNDLEVLRgkfyaidaETLQypegaficptcKRELEVEDIQAKQ-QELQDNFNLN-- 391
Cdd:PRK12704   93 QKEENLDRKLELLEKREEELEKKEKELEQKQ--------QELE-----------KKEEELEELIEEQlQELERISGLTae 153
                         170       180
                  ....*....|....*....|
gi 2796428067 392 --KANRLKAVQNEGKEKAAK 409
Cdd:PRK12704  154 eaKEILLEKVEEEARHEAAV 173
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
279-538 2.99e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 279 NKKLAKSQRENEIRQNANKSYHDVLDnisKLEYQVKSKDAEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIdaETLqy 358
Cdd:PRK02224  184 DQRGSLDQLKAQIEEKEEKDLHERLN---GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL--ETL-- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 359 pegaficptckrELEVEDIQAKQQELQ---DNFnlnkANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILV 435
Cdd:PRK02224  257 ------------EAEIEDLRETIAETErerEEL----AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 436 HNINECKGNMPEEQDTQKIILSDPTwlSLSNEIVDLENQ---LKAEAKPIDtTELKEAKATLS---EAIDELNKKLgkRD 509
Cdd:PRK02224  321 DRDEELRDRLEECRVAAQAHNEEAE--SLREDADDLEERaeeLREEAAELE-SELEEAREAVEdrrEEIEELEEEI--EE 395
                         250       260
                  ....*....|....*....|....*....
gi 2796428067 510 TIERSNKVIEDLEDRRDKNNEALAEQERL 538
Cdd:PRK02224  396 LRERFGDAPVDLGNAEDFLEELREERDEL 424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-347 3.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  195 RTLEQLAKEIASKKSAIKDELKGIPGRIDS---VRDAMPESEDWAVLEKEIADKKEKIKDIDS------QLADKSKQIEA 265
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREAlqrLAEYSWDEIDVASAEREIAELEAELERLDAssddlaALEEQLEELEA 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  266 EFKaksELQKQIGNKKLAKSQRENEIRQNAN--KSYHDVLDNISKLEYQVKSKDAEISRKQEEHSRIKANI-EALNNDLE 342
Cdd:COG4913    700 ELE---ELEEELDELKGEIGRLEKELEQAEEelDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELrENLEERID 776

                   ....*
gi 2796428067  343 VLRGK 347
Cdd:COG4913    777 ALRAR 781
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
236-544 6.28e-03

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: 39.82  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  236 AVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIRQNANKSYHDVLDNISKLEYQVKS 315
Cdd:pfam12128  607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  316 KDAEisRKQEEHsRIKANIEALNNDLEVLRGKfyaiDAETLQYPEGAFicpTCKRELEVEDIQAKQQelqdnfnlNKANR 395
Cdd:pfam12128  687 LEAQ--LKQLDK-KHQAWLEEQKEQKREARTE----KQAYWQVVEGAL---DAQLALLKAAIAARRS--------GAKAE 748
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  396 LKAVQNEGKekaakvEELKKQcSIIQATITQLSNEKEILVHNINECKGNMPEeqdtqkiILSDPTWLslsNEIVDLENQl 475
Cdd:pfam12128  749 LKALETWYK------RDLASL-GVDPDVIAKLKREIRTLERKIERIAVRRQE-------VLRYFDWY---QETWLQRRP- 810
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796428067  476 kaeakpidttELKEAKATLSEAIDELNKKLGK--------RDTIERSNKVIEDLEDRRDKNNEAL-AEQERLEFLVQD 544
Cdd:pfam12128  811 ----------RLATQLSNIERAISELQQQLARliadtklrRAKLEMERKASEKQQVRLSENLRGLrCEMSKLATLKED 878
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
238-533 8.62e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIrQNANKSYHDVLDNISKLEYQVKSKD 317
Cdd:COG4372    64 LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQ 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQypegaficpTCKRELEVEDIQAKQQELQDNFNLNKANRLK 397
Cdd:COG4372   143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE---------QALDELLKEANRNAEKEEELAEAEKLIESLP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 398 AVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPEEQDTQKIILSDPTWLSLSNEIVDLENQLKA 477
Cdd:COG4372   214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2796428067 478 EAKPIDTTELKEAKATLSEAIDELNKKLGKRDTIERSNKVIEDLEDRRDKNNEALA 533
Cdd:COG4372   294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
PTZ00121 PTZ00121
MAEBL; Provisional
205-557 9.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  205 ASKKSAIKDELKGIPGR--IDSVRDAMPESEDWAVLEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKL 282
Cdd:PTZ00121  1361 AAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  283 AKSQRENEIRQNANKSYHdvLDNISKlEYQVKSKDAEISRKQEEHSR---IKANIEALNNDLEVLRGKFYA-IDAETLQY 358
Cdd:PTZ00121  1441 EEAKKADEAKKKAEEAKK--AEEAKK-KAEEAKKADEAKKKAEEAKKadeAKKKAEEAKKKADEAKKAAEAkKKADEAKK 1517
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  359 PEGAFICPTCKRELEVE--DIQAKQQELQDNFNLNKANRLKAVQNEGKEKAAKVEELKKQCSIIQATITQLSNEKEI-LV 435
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeEV 1597
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067  436 HNINECKGNMPEEQDTQKiilsdptwlslSNEIVDLENQLKAEAKPIDTTELKEAKATLSEAIDELnKKLGKRDTIERSN 515
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKA-----------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAE 1665
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2796428067  516 KVIEDLEDRRDKNNEALAEQERLEFLVQDFQKEKDNKLMERI 557
Cdd:PTZ00121  1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
238-555 9.59e-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: 39.23  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 238 LEKEIADKKEKIKDIDSQLADKSKQIEAEFKAKSELQKQIGNKKLAKSQRENEIrQNANKSYHDVLDNISKLEYQVKSKD 317
Cdd:TIGR04523  73 SNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVEL-NKLEKQKKENKKNIDKFLTEIKKKE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 318 AEISRKQEEHSRIKANIEALNNDLEVLRGKFYAIDAETLQYPEGAFicptcKRELEVEDIQAKQQElqDNFNLNKANRLK 397
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-----KLELLLSNLKKKIQK--NKSLESQISELK 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 398 AVQNE-GKEKAAKVEELKKQCSIIQATITQLSNEKEILVHNINECKGNMPE-EQDTQKIILSDPTWLSLSNEIVDLENQL 475
Cdd:TIGR04523 225 KQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKElEQNNKKIKELEKQLNQLKSEISDLNNQK 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796428067 476 KAEAkpidTTELKEAKATLSEAIDELNKKLGKRD-TIERSNKVIEDLE-DRRDKNNEALAEQERLE---FLVQDFQKEKD 550
Cdd:TIGR04523 305 EQDW----NKELKSELKNQEKKLEEIQNQISQNNkIISQLNEQISQLKkELTNSESENSEKQRELEekqNEIEKLKKENQ 380

                  ....*
gi 2796428067 551 NKLME 555
Cdd:TIGR04523 381 SYKQE 385
 
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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