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Conserved domains on  [gi|46852390|ref|NP_005427|]
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coiled-coil domain-containing protein 6 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein 6( domain architecture ID 12101877)

coiled-coil domain containing protein 6 may be a DUF2046 domain-containing cytoskeletal protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 52-337 9.67e-149

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


:

Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 426.17  E-value: 9.67e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    52 SPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 131
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   132 VNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 211
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   212 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYL 291
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 46852390   292 EEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYF 337
Cdd:pfam09755 259 QEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
 
Name Accession Description Interval E-value
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 52-337 9.67e-149

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 426.17  E-value: 9.67e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    52 SPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 131
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   132 VNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 211
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   212 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYL 291
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 46852390   292 EEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYF 337
Cdd:pfam09755 259 QEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-333 8.46e-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: 67.79  E-value: 8.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKEtlavNY 134
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIE----NV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEEEFLTNELSR---KLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKK-----------LENDTISKQLTLEQLRREKI 200
Cdd:TIGR02169  757 KSELKELEARIEEleeDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEevsriearlreIEQKLNRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    201 DLENTLEqEQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHirfLKNEVERLKKQLRAAQ 280
Cdd:TIGR02169  837 ELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEELEE----------LEAALRDLESRLGD---LKKERDELEAQLRELE 902

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 46852390    281 LQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDD 333
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-335 2.33e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEefisntlfKKIQALQKEKEtlavny 134
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE--------QDIARLEERRR------ 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 ekeeefltnELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALV 214
Cdd:COG1196 313 ---------ELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 215 NRlwkRMDKLEAEKRILQEKLDQpvsappsprdismeidspENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEE 294
Cdd:COG1196 383 EL---AEELLEALRAAAELAAQL------------------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46852390 295 RHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDER 335
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
56-330 2.05e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   56 LEELTNRLASLQQENKVLK---IELETYKLKC----KALQEENR---------DLRKASVTIQARAEQEEEFISNtlFKK 119
Cdd:PRK03918 407 ISKITARIGELKKEIKELKkaiEELKKAKGKCpvcgRELTEEHRkelleeytaELKRIEKELKEIEEKERKLRKE--LRE 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  120 IQALQKEKETLAVNYEKEEEFltNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQL---TLEQLR 196
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQL--KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELE 562

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  197 REKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQL 276
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46852390  277 RAAQLQHSEKMAQYLEEE-RHMREENLRLQRKLQREMERREALCRQLSESESSLE 330
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 85-254 2.97e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  85 KALQEENRDLRKASVTIQARAEQeeefISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSrklMQLQHEKAELEQHLE 164
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAK----VVDKLTDFENQTEKDQTALETLEKALKDLLTDEGG---AIARKEIKDLQKELE 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 165 QEQEFQVNKLMKKIKKLENDTISKQLTLEQ-------LRREKIDLENTLEQEQEAL--VNRLWKRMDKLEAEKRILQEKL 235
Cdd:cd22656 190 KLNEEYAAKLKAKIDELKALIADDEAKLAAalrliadLTAADTDLDNLLALIGPAIpaLEKLQGAWQAIATDLDSLKDLL 269

                       170
                ....*....|....*....
gi 46852390 236 DQPVSAPPSPRDISMEIDS 254
Cdd:cd22656 270 EDDISKIPAAILAKLELEK 288
 
Name Accession Description Interval E-value
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 52-337 9.67e-149

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 426.17  E-value: 9.67e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    52 SPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 131
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   132 VNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 211
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   212 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYL 291
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 46852390   292 EEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYF 337
Cdd:pfam09755 259 QEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-333 8.46e-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: 67.79  E-value: 8.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKEtlavNY 134
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIE----NV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEEEFLTNELSR---KLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKK-----------LENDTISKQLTLEQLRREKI 200
Cdd:TIGR02169  757 KSELKELEARIEEleeDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEevsriearlreIEQKLNRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    201 DLENTLEqEQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHirfLKNEVERLKKQLRAAQ 280
Cdd:TIGR02169  837 ELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEELEE----------LEAALRDLESRLGD---LKKERDELEAQLRELE 902

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 46852390    281 LQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDD 333
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-326 2.33e-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: 66.23  E-value: 2.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKETLAVNY 134
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEEEFLTnELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALV 214
Cdd:TIGR02168  757 TELEAEIE-ELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    215 nRLWKRMDKLEAEKRILQEKLDQPVSAppsprdISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMaqylEEE 294
Cdd:TIGR02168  835 -ATERRLEDLEEQIEELSEDIESLAAE------IEELEELIEELESELEALLNERASLEEALALLRSELEELS----EEL 903

                          250       260       270
                   ....*....|....*....|....*....|..
gi 46852390    295 RHMREENLRLQRKLQREMERREALCRQLSESE 326
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-335 2.33e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEefisntlfKKIQALQKEKEtlavny 134
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE--------QDIARLEERRR------ 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 ekeeefltnELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALV 214
Cdd:COG1196 313 ---------ELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 215 NRlwkRMDKLEAEKRILQEKLDQpvsappsprdismeidspENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEE 294
Cdd:COG1196 383 EL---AEELLEALRAAAELAAQL------------------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46852390 295 RHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDER 335
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-318 1.41e-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: 57.37  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQAR-AEQEEEFIS-----NTLFKKIQALQKEKE 128
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEiEELQKELYAlaneiSRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    129 TLAVNYEKEEEFLTNELSRK------LMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDL 202
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLdelaeeLAELEEKLEELKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    203 ENTLE------QEQEALVNRLWKRMDKLEAEKRILQEKLDqpvsaPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQL 276
Cdd:TIGR02168  392 ELQIAslnneiERLEARLERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEEL 466

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 46852390    277 RAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREAL 318
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
56-330 2.05e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   56 LEELTNRLASLQQENKVLK---IELETYKLKC----KALQEENR---------DLRKASVTIQARAEQEEEFISNtlFKK 119
Cdd:PRK03918 407 ISKITARIGELKKEIKELKkaiEELKKAKGKCpvcgRELTEEHRkelleeytaELKRIEKELKEIEEKERKLRKE--LRE 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  120 IQALQKEKETLAVNYEKEEEFltNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQL---TLEQLR 196
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQL--KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELE 562

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  197 REKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQL 276
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46852390  277 RAAQLQHSEKMAQYLEEE-RHMREENLRLQRKLQREMERREALCRQLSESESSLE 330
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-318 8.48e-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: 55.07  E-value: 8.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNY 134
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEeeflTNELSRKLMQLQHEKAELEQHL----EQEQEF--QVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLE- 207
Cdd:TIGR02169  818 EQK----LNRLTLEKEYLEKEIQELQEQRidlkEQIKSIekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDe 893

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    208 ------------QEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSpenmmrhIRFLKNEVERLKKQ 275
Cdd:TIGR02169  894 leaqlrelerkiEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-------LEDVQAELQRVEEE 966

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 46852390    276 LRAAQLQHSEKMAQYLEEERHMREenlrLQRKLQREMERREAL 318
Cdd:TIGR02169  967 IRALEPVNMLAIQEYEEVLKRLDE----LKEKRAKLEEERKAI 1005
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 118-330 2.49e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 2.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 118 KKIQALQKEKETLAVNYEkeeefltnELSRKLMQLQHEKAELEQHLEQeQEFQVNKLMKKIKKLENDTISKQLTLEQLRR 197
Cdd:COG4942  20 DAAAEAEAELEQLQQEIA--------ELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 198 EKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILqekldqpvsappSPRDISMEIDSPENMMRHIRFLKNEVERLKKQ 275
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRAlyRLGRQPPLALLL------------SPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46852390 276 LRAAQLQHSEKMAQYLEEERhMREENLRLQRKLQREMERREALCRQLSESESSLE 330
Cdd:COG4942 159 LAELAALRAELEAERAELEA-LLAELEEERAALEALKAERQKLLARLEKELAELA 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 56-326 2.87e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     56 LEELTNRLASLQQENKVLKieletyklKCKALQEENRDLRKASVTIQARAEQEEEfisNTLFKKIQALQKEKETLAVNYE 135
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAE--------RYKELKAELRELELALLVLRLEELREEL---EELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    136 KEEEfltnelsrKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALvN 215
Cdd:TIGR02168  264 ELEE--------KLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-D 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    216 RLWKRMDKLEAEKRILQEKLDqpvsappsprDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEER 295
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELE----------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403

                          250       260       270
                   ....*....|....*....|....*....|.
gi 46852390    296 HMREENLRLQRKLQREMERREALCRQLSESE 326
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAE 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-236 1.52e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEfisntLFKKIQALQKEKETLAVNY 134
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-----ELAEAEEELEELAEELLEA 391

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 EKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEfqvnkLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALV 214
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                       170       180
                ....*....|....*....|..
gi 46852390 215 NRLWKRMDKLEAEKRILQEKLD 236
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAE 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-335 2.19e-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: 50.45  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETyKLKCKALQEEnrdLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLavny 134
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRREREK-AERYQALLKE---KREYEGYELLKEKEALERQKEAIERQLASLEEELEKL---- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 ekeeEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLeQEQEALV 214
Cdd:TIGR02169  257 ----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-AKLEAEI 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    215 NRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEE 294
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDK----------LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 46852390    295 RHMREENLRLQRKLQREMERREALCRQLSESESSL-EMDDER 335
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKInELEEEK 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-238 3.75e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQK--EKETLAV 132
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaELAAQLE 403

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 133 NYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQvnklmKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEA 212
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                       170       180
                ....*....|....*....|....*.
gi 46852390 213 LVNRLWKRMDKLEAEKRILQEKLDQP 238
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-335 9.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 9.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 118 KKIQALQKEKETlAVNY----EKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENdtiskqlTLE 193
Cdd:COG1196 200 RQLEPLERQAEK-AERYrelkEELKELEAELLLLKLRELEAELEELEAELEELEA-ELEELEAELAELEA-------ELE 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 194 QLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLdqpvsappspRDISMEIDSPENMMRHIRF--------- 264
Cdd:COG1196 271 ELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERR----------RELEERLEELEEELAELEEeleeleeel 339

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852390 265 --LKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDER 335
Cdd:COG1196 340 eeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-275 1.54e-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: 47.74  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNT------LFKKIQALQKEKE 128
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    129 TLAVNY---EKEEEFLTNELSR---KLMQLQHEKAELEQHLEQEQEFQVNKLMKKIkklendtiskQLTLEQLRREKIDL 202
Cdd:TIGR02168  383 TLRSKVaqlELQIASLNNEIERleaRLERLEDRRERLQQEIEELLKKLEEAELKEL----------QAELEELEEELEEL 452

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852390    203 ENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHIRFLKNEVERLKKQ 275
Cdd:TIGR02168  453 QEELERLEEAL-EELREELEEAEQALDAAERELAQ----------LQARLDSLERLQENLEGFSEGVKALLKN 514
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
155-303 3.20e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 155 EKAELEQHLEQEQEFQVNKLMKKIKKLENdtiskqlTLEQLRREKIDLENTLEqeqealvnrlwkrmdklEAEKRI--LQ 232
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELE-----------------EKDERIerLE 447

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852390 233 EKLdqpvsappspRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQlQHSEKMAQYLEEERHMREENLR 303
Cdd:COG2433 448 REL----------SEARSEERREIRKDREISRLDREIERLERELEEER-ERIEELKRKLERLKELWKLEHS 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-237 3.95e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNY 134
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 EKEEEflTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENT--------- 205
Cdd:COG1196 376 EAEEE--LEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEAleeaaeeea 452

                       170       180       190
                ....*....|....*....|....*....|...
gi 46852390 206 -LEQEQEALVNRLWKRMDKLEAEKRILQEKLDQ 237
Cdd:COG1196 453 eLEEEEEALLELLAELLEEAALLEAALAELLEE 485
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
55-330 3.95e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKA-------------LQEENRDLRKASVTIQARAEQEEEfiSNTLFKKIQ 121
Cdd:COG4717  96 ELEELEEELEELEAELEELREELEKLEKLLQLlplyqelealeaeLAELPERLEELEERLEELRELEEE--LEELEAELA 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 122 ALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLtLEQLRREKID 201
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEQLENELEAAAL-EERLKEARLL 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 202 L------------------------------------ENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSP 245
Cdd:COG4717 252 LliaaallallglggsllsliltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 246 RDISM-EIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEK--MAQYLEEERHMREENLRLQRKLQREMERREALCRQL 322
Cdd:COG4717 332 PDLSPeELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL 411


                ....*...
gi 46852390 323 SESESSLE 330
Cdd:COG4717 412 EELLGELE 419
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 55-317 4.00e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 4.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFIsNTLFKKIQALQKEKETLavny 134
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAEL---- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 EKEEEFLTNELSRKL--MQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLeNDTISKQLtlEQLRREKIDLEnTLEQEQEA 212
Cdd:COG4942  96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQA--EELRADLAELA-ALRAELEA 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 213 LVNRLWKRMDKLEAEKRILQEkldqpvsappsprdismeidspenmmrhirfLKNEVERLKKQLRAAQLQHSEKMAQYLE 292
Cdd:COG4942 172 ERAELEALLAELEEERAALEA-------------------------------LKAERQKLLARLEKELAELAAELAELQQ 220

                       250       260
                ....*....|....*....|....*
gi 46852390 293 EERHMREENLRLQRKLQREMERREA 317
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPA 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
62-326 4.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   62 RLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFI-SNTLFKKIQALQKEKETLavnyekeeef 140
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERL---------- 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  141 ltNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKR 220
Cdd:COG4913  681 --DASSDDLAALEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  221 MDKLEAEKRILqekldqpvsappsprdismeidspENMMRHIRFLKNEVERLKKQLRAAQLQHSEK-------------- 286
Cdd:COG4913  758 ALGDAVERELR------------------------ENLEERIDALRARLNRAEEELERAMRAFNREwpaetadldadles 813

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 46852390  287 MAQYLEEERHMREENL-----RLQRKLQREMER-REALCRQLSESE 326
Cdd:COG4913  814 LPEYLALLDRLEEDGLpeyeeRFKELLNENSIEfVADLLSKLRRAI 859
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-329 1.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  151 QLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDtiskqltLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRI 230
Cdd:COG4913  285 FAQRRLELLEAELEELRA-ELARLEAELERLEAR-------LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  231 LQEKLDQ--------PVSAPPSPRDIsmeidspENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREE-- 300
Cdd:COG4913  357 RERRRARleallaalGLPLPASAEEF-------AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEia 429

                        170       180       190
                 ....*....|....*....|....*....|.
gi 46852390  301 NLRLQRKL--QREMERREALCRQLSESESSL 329
Cdd:COG4913  430 SLERRKSNipARLLALRDALAEALGLDEAEL 460
PRK12704 PRK12704
phosphodiesterase; Provisional
 94-233 1.22e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   94 LRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAvnyeKEEEF-LTNELSRKLMQLQHEKAELEQHLEQEQEfQVN 172
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA----KEEIHkLRNEFEKELRERRNELQKLEKRLLQKEE-NLD 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852390  173 KLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILQE 233
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEEAKEILLEK 162
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 55-257 1.57e-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: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEfisntlfkKIQALQKE-KETLAVN 133
Cdd:COG3883  24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------EIEERREElGERARAL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 134 YEKE---------------EEFLTN-ELSRKLM--------QLQHEKAELEQhLEQEQEFQVNKLMKKIKKLEndtiSKQ 189
Cdd:COG3883  96 YRSGgsvsyldvllgsesfSDFLDRlSALSKIAdadadlleELKADKAELEA-KKAELEAKLAELEALKAELE----AAK 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852390 190 LTLEQLRREKIDLENTLEQEQEALVNRLwkrmDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPEN 257
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQL----AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 55-329 1.70e-04

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: 44.19  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELEtyklkckaLQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNY 134
Cdd:pfam02463  238 RIDLLQELLRDEQEEIESSKQEIE--------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEEEFLTNELSRKlmqlqhEKAELEQHLEQEQ--EFQVNKLMKKIKKLENDTI-----SKQLTLEQLRREKIDLENTLE 207
Cdd:pfam02463  310 VDDEEKLKESEKEK------KKAEKELKKEKEEieELEKELKELEIKREAEEEEeeeleKLQEKLEQLEEELLAKKKLES 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    208 QEQEALVNRLWKRMDKLEAEKRILQEKL--------DQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAA 279
Cdd:pfam02463  384 ERLSSAAKLKEEELELKSEEEKEAQLLLelarqledLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 46852390    280 QLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSL 329
Cdd:pfam02463  464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 96-238 2.09e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   96 KASVTIQARAEQEEEFISNTLFKKIQALQKEKEtlAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEqefqVNKLM 175
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEE--AEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE----AQQAI 579

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852390  176 KKIKKlENDTISKQLtleQLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDQP 238
Cdd:PRK00409 580 KEAKK-EADEIIKEL---RQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKEKQEEL 637
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 55-314 2.20e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRkasvtiqARAEQEEEFISNTLfKKIQALQKEKETLAVNY 134
Cdd:pfam10174 311 KLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALR-------LRLEEKESFLNKKT-KQLQDLTEEKSTLAGEI 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   135 EKEEEFLTNElSRKLMQLQHEKAELEQHLeQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLE--QEQEA 212
Cdd:pfam10174 383 RDLKDMLDVK-ERKINVLQKKIENLQEQL-RDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIErlKEQRE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   213 LVNRlwKRMDKLEAEKRILQ-----------EKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQL 281
Cdd:pfam10174 461 REDR--ERLEELESLKKENKdlkekvsalqpELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538

                         250       260       270
                  ....*....|....*....|....*....|...
gi 46852390   282 QHseKMAQYLEEERHMREENLRLQRKLQREMER 314
Cdd:pfam10174 539 QL--KKAHNAEEAVRTNPEINDRIRLLEQEVAR 569
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 74-336 2.35e-04

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: 43.81  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     74 KIELETYKLKCKALQEENRDLRKASVtIQARAEQEEEFISNTLFKKiqalqkEKETLAVNYEKEEEFLTNELSRKLMQLQ 153
Cdd:pfam02463  178 LIEETENLAELIIDLEELKLQELKLK-EQAKKALEYYQLKEKLELE------EEYLLYLDYLKLNEERIDLLQELLRDEQ 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    154 HEKAELEQHLEQEQEF--QVNKLMKKIKKLENDTISKQLTL----EQLRREKIDLE---NTLEQEQEALVNRLWKRMDKL 224
Cdd:pfam02463  251 EEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEEELKLLakeeEELKSELLKLErrkVDDEEKLKESEKEKKKAEKEL 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    225 EAEKRILQEKLDQPVSAppSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQL------QHSEKMAQYLEEERHMR 298
Cdd:pfam02463  331 KKEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlssaakLKEEELELKSEEEKEAQ 408

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 46852390    299 EENLRLQRKLQREMERREALCRQLSESESSLEMDDERY 336
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL 446
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-331 2.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 115 TLFKKIQALQKEKetlaVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDtiskqltLEQ 194
Cdd:COG4717  38 TLLAFIRAMLLER----LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-------LEE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 195 LRREKIDLENTLEQ-EQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHIRFLKNEVERLK 273
Cdd:COG4717 107 LEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEE----------LEERLEELRELEEELEELEAELAELQ 176

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46852390 274 KQLRAAQLQHSEKMAQYLE------EERHMREENLRLQRK-LQREMERREALCRQLSESESSLEM 331
Cdd:COG4717 177 EELEELLEQLSLATEEELQdlaeelEELQQRLAELEEELEeAQEELEELEEELEQLENELEAAAL 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 144-324 2.90e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 2.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 144 ELSRKLMQLQHEKAELEQHLEqeqefqvnKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEqEALVNRLWKRMDK 223
Cdd:COG1579  14 ELDSELDRLEHRLKELPAELA--------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 224 LEAEKRIlqekldqpvsappspRDISMEIDSPENMMR----HIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMRE 299
Cdd:COG1579  85 VRNNKEY---------------EALQKEIESLKRRISdledEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149

                       170       180
                ....*....|....*....|....*
gi 46852390 300 ENLRLQRKLQREMERREALCRQLSE 324
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPP 174
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-235 3.97e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  61 NRLASLQQENKVLKIELETYKLKCKALQEENR---DLRKASVTIQARAEQEEEFISN-TLFKKIQALQKEKETLAVNYEK 136
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEELEEeleELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEE 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 137 EEEFLT--NELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALv 214
Cdd:COG4717 151 LEERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL- 229

                       170       180
                ....*....|....*....|.
gi 46852390 215 NRLWKRMDKLEAEKRILQEKL 235
Cdd:COG4717 230 EQLENELEAAALEERLKEARL 250
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 53-209 4.10e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 4.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  53 PFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKAsvtiQARAEQEEEFISNTlfKKIQALQKEKETLav 132
Cdd:COG1579  30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVRNN--KEYEALQKEIESL-- 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852390 133 nyEKEEEFLTNELSRKLMQLQHEKAELEQhLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQE 209
Cdd:COG1579 102 --KRRISDLEDEILELMERIEELEEELAE-LEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 114-321 4.82e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    114 NTLFKKIQALQKEKETLAVNYEKEEEFLTNE------LSRKLMQLQHEKAELEQHLEQEQEFQVN----------KLMKK 177
Cdd:pfam01576  450 NEAEGKNIKLSKDVSSLESQLQDTQELLQEEtrqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNverqlstlqaQLSDM 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    178 IKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALvnrlwKRMDKLEAEKRILQEKLDqpvsappsprDISMEIDspen 257
Cdd:pfam01576  530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA-----AAYDKLEKTKNRLQQELD----------DLLVDLD---- 590

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852390    258 mmrHIRFLKNEVErlKKQLRAAQLQHSEKM--AQYLEE----ERHMREENLR---LQRKLQREMERREALCRQ 321
Cdd:pfam01576  591 ---HQRQLVSNLE--KKQKKFDQMLAEEKAisARYAEErdraEAEAREKETRalsLARALEEALEAKEELERT 658
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 143-343 4.84e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 4.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 143 NELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRL----- 217
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQA-ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 218 -WKRMDKLEA--EKRILQEKLDQpVSAppsprdISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQlqhsekmaqylEEE 294
Cdd:COG3883  98 sGGSVSYLDVllGSESFSDFLDR-LSA------LSKIADADADLLEELKADKAELEAKKAELEAKL-----------AEL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 46852390 295 RHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQ 343
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 55-310 7.48e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.04  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEfisntlfkKIQALQKEKETLAVNY 134
Cdd:pfam05557  98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQ--------LRQNLEKQQSSLAEAE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   135 EKeeeflTNELSRKLMQLQHEKAELEQhlEQEQEFQVNKLMKKIKKLENDTI---SKQLTLEQLRREKIDLENTLEQEQE 211
Cdd:pfam05557 170 QR-----IKELEFEIQSQEQDSEIVKN--SKSELARIPELEKELERLREHNKhlnENIENKLLLKEEVEDLKRKLEREEK 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   212 ALvnrlwKRMDKLEAEKRILQEKLDQPVSAPpspRDISMEIDSPENMMRHIRFLKNEVERLK----------KQLRAAQL 281
Cdd:pfam05557 243 YR-----EEAATLELEKEKLEQELQSWVKLA---QDTGLNLRSPEDLSRRIEQLQQREIVLKeenssltssaRQLEKARR 314

                         250       260       270
                  ....*....|....*....|....*....|..
gi 46852390   282 QHSEKMAQYL---EEERHMREENLRLQRKLQR 310
Cdd:pfam05557 315 ELEQELAQYLkkiEDLNKKLKRHKALVRRLQR 346
PRK12704 PRK12704
phosphodiesterase; Provisional
 118-237 7.96e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 7.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  118 KKIQALQKEKETLAVNYEKEEEFLTNElsrKLMQLQHEkaelEQHLEQEQEFQVNKLMKKIKKLENDTISKQltlEQLRR 197
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAIKKE---ALLEAKEE----IHKLRNEFEKELRERRNELQKLEKRLLQKE---ENLDR 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 46852390  198 EKIDLENtLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQ 237
Cdd:PRK12704 101 KLELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEE 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 55-237 9.33e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 9.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390     55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEefisntlfKKIQALQKEKETLAVNY 134
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE--------AQLRELERKIEELEAQI 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    135 EKEEEFLtNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLmkKIKKLendtiskQLTLEQLRREKIDLE---NTLEQEQE 211
Cdd:TIGR02169  913 EKKRKRL-SELKAKLEALEEELSEIEDPKGEDEEIPEEEL--SLEDV-------QAELQRVEEEIRALEpvnMLAIQEYE 982

                          170       180
                   ....*....|....*....|....*....
gi 46852390    212 ALVNR---LWKRMDKLEAEKRILQEKLDQ 237
Cdd:TIGR02169  983 EVLKRldeLKEKRAKLEEERKAILERIEE 1011
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-335 1.09e-03

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: 41.58  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    163 LEQEQEfqVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQ------EQEALVNRLWKRMDKLEAEKRILQEKLD 236
Cdd:TIGR02168  673 LERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkeleELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    237 QPVSAPPSPRDISMEIDSPENmmrHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERRE 316
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*....
gi 46852390    317 ALCRQLSESESSLEMDDER 335
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQ 846
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
196-332 1.26e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 196 RREKIDLENTLEQEQEaLVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdismeidspenmmrhirfLKNEVERLKKQ 275
Cdd:COG2433 398 EREKEHEERELTEEEE-EIRRLEEQVERLEAEVEELEAELEE---------------------------KDERIERLERE 449

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46852390 276 LRAAQLQHSEKmAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMD 332
Cdd:COG2433 450 LSEARSEERRE-IRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
55-335 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   55 RLEELTNRLASLQQENKVLKIELETYKlKCKALQEENRDLRKasvtiqaraeQEEEFISNTLFKKIQALQKEKETLavny 134
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKK----------RLTGLTPEKLEKELEELEKAKEEI---- 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  135 EKEEEfltnELSRKLMQLQHEKAELEQHL------------------EQEQEFQVNKLMKKIKKLENDTISKQLTLEQLR 196
Cdd:PRK03918 404 EEEIS----KITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLR 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  197 REKIDLENTLEQEQEALVNRlwkrmdKLEAEKRILQEKLDqpvsappsprdiSMEIDSPENMMRHIRFLKNEVERLKKQL 276
Cdd:PRK03918 480 KELRELEKVLKKESELIKLK------ELAEQLKELEEKLK------------KYNLEELEKKAEEYEKLKEKLIKLKGEI 541

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  277 RAaqlqhsekMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSE-SESSLEMDDER 335
Cdd:PRK03918 542 KS--------LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEER 593
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 55-233 1.62e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEE-----------NRDLRKASVTIQARAEQEEEFISNTLFKKIQAL 123
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEleqnnkkikelEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQ 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   124 QKEKETLAVNYEKEEEfLTNELSRKLMQLQHEKAELEQHlEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLE 203
Cdd:TIGR04523 320 EKKLEEIQNQISQNNK-IISQLNEQISQLKKELTNSESE-NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397

                         170       180       190
                  ....*....|....*....|....*....|
gi 46852390   204 NTLeQEQEALVNRLWKRMDKLEAEKRILQE 233
Cdd:TIGR04523 398 SKI-QNQEKLNQQKDEQIKKLQQEKELLEK 426
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 55-239 1.67e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELEtyklkckALQEENRDLRKASVTIQARAEQEEEFIsntlfKKIQALQKEKETLAVNY 134
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELA-------ELEDELAALEARLEAAKTELEDLEKEI-----KRLELEIEEVEARIKKY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 EKEEEFLTNelSRKLMQLQHEKAELEQHLEqEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALV 214
Cdd:COG1579  79 EEQLGNVRN--NKEYEALQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155

                       170       180
                ....*....|....*....|....*
gi 46852390 215 nrlwKRMDKLEAEKRILQEKLDQPV 239
Cdd:COG1579 156 ----AELEELEAEREELAAKIPPEL 176
PRK14644 PRK14644
hypothetical protein; Provisional
 118-207 1.82e-03

hypothetical protein; Provisional


Pssm-ID: 184779 [Multi-domain]  Cd Length: 136  Bit Score: 38.66  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  118 KKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQ---LTLE- 193
Cdd:PRK14644  39 KDIEELTKEISDFIDNLSVEFDFDSLDISSPGFDMDYETDELENHIGEIIDVSLNKEVNKTDFITGELLENNpetITLKw 118

                         90
                 ....*....|....*...
gi 46852390  194 ----QLRREKIDLENTLE 207
Cdd:PRK14644 119 nckgQFRKVEINKENIKK 136
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 85-254 2.97e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  85 KALQEENRDLRKASVTIQARAEQeeefISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSrklMQLQHEKAELEQHLE 164
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAK----VVDKLTDFENQTEKDQTALETLEKALKDLLTDEGG---AIARKEIKDLQKELE 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 165 QEQEFQVNKLMKKIKKLENDTISKQLTLEQ-------LRREKIDLENTLEQEQEAL--VNRLWKRMDKLEAEKRILQEKL 235
Cdd:cd22656 190 KLNEEYAAKLKAKIDELKALIADDEAKLAAalrliadLTAADTDLDNLLALIGPAIpaLEKLQGAWQAIATDLDSLKDLL 269

                       170
                ....*....|....*....
gi 46852390 236 DQPVSAPPSPRDISMEIDS 254
Cdd:cd22656 270 EDDISKIPAAILAKLELEK 288
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
55-330 4.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   55 RLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFI-SNTLFKKIQALQKEKETLAVN 133
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKeKAEEYIKLSEFYEEYLDELRE 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  134 YEKEEEFLTNELS---RKLMQLQHEKAELEQHLEQEQEFQ--VNKLMKKIKKLEnDTISKQLTLEQLRREKIDLEntlEQ 208
Cdd:PRK03918 312 IEKRLSRLEEEINgieERIKELEEKEERLEELKKKLKELEkrLEELEERHELYE-EAKAKKEELERLKKRLTGLT---PE 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  209 EQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVER--LKKQLRAAQLQHSEK 286
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRkeLLEEYTAELKRIEKE 467

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 46852390  287 MAQYLEEERHMREENLRLQRKLQREME--RREALCRQLSESESSLE 330
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 102-335 5.12e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   102 QARAEQEEEFISNTLFKKIQ------ALQKEKETLAVNYeKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNklM 175
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKleeaekARQAEMDRQAAIY-AEQERMAMERERELERIRQEERKRELERIRQEEIAME--I 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   176 KKIKKLENDTISKQLTLEQLRRE--KIDLENTLEQEQEALVNRLWKRMDKLEAEKrilQEKLDQPVSAPPSPRDISMEID 253
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQEleAARKVKILEEERQRKIQQQKVEMEQIRAEQ---EEARQREVRRLEEERAREMERV 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   254 SPENMMRHI---RFLKNEVERLKKQLRAAQLQHSEKMA---------QYLEEERHMREENLRLQRKLQREMERREalcRQ 321
Cdd:pfam17380 452 RLEEQERQQqveRLRQQEEERKRKKLELEKEKRDRKRAeeqrrkileKELEERKQAMIEEERKRKLLEKEMEERQ---KA 528

                         250
                  ....*....|....
gi 46852390   322 LSESESSLEMDDER 335
Cdd:pfam17380 529 IYEEERRREAEEER 542
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 94-180 7.32e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 37.51  E-value: 7.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  94 LRKASVTIQARAEQEEEFisNTLFKKIQALQKEKETLAVNYEKEEEFLT--------NELSRKLMQLQHEKAELEQHLEQ 165
Cdd:COG2825  35 LQESPEGKAAQKKLEKEF--KKRQAELQKLEKELQALQEKLQKEAATLSeeerqkkeRELQKKQQELQRKQQEAQQDLQK 112

                        90
                ....*....|....*
gi 46852390 166 EQEFQVNKLMKKIKK 180
Cdd:COG2825 113 RQQELLQPILEKIQK 127
mukB PRK04863
chromosome partition protein MukB;
61-318 7.53e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390    61 NRLASLQQENkvLKIELETYKLKCKALQEENRDL-RKASVTIQARAEQEEEFIsntLFKKI-------QALQKEKETLAv 132
Cdd:PRK04863  430 CGLPDLTADN--AEDWLEEFQAKEQEATEELLSLeQKLSVAQAAHSQFEQAYQ---LVRKIagevsrsEAWDVARELLR- 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   133 NYEKEEEfltneLSRKLMQLQHEKAELEQHLEQEQefQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEA 212
Cdd:PRK04863  504 RLREQRH-----LAEQLQQLRMRLSELEQRLRQQQ--RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390   213 LVNRlwkRMDkLEAEkrilQEKLDQPVSappsprdiSMEIDSPEnmmrhIRFLKNEVERLKKQLRAAQL---QHSEKMAQ 289
Cdd:PRK04863  577 ARER---RMA-LRQQ----LEQLQARIQ--------RLAARAPA-----WLAAQDALARLREQSGEEFEdsqDVTEYMQQ 635

                         250       260
                  ....*....|....*....|....*....
gi 46852390   290 YLEEERHMREENLRLQRKLQREMERREAL 318
Cdd:PRK04863  636 LLERERELTVERDELAARKQALDEEIERL 664
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-236 7.83e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 7.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390  55 RLEELTNRLASLQQENKVLKIELETyklkcKALQEENRDLRKASVTIQARAEQEEEfisntlfkKIQALQKEketLAVNY 134
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA--------RLAALRAQ---LGSGP 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852390 135 EKEEEFLTN----ELSRKLMQLQHEKAELEQHLeQEQEFQVNKLMKKIKKLENDtISKQL--TLEQLRREKIDL---ENT 205
Cdd:COG3206 254 DALPELLQSpviqQLRAQLAELEAELAELSARY-TPNHPDVIALRAQIAALRAQ-LQQEAqrILASLEAELEALqarEAS 331

                       170       180       190
                ....*....|....*....|....*....|.
gi 46852390 206 LEQEQEALVNRLwKRMDKLEAEKRILQEKLD 236
Cdd:COG3206 332 LQAQLAQLEARL-AELPELEAELRRLEREVE 361
 
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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