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Conserved domains on  [gi|41053405|ref|NP_956279|]
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coiled-coil domain-containing protein 6a [Danio rerio]

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 ...
 49-334 6.40e-143

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: 411.14  E-value: 6.40e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 128
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   129 VNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 208
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   209 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEKRAQYI 288
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 41053405   289 EEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDERYF 334
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 ...
 49-334 6.40e-143

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: 411.14  E-value: 6.40e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 128
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   129 VNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 208
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   209 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEKRAQYI 288
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 41053405   289 EEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDERYF 334
Cdd:pfam09755 259 QEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 50-331 1.30e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLfKKIQALQKEKETLAV 129
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-ERRRELEERLEELEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 130 NYEKEEEFLTND------LSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTL 203
Cdd:COG1196 324 ELAELEEELEELeeeleeLEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 204 EQEQEALVNRLwKRMDKLEAEKRILQEKLDQpvsappsprevsmEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEK 283
Cdd:COG1196 403 EELEEAEEALL-ERLERLEEELEELEEALAE-------------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41053405 284 RAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDE 331
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-345 1.90e-10

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: 63.15  E-value: 1.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKETLAV 129
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    130 NYEKEEEFLTnDLSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEA 209
Cdd:TIGR02168  755 ELTELEAEIE-ELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    210 LVnRLWKRMDKLEAEKRILQEKL--------DQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHT 281
Cdd:TIGR02168  833 IA-ATERRLEDLEEQIEELSEDIeslaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053405    282 EKRAQYIEEERQMREENIRLQRKLQREMERREALcrqLSESESSLEMDDERYFN-EMSAQGLRAR 345
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKiEDDEEEARRR 973
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
53-327 2.59e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   53 LEELTNRLASLQQENKVLK---IELETFKLKC----KALQEENR---------DLRKASVTIQARAEQEEEFISNtlFKK 116
Cdd:PRK03918 407 ISKITARIGELKKEIKELKkaiEELKKAKGKCpvcgRELTEEHRkelleeytaELKRIEKELKEIEEKERKLRKE--LRE 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  117 IQALQKEKETLAVNYEKEEEFltNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQL---TLEQLR 193
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQL--KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELE 562

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  194 REKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSL 273
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41053405  274 RTTELQHTEKRAQYIEEE-RQMREENIRLQRKLQREMERREALCRQLSESESSLE 327
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 82-251 4.60e-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: 38.89  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  82 KALQEENRDLRKASVTIQARAEQeeefISNTLFKKIQALQKEKETLAVNYEKEEEFLTNDLSrklMQLQHEKAELEQHLE 161
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAK----VVDKLTDFENQTEKDQTALETLEKALKDLLTDEGG---AIARKEIKDLQKELE 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 162 QEQEFQVNKLMKKIKKLENDTISKQLTLEQ-------LRREKIDLENTLEQEQEAL--VNRLWKRMDKLEAEKRILQEKL 232
Cdd:cd22656 190 KLNEEYAAKLKAKIDELKALIADDEAKLAAalrliadLTAADTDLDNLLALIGPAIpaLEKLQGAWQAIATDLDSLKDLL 269

                       170
                ....*....|....*....
gi 41053405 233 DQPVSAPPSPREVSMEIDS 251
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 ...
 49-334 6.40e-143

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: 411.14  E-value: 6.40e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 128
Cdd:pfam09755  19 SPVTREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKETLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   129 VNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 208
Cdd:pfam09755  99 MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   209 ALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEKRAQYI 288
Cdd:pfam09755 179 ALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTEKMAQYA 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 41053405   289 EEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDERYF 334
Cdd:pfam09755 259 QEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 50-331 1.30e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLfKKIQALQKEKETLAV 129
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-ERRRELEERLEELEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 130 NYEKEEEFLTND------LSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTL 203
Cdd:COG1196 324 ELAELEEELEELeeeleeLEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 204 EQEQEALVNRLwKRMDKLEAEKRILQEKLDQpvsappsprevsmEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEK 283
Cdd:COG1196 403 EELEEAEEALL-ERLERLEEELEELEEALAE-------------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41053405 284 RAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDE 331
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-345 1.90e-10

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: 63.15  E-value: 1.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKETLAV 129
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    130 NYEKEEEFLTnDLSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEA 209
Cdd:TIGR02168  755 ELTELEAEIE-ELEERLEEAEEELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    210 LVnRLWKRMDKLEAEKRILQEKL--------DQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHT 281
Cdd:TIGR02168  833 IA-ATERRLEDLEEQIEELSEDIeslaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053405    282 EKRAQYIEEERQMREENIRLQRKLQREMERREALcrqLSESESSLEMDDERYFN-EMSAQGLRAR 345
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKiEDDEEEARRR 973
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-330 1.58e-09

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: 60.47  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQALQKEKEtlav 129
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIE---- 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    130 NYEKEEEFLTNDLSR---KLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKK-----------LENDTISKQLTLEQLRRE 195
Cdd:TIGR02169  755 NVKSELKELEARIEEleeDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEevsriearlreIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    196 KIDLENTLEqEQEALVNRLWKRMDKLEAEKRILQEKLdqpvsappspREVSMEIDSPENMMRHirfLKSEVERLKRSLRT 275
Cdd:TIGR02169  835 IQELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEEL----------EELEAALRDLESRLGD---LKKERDELEAQLRE 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 41053405    276 TELQHTEKRAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDD 330
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-313 3.42e-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: 59.30  E-value: 3.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     52 RLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQAR-AEQEEEFIS-----NTLFKKIQALQKEKE 125
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEiEELQKELYAlaneiSRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    126 TLAVNYEKEEEFLTNDLSRK------LMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDL 199
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLdelaeeLAELEEKLEELKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    200 ENTLE------QEQEALVNRLWKRMDKLEAEKRILQEKLDqpvsaPPSPREVSMEIDSPENMmrhIRFLKSEVERLKRSL 273
Cdd:TIGR02168  392 ELQIAslnneiERLEARLERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEE---LEELQEELERLEEAL 463

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 41053405    274 RTTELQHTEKRAQYIEEERQMREENIRLqRKLQREMERRE 313
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARL-DSLERLQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-332 4.77e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 4.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  53 LEELTNRLASL-------------QQENKVLKIELETFKLkcKALQEENRDLRKASVTIQARAEQEEEFISNtLFKKIQA 119
Cdd:COG1196 195 LGELERQLEPLerqaekaeryrelKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAE-LEAELEE 271

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 120 LQKEKETLAVNYE---KEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEF--QVNKLMKKIKKLENDTISKQLTLEQLRR 194
Cdd:COG1196 272 LRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELeeELAELEEELEELEEELEELEEELEEAEE 351

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 195 EKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsPREVSMEIDSPENMMRHIRFLKSEVERLKRSLR 274
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-------LRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41053405 275 TTELQHTEKRAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDER 332
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 49-315 2.46e-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: 56.61  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLA 128
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    129 VNYEKEeeflTNDLSRKLMQLQHEKAELEQHL----EQEQEF--QVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENT 202
Cdd:TIGR02169  815 REIEQK----LNRLTLEKEYLEKEIQELQEQRidlkEQIKSIekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    203 LE-------------QEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSpenmmrhIRFLKSEVERL 269
Cdd:TIGR02169  891 RDeleaqlrelerkiEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-------LEDVQAELQRV 963

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 41053405    270 KRSLRTTELQHTEKRAQYIEEERQMREenirLQRKLQREMERREAL 315
Cdd:TIGR02169  964 EEEIRALEPVNMLAIQEYEEVLKRLDE----LKEKRAKLEEERKAI 1005
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
53-327 2.59e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   53 LEELTNRLASLQQENKVLK---IELETFKLKC----KALQEENR---------DLRKASVTIQARAEQEEEFISNtlFKK 116
Cdd:PRK03918 407 ISKITARIGELKKEIKELKkaiEELKKAKGKCpvcgRELTEEHRkelleeytaELKRIEKELKEIEEKERKLRKE--LRE 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  117 IQALQKEKETLAVNYEKEEEFltNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQL---TLEQLR 193
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQL--KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELE 562

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  194 REKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSL 273
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41053405  274 RTTELQHTEKRAQYIEEE-RQMREENIRLQRKLQREMERREALCRQLSESESSLE 327
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-327 4.90e-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: 52.37  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     53 LEELTNRLASLQQENKVLKieletfklKCKALQEENRDLRKASVTIQARAEQEEEfisNTLFKKIQALQKEKETLAVNYE 132
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAE--------RYKELKAELRELELALLVLRLEELREEL---EELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    133 KEEEfltndlsrKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQealvn 212
Cdd:TIGR02168  264 ELEE--------KLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE----- 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    213 rlwKRMDKLEAEKRILQEKLDqpvsappsprEVSMEIDSPENMMRHirfLKSEVERLKRSLRTTELQHTEKRAQYIEEER 292
Cdd:TIGR02168  330 ---SKLDELAEELAELEEKLE----------ELKEELESLEAELEE---LEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 41053405    293 QMREENIRLQR---KLQREMERREALCRQLSESESSLE 327
Cdd:TIGR02168  394 QIASLNNEIERleaRLERLEDRRERLQQEIEELLKKLE 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-327 9.44e-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: 50.92  E-value: 9.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 115 KKIQALQKEKETLAVNYEKEEEfltndlsrKLMQLQHEKAELEQHLEQeQEFQVNKLMKKIKKLENDTISKQLTLEQLRR 194
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 195 EKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILqekldqpvsappSPREVSMEIDSPENMMRHIRFLKSEVERLKRS 272
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRAlyRLGRQPPLALLL------------SPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41053405 273 LRTTELQHTEKRAQyIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLE 327
Cdd:COG4942 159 LAELAALRAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 50-332 8.18e-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: 8.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLfKKIQALQKEKETLAV 129
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEE 421

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 130 NYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQvnKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEA 209
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 210 LVNRLWKRMDKLEAEKRILQEKLDQPVS-------APPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSL--RTTELQH 280
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAvligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagRATFLPL 579

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41053405 281 TEKRAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDER 332
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 52-332 1.59e-05

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: 47.37  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     52 RLEELTNRLASLQQENKVLKIELETfKLKCKALQEEnrdLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLavny 131
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRREREK-AERYQALLKE---KREYEGYELLKEKEALERQKEAIERQLASLEEELEKL---- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    132 ekeeEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLeQEQEALV 211
Cdd:TIGR02169  257 ----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-AKLEAEI 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    212 NRLWKRMDKLEAEKRILQEKLDQpvsappspreVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEKRAQYIEEE 291
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDK----------LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 41053405    292 RQMREENIRLQRKLQREMERREALCRQLSESESSL-EMDDER 332
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKInELEEEK 443
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 49-254 2.16e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEfisntlfkKIQALQKE-KETL 127
Cdd:COG3883  21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------EIEERREElGERA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 128 AVNYEKE---------------EEFLTN--------DLSRKLM-QLQHEKAELEQhLEQEQEFQVNKLMKKIKKLEndti 183
Cdd:COG3883  93 RALYRSGgsvsyldvllgsesfSDFLDRlsalskiaDADADLLeELKADKAELEA-KKAELEAKLAELEALKAELE---- 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41053405 184 SKQLTLEQLRREKIDLENTLEQEQEALVNRLwkrmDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPEN 254
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQL----AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 48-319 5.54e-05

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: 45.73  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     48 ISQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEfiSNTLFKKIQALQKEKETL 127
Cdd:pfam02463  259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE--SEKEKKKAEKELKKEKEE 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    128 AVNYEKEEEFLTNDLSRKLMQLQhEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREK--IDLENTLEQ 205
Cdd:pfam02463  337 IEELEKELKELEIKREAEEEEEE-ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEkeAQLLLELAR 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    206 EQEALVNRLWKRMDKLEAEKRILQEKLdqpvsappspREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTTELQHTEKRA 285
Cdd:pfam02463  416 QLEDLLKEEKKEELEILEEEEESIELK----------QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485

                          250       260       270
                   ....*....|....*....|....*....|....
gi 41053405    286 QYIEEERQMREENIRLQRKLQREMERREALCRQL 319
Cdd:pfam02463  486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-207 8.12e-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: 45.43  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKAsvtiQARAEQEEEFISNTLF---KKIQALQKEKE 125
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIErleARLERLEDRRE 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    126 TLAVNYEKEEEFLTN----DLSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLEN 201
Cdd:TIGR02168  418 RLQQEIEELLKKLEEaelkELQAELEELEEELEELQEELERLEE-ALEELREELEEAEQALDAAERELAQLQARLDSLER 496


                   ....*.
gi 41053405    202 TLEQEQ 207
Cdd:TIGR02168  497 LQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 144-340 1.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 144 RKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALvNRLWKRMDKLEA 223
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQ 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 224 EKRILQEKldqpvsappsprevsmeidspenmmrhIRFLKSEVERLKRSLRTTELQHTEKRAQYIEEERQMREENIRL-- 301
Cdd:COG1196 303 DIARLEER---------------------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELee 355

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 41053405 302 -QRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQ 340
Cdd:COG1196 356 aEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 49-234 1.33e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  49 SQSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFIsNTLFKKIQALQKEKETLA 128
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 129 VNYEKEEEFLT------------------------NDLSRKLMQLQHEKAELEQHLEQ---------EQEFQVNKLMKKI 175
Cdd:COG4942  97 AELEAQKEELAellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEElradlaelaALRAELEAERAEL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41053405 176 KKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLwkrmDKLEAEKRILQEKLDQ 234
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIAR 231
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
152-307 1.53e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 152 EKAELEQHLEQEQEFQVNKLMKKIKKLENdtiskqlTLEQLRREKIDLENTLEqeqealvnrlwkrmdklEAEKRI--LQ 229
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELE-----------------EKDERIerLE 447

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053405 230 EKLdqpvsappspREVSMEIDSPENMMRHIRFLKSEVERLKRSLrttelqhtekraqyiEEERQMREEnirLQRKLQR 307
Cdd:COG2433 448 REL----------SEARSEERREIRKDREISRLDREIERLEREL---------------EEERERIEE---LKRKLER 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
50-307 1.66e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   50 QSRLEELTNRLASLQQENKVLKIELEtfklkckALQEENRDLRKASVTIQARAEQEEEFI-SNTLFKKIQALQKEKETLa 128
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLE-------ALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERL- 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  129 vnyekeeefltNDLSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQE 208
Cdd:COG4913  681 -----------DASSDDLAALEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  209 ALVNRLW-----------------KRMDKLEAEKRILQEKLDQPVSA-----PPSPREVSMEIDSPENMMRHIRFLKSE- 265
Cdd:COG4913  749 ALLEERFaaalgdaverelrenleERIDALRARLNRAEEELERAMRAfnrewPAETADLDADLESLPEYLALLDRLEEDg 828

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 41053405  266 ----VERLKRSLRTTELQHTEKRAQYIEEERQMREENI-RLQRKLQR 307
Cdd:COG4913  829 lpeyEERFKELLNENSIEFVADLLSKLRRAIREIKERIdPLNDSLKR 875
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 140-345 1.84e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 140 NDLSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLwkrmd 219
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQA-ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA----- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 220 kleaekRILQEKldqpvSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLRTT-----ELQHTEKRAQYIEEE-RQ 293
Cdd:COG3883  93 ------RALYRS-----GGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELkadkaELEAKKAELEAKLAElEA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41053405 294 MREENIRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQGLRAR 345
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-234 1.92e-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: 43.90  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEefisntlfKKIQALQKEKETLAV 129
Cdd:TIGR02169  839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE--------AQLRELERKIEELEA 910

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    130 NYEKEEEFLtNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLmkKIKKLendtiskQLTLEQLRREKIDLE---NTLEQE 206
Cdd:TIGR02169  911 QIEKKRKRL-SELKAKLEALEEELSEIEDPKGEDEEIPEEEL--SLEDV-------QAELQRVEEEIRALEpvnMLAIQE 980

                          170       180       190
                   ....*....|....*....|....*....|.
gi 41053405    207 QEALVNR---LWKRMDKLEAEKRILQEKLDQ 234
Cdd:TIGR02169  981 YEEVLKRldeLKEKRAKLEEERKAILERIEE 1011
PRK14644 PRK14644
hypothetical protein; Provisional
 115-204 3.01e-04

hypothetical protein; Provisional


Pssm-ID: 184779 [Multi-domain]  Cd Length: 136  Bit Score: 40.98  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  115 KKIQALQKEKETLAVNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQ---LTLE- 190
Cdd:PRK14644  39 KDIEELTKEISDFIDNLSVEFDFDSLDISSPGFDMDYETDELENHIGEIIDVSLNKEVNKTDFITGELLENNpetITLKw 118

                         90
                 ....*....|....*...
gi 41053405  191 ----QLRREKIDLENTLE 204
Cdd:PRK14644 119 nckgQFRKVEINKENIKK 136
PRK12704 PRK12704
phosphodiesterase; Provisional
 91-230 3.04e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   91 LRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAvnyeKEEEF-LTNDLSRKLMQLQHEKAELEQHLEQEQEfQVN 169
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA----KEEIHkLRNEFEKELRERRNELQKLEKRLLQKEE-NLD 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41053405  170 KLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILQE 230
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEEAKEILLEK 162
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 93-235 3.96e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   93 KASVTIQARAEQEEEFISNTLFKKIQALQKEKEtlAVNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEqefqVNKLM 172
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEE--AEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE----AQQAI 579

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41053405  173 KKIKKlENDTISKQLtleQLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDQP 235
Cdd:PRK00409 580 KEAKK-EADEIIKEL---RQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKEKQEEL 637
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-327 4.75e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   73 ELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISN-TLFKKIQALQKEKETLAVNYEKEEEFLTNDLSRKLMQLQH 151
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  152 EKAELEQHLEQEQEFQVNK--LMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRlWKRMDKLEAEKRILQ 229
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLaeLEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE-YLELKDAEKELEREE 618

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  230 EKLDQpvsappSPREVSMEIDSPENMMRHIRFLKSEVERLKRslRTTELQHTEKRAQYIEEERQM-------------RE 296
Cdd:PRK03918 619 KELKK------LEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELaglraeleelekrRE 690

                        250       260       270
                 ....*....|....*....|....*....|.
gi 41053405  297 ENIRLQRKLQREMERREALCRQLSESESSLE 327
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALE 721
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 50-230 6.15e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    50 QSRLEELTNRLASLQQENKVLKIELETFKLKCKALQEE-----------NRDLRKASVTIQARAEQEEEFISNTLFKKIQ 118
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEleqnnkkikelEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   119 ALQKEKETLAVNYEKEEEfLTNDLSRKLMQLQHEKAELEQHlEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKID 198
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNK-IISQLNEQISQLKKELTNSESE-NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395

                         170       180       190
                  ....*....|....*....|....*....|..
gi 41053405   199 LENTLeQEQEALVNRLWKRMDKLEAEKRILQE 230
Cdd:TIGR04523 396 LESKI-QNQEKLNQQKDEQIKKLQQEKELLEK 426
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
77-234 6.67e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 6.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  77 FKLKCKALQEENRDLRKASVTIQARAEQEEEFisNTLFKKIQALQKEKETLavnyEKEEEFLTNDLSRKLMQLQH----- 151
Cdd:COG4717  59 FKPQGRKPELNLKELKELEEELKEAEEKEEEY--AELQEELEELEEELEEL----EAELEELREELEKLEKLLQLlplyq 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 152 EKAELEQHLEQEQEfQVNKLMKKIKKLENdtisKQLTLEQLRREKIDLENTLEQEQEAL-------VNRLWKRMDKLEAE 224
Cdd:COG4717 133 ELEALEAELAELPE-RLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLslateeeLQDLAEELEELQQR 207

                       170
                ....*....|
gi 41053405 225 KRILQEKLDQ 234
Cdd:COG4717 208 LAELEEELEE 217
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
128-319 7.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 128 AVNYEKEEEFLTNDLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDtiskqltLEQLRREKIDLENTLEQ-E 206
Cdd:COG4717  50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-------LEELEAELEELREELEKlE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 207 QEALVNRLWKRMDKLEAEKRILQEKLDqpvsappsprEVSMEIDSPENMMRHIRFLKSEVERLKRSLRTT---------- 276
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLE----------ELEERLEELRELEEELEELEAELAELQEELEELleqlslatee 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41053405 277 ELQHTEKRAQYIEEERQMREENI-RLQRKLQREMERREALCRQL 319
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELeEAQEELEELEEELEQLENEL 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
148-326 1.01e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  148 QLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDtiskqltLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRI 227
Cdd:COG4913  285 FAQRRLELLEAELEELRA-ELARLEAELERLEAR-------LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  228 LQEKLDQ--------PVSAPPSPREVsmeidspENMMRHIRFLKSEVERLKRSLRTTELQHTEKRAQYIEEERQMREE-- 297
Cdd:COG4913  357 RERRRARleallaalGLPLPASAEEF-------AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEia 429

                        170       180       190
                 ....*....|....*....|....*....|.
gi 41053405  298 NIRLQRKL--QREMERREALCRQLSESESSL 326
Cdd:COG4913  430 SLERRKSNipARLLALRDALAEALGLDEAEL 460
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 144-321 1.02e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 144 RKLMQLQHEKAELEQ--HLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEalvnrlwkRMDKL 221
Cdd:COG1579   7 RALLDLQELDSELDRleHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA--------RIKKY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 222 eaekrilQEKLDQpVSappSPREV---SMEIDSPENMMR----HIRFLKSEVERLKRSLRTTELQHTEKRAQYIEEERQM 294
Cdd:COG1579  79 -------EEQLGN-VR---NNKEYealQKEIESLKRRISdledEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147

                       170       180
                ....*....|....*....|....*..
gi 41053405 295 REENIRLQRKLQREMERREALCRQLSE 321
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPP 174
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 65-333 1.11e-03

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: 41.50  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405     65 QENKVLKIELETFKLKCKALQEENRDLRKasVTIQARAEQEEEFISNTLFKKiqalqkEKETLAVNYEKEEEFLTNDLSR 144
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELE------EEYLLYLDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    145 KLMQLQHEKAELEQHLEQEQEF--QVNKLMKKIKKLENDTISKQLTL----EQLRREKIDLE---NTLEQEQEALVNRLW 215
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEEELKLLakeeEELKSELLKLErrkVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405    216 KRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKRSLR----TTELQHTEKRAQYIEEE 291
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESerlsSAAKLKEEELELKSEEE 404

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 41053405    292 RQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDERY 333
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKL 446
PRK12704 PRK12704
phosphodiesterase; Provisional
 115-234 1.58e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  115 KKIQALQKEKETLAVNYEKEEEFLtndlsRKLMQLQHEKAELEQHLEQEQEFQVNKlmKKIKKLENDTISKQltlEQLRR 194
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAI-----KKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKE---ENLDR 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 41053405  195 EKIDLENtLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQ 234
Cdd:PRK12704 101 KLELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEE 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 51-206 1.70e-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: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  51 SRLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFI--------SNTLFKKIQALQK 122
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyeeqlgNVRNNKEYEALQK 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 123 EKETLavnyEKEEEFLTNDLSRKLMQLQHEKAELEQhLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENT 202
Cdd:COG1579  97 EIESL----KRRISDLEDEILELMERIEELEEELAE-LEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171


                ....
gi 41053405 203 LEQE 206
Cdd:COG1579 172 IPPE 175
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
51-332 1.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   51 SRLEELTNRLASLQQENKVLKIELETFKlKCKALQEENRDLRKasvtiqaraeQEEEFISNTLFKKIQALQKEKETLavn 130
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKK----------RLTGLTPEKLEKELEELEKAKEEI--- 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  131 yEKEEEFLTndlsRKLMQLQHEKAELEQHL------------------EQEQEFQVNKLMKKIKKLENDTISKQLTLEQL 192
Cdd:PRK03918 404 -EEEISKIT----ARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  193 RREKIDLENTLEQEQEALVNR-LWKRMDKLEAE-KRILQEKLDQPVSAPPSPREVSMEIDSpenmmrHIRFLKSEVER-- 268
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKeLAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKG------EIKSLKKELEKle 552

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053405  269 -LKRSLRTTELQHTEKRAQYIEEERQMREENIRLQRKLQREMERREALCRQ---LSESESSLEMDDER 332
Cdd:PRK03918 553 eLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKE 620
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-212 2.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  48 ISQSRLEELTNRLASLQQENKvlkiELETFKLKCKALQEENRDLRKASVTIQARAEQEEEFISN-TLFKKIQALQKEKET 126
Cdd:COG4717  68 LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAE 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 127 LAVNYEKEEEFLTN---------DLSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKI 197
Cdd:COG4717 144 LPERLEELEERLEElreleeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223

                       170
                ....*....|....*
gi 41053405 198 DLENTLEQEQEALVN 212
Cdd:COG4717 224 ELEEELEQLENELEA 238
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
52-327 2.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   52 RLEELTNRLASLQQENKVLKIELETFKLKCKALQEENRDLRKASVTIQARAEQEEEfisntlfkkIQALQKEKETLAVNY 131
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE---------LKEKAEEYIKLSEFY 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  132 EKEEEFLtNDLSRKLMQLQHEKAELEQHLEQ--EQEFQVNKLMKKIKKLENDTI---SKQLTLEQLRREKIDLENTLEQE 206
Cdd:PRK03918 303 EEYLDEL-REIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEeleERHELYEEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  207 QEALVNRLWKRMDKLEAEKRILQEKLdqpvsappspREVSMEIDSPENmmrHIRFLKSEVERLKRSLR------------ 274
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEI----------SKITARIGELKK---EIKELKKAIEELKKAKGkcpvcgreltee 448

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41053405  275 ---------TTELQHTEKRAQYIEE-ERQMREENIRLQRKLQREME--RREALCRQLSESESSLE 327
Cdd:PRK03918 449 hrkelleeyTAELKRIEKELKEIEEkERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
COG5022 COG5022
Myosin heavy chain [General function prediction only];
55-336 2.56e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405   55 ELTNRLASLQQENKVLKIELETFKLKC-KALQEENR--DLRKASVTIQARAEQEEefisntLFKKIQALQKEKETLA--- 128
Cdd:COG5022  825 TIKREKKLRETEEVEFSLKAEVLIQKFgRSLKAKKRfsLLKKETIYLQSAQRVEL------AERQLQELKIDVKSISslk 898

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  129 -VNYEKEEEF--LTNDLSRKLM---QLQHEK-AELEQHLEqEQEFQVNKLMKKIKKLEndTISKQLTLEQLRREKIDLEN 201
Cdd:COG5022  899 lVNLELESEIieLKKSLSSDLIenlEFKTELiARLKKLLN-NIDLEEGPSIEYVKLPE--LNKLHEVESKLKETSEEYED 975

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  202 TLEQEqEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPREVSMEIDSPENMMRHIRFLKSEVERLKrslRTTELQHT 281
Cdd:COG5022  976 LLKKS-TILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELS---ILKPLQKL 1051

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41053405  282 EKRAQYIEEERQMREENIRLQRKLQREMERREALCRQLSESESSLEMDDERYFNE 336
Cdd:COG5022 1052 KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNR 1106
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
198-329 3.38e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 198 DLENTLEQeqeaLVNRLWKRMDKLEAEKRILQ--------EKLDQPVSAPPSPREVSMEIDSPEN---MMRHIRFLKSEV 266
Cdd:COG2433 347 AYKNKFER----VEKKVPPDVDRDEVKARVIRglsieealEELIEKELPEEEPEAEREKEHEERElteEEEEIRRLEEQV 422

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 267 ERLK---RSLRtTELQHTEKRAQYIEEE------------------RQMREENIRLQRKLQREMERREALCRQLSESESS 325
Cdd:COG2433 423 ERLEaevEELE-AELEEKDERIERLERElsearseerreirkdreiSRLDREIERLERELEEERERIEELKRKLERLKEL 501


                ....
gi 41053405 326 LEMD 329
Cdd:COG2433 502 WKLE 505
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 82-251 4.60e-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: 38.89  E-value: 4.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  82 KALQEENRDLRKASVTIQARAEQeeefISNTLFKKIQALQKEKETLAVNYEKEEEFLTNDLSrklMQLQHEKAELEQHLE 161
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAK----VVDKLTDFENQTEKDQTALETLEKALKDLLTDEGG---AIARKEIKDLQKELE 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 162 QEQEFQVNKLMKKIKKLENDTISKQLTLEQ-------LRREKIDLENTLEQEQEAL--VNRLWKRMDKLEAEKRILQEKL 232
Cdd:cd22656 190 KLNEEYAAKLKAKIDELKALIADDEAKLAAalrliadLTAADTDLDNLLALIGPAIpaLEKLQGAWQAIATDLDSLKDLL 269

                       170
                ....*....|....*....
gi 41053405 233 DQPVSAPPSPREVSMEIDS 251
Cdd:cd22656 270 EDDISKIPAAILAKLELEK 288
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 50-213 5.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  50 QSRLEELTNRLASLQQENKVLKIELETFKLKCK----ALQEENRD------LRKASVTIQARAEQEEEFISNTLFKKIQA 119
Cdd:COG4942  75 EQELAALEAELAELEKEIAELRAELEAQKEELAellrALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEE 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 120 LQKEKETLAVNyEKEEEFLTNDLSRKLMQLQHEKAELEQhLEQEQEFQVNKLMKKIKKLENdtiskqlTLEQLRREKIDL 199
Cdd:COG4942 155 LRADLAELAAL-RAELEAERAELEALLAELEEERAALEA-LKAERQKLLARLEKELAELAA-------ELAELQQEAEEL 225

                       170
                ....*....|....
gi 41053405 200 ENTLEQEQEALVNR 213
Cdd:COG4942 226 EALIARLEAEAAAA 239
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
50-234 6.37e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 6.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405  50 QSRLEELTNRLASLQQENKVLKIELETfKLKCKALQEENRDLRKASVTI---QARAEQEEEFISNTLFKK--------IQ 118
Cdd:COG3206 188 RKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSELESQLAEARAELaeaEARLAALRAQLGSGPDALpellqspvIQ 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053405 119 ALQKEKETLAVNYEKEEEFLTNDlSRKLMQLQHEKAELEQHLEQEQEfqvnklmKKIKKLENDTISKQLTLEQLRREKID 198
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPN-HPDVIALRAQIAALRAQLQQEAQ-------RILASLEAELEALQAREASLQAQLAQ 338

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 41053405 199 LENTLEQEQEALVnrlwkRMDKLEAEKRILQEKLDQ 234
Cdd:COG3206 339 LEARLAELPELEA-----ELRRLEREVEVARELYES 369
 
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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