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Conserved domains on  [gi|46276360|gb|AAS86437|]
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kazrin isoform D [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-167 1.20e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 162
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492


                ....*
gi 46276360 163 RHSLA 167
Cdd:COG1196 493 LLLLL 497
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-167 1.20e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 162
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492


                ....*
gi 46276360 163 RHSLA 167
Cdd:COG1196 493 LLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-160 1.59e-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: 52.75  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     25 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360    102 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
25-146 4.09e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESE 94
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHN 341

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46276360   95 DAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 26-168 7.94e-05

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: 44.43  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    26 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 101
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46276360   102 KEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 168
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 31-157 6.04e-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: 37.73  E-value: 6.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  31 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 109
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 46276360 110 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:cd22656 179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-167 1.20e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 82
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  83 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 162
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492


                ....*
gi 46276360 163 RHSLA 167
Cdd:COG1196 493 LLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-160 1.59e-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: 52.75  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     25 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360    102 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-159 1.62e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlrdfIR 84
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RR 312

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46276360  85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-158 4.42e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46276360  85 ---NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG1196 394 aaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 25-159 4.91e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 4.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 104
Cdd:COG1579  28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46276360 105 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG1579  99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-156 1.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   2 KEMLAKDLEESQGGKSSEVLSATELRVQL--------------AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 67
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  68 LYATLESREEQLRDF---IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEA 144
Cdd:COG1196 335 LEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                       170
                ....*....|..
gi 46276360 145 ELAMAKQSLATL 156
Cdd:COG1196 415 RLERLEEELEEL 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-162 1.87e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 1.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   2 KEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 81
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  82 FIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 140
Cdd:COG4942 109 LLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                       170       180
                ....*....|....*....|..
gi 46276360 141 ELEAELAMAKQSLATLTKDVPK 162
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAE 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-159 4.32e-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: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   2 KEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM---QQLYATLESREEQ 78
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  79 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400


                .
gi 46276360 159 D 159
Cdd:COG1196 401 Q 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-158 5.07e-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: 48.14  E-value: 5.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360      3 EMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATL-ESREEQLRD 81
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQA 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     82 FIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878


                   ....
gi 46276360    155 TLTK 158
Cdd:TIGR02169  879 DLES 882
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-157 6.60e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 6.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46276360  85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-147 9.88e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 9.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   27 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDF------IRNYEQHRKE---SEDAV 97
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVasaereIAELEAELERldaSSDDL 687

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 46276360   98 KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELA 147
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-160 1.26e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  19 EVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVK 98
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46276360  99 ALAKEKDL-------LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG1196 303 DIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
19-160 1.66e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   19 EVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvsqmQQLYATLESREEQLRdfirnyEQHRKESEDAVK 98
Cdd:COG4913  272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL----EARLDALREELDELE------AQIRGNGGDRLE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46276360   99 ALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4913  342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-160 2.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     25 ELRVQLAQKEQELA-----RAKEALQAMKADRKRLKGEKTDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVKA 99
Cdd:TIGR02168  217 ELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46276360    100 LAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
24-160 2.30e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKE 103
Cdd:COG4372  48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKE 123

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46276360 104 KDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4372 124 RQDLEQQRKQLEAQIAE-------LQSEIAEREEELKELEEQLESLQEELAALEQEL 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-160 2.35e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 2.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 104
Cdd:COG4717  92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46276360 105 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-159 2.65e-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: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL----YATLESREEQLRDFIRNYEQHRKESEDAVKAL 100
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAAL 371

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 46276360  101 AKEKDLLEREKWELRRQAKEATDHATALRSQLdlkDNRMKELEAELAMAKQSLATLTKD 159
Cdd:COG4913  372 GLPLPASAEEFAALRAEAAALLEALEEELEAL---EEALAEAEAALRDLRRELRELEAE 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-164 3.00e-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: 45.83  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46276360    102 KEKDLLEREKWELrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRH 164
Cdd:TIGR02169  765 ARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
25-146 4.09e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESE 94
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHN 341

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46276360   95 DAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 29-120 4.15e-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: 44.75  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                        90
                ....*....|..
gi 46276360 109 REKWELRRQAKE 120
Cdd:COG4942  97 AELEAQKEELAE 108
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
9-160 5.91e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 5.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   9 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 82
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46276360  83 IRNYEQHRKESEDAVKALAKEKDLLerekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-158 6.85e-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: 44.66  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360      2 KEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRD 81
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     82 FIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATD-------HATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRRELE 918


                   ....
gi 46276360    155 TLTK 158
Cdd:TIGR02168  919 ELRE 922
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 26-168 7.94e-05

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: 44.43  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    26 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkala 101
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLeeaLSEKERIIERLkEQREREDRERLEELESLKKENKDL----- 480

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46276360   102 KEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAM 168
Cdd:pfam10174 481 KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-156 8.44e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEA---LQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALA 101
Cdd:COG4913  665 SAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAE 740

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 46276360  102 KEKDLLEREKWELRRQAKEATDHATALRSQLdlkDNRMKELEAELAMAKQSLATL 156
Cdd:COG4913  741 DLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERA 792
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-156 1.37e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  23 ATELRVQLAQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 96
Cdd:COG1196 215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46276360  97 ----VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 156
Cdd:COG1196 293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-161 1.73e-04

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: 43.51  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360      1 MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLR 80
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     81 DFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKELQAELEELEEELEELQEEL 456


                   .
gi 46276360    161 P 161
Cdd:TIGR02168  457 E 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-149 2.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 103
Cdd:COG4913  327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46276360  104 KDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMA 149
Cdd:COG4913  407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 5-156 3.62e-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: 42.27  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360      5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlYATLESREEQLRDFIR 84
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQE 366

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360     85 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 156
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
24-158 4.12e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 4.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  24 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLV--SQMQQLYATLESREEQLRDFIRNY-EQHRKesedaVKAL 100
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYtPNHPD-----VIAL 296

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46276360 101 AKEKDLLERekwELRRQAKEAtdhATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:COG3206 297 RAQIAALRA---QLQQEAQRI---LASLEAELEALQAREASLQAQLAQLEARLAELPE 348
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 23-249 4.89e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 4.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  23 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 90
Cdd:COG3883  32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  91 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 146
Cdd:COG3883 112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360 147 AMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPS 224
Cdd:COG3883 192 AAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                       250       260
                ....*....|....*....|....*
gi 46276360 225 VISDASAAEGDRSSTPSDINSPRHR 249
Cdd:COG3883 272 AGAGAAAASAAGGGAGGAGGGGGGG 296
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 26-161 7.09e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 7.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  26 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 105
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360 106 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:COG0542 460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
17-158 9.06e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 9.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   17 SSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDA 96
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRET 531

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46276360   97 VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 29-103 1.05e-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: 40.52  E-value: 1.05e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46276360  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 103
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 25-183 1.12e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 103
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   104 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 181
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570


                  ..
gi 46276360   182 VQ 183
Cdd:TIGR04523 571 EE 572
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-131 1.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEK 104
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                         90       100
                 ....*....|....*....|....*..
gi 46276360  105 DLLEREKWELRRQAKEATDHATALRSQ 131
Cdd:COG4913  769 ENLEERIDALRARLNRAEEELERAMRA 795
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 7-163 1.27e-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: 39.52  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   7 KDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKTDLVSQMQQLYATLESREE 77
Cdd:COG1579  34 AELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKRRISDLED 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  78 QLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRMKELEAELAMAKQSLATLT 157
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEELAELEAELEELEAEREELA 169


                ....*.
gi 46276360 158 KDVPKR 163
Cdd:COG1579 170 AKIPPE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-138 1.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEA--------LQAMKADRKRLKGEKTDLVSQMQQLYATLESRE 76
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALG 372

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46276360   77 EQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLD-LKDNR 138
Cdd:COG4913  373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERRK 435
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 25-153 1.33e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    25 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 104
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 46276360   105 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 153
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 22-109 1.52e-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: 40.13  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  22 SATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 101
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100


                ....*...
gi 46276360 102 KEKDLLER 109
Cdd:COG4942 101 AQKEELAE 108
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
29-150 1.59e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  29 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG2268 238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 46276360 109 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 150
Cdd:COG2268 306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 7-158 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: 40.00  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     7 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 86
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46276360    87 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 158
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 29-121 1.69e-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: 39.75  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 108
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        90
                ....*....|...
gi 46276360 109 REKWELRRQAKEA 121
Cdd:COG4942 227 ALIARLEAEAAAA 239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-155 2.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    7 KDLEESQGGKSSEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY 86
Cdd:PRK02224 229 REQARETRDEADEVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   87 EQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALRSQLDLKDNRMKELEAELAMAKQS 152
Cdd:PRK02224 303 GLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLEERAEELREEAAELESELEEAREA 378


                 ...
gi 46276360  153 LAT 155
Cdd:PRK02224 379 VED 381
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 25-157 2.54e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 38.94  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    25 ELRVQLAQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 91
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    92 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN----RMKELEAELAMAKQSLATLT 157
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-155 3.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   22 SATELRVQLAQKEQE-----LARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQlRDFIRNYEQHRKESEDA 96
Cdd:PRK02224 188 SLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRET 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360   97 VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD-------NRMKELEAELAMAKQSLAT 155
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEE 332
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
5-154 3.35e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   5 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR 84
Cdd:COG4372  78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46276360  85 NYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLA 154
Cdd:COG4372 158 QLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 23-153 4.25e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   23 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT---DLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKA 99
Cdd:COG3096  514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQ-LEQLRA 592

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46276360  100 LAKE-----------KDLLERekweLRRQAKEATDHATALRSQLDLKDNRMKELEAE---LAMAKQSL 153
Cdd:COG3096  593 RIKElaarapawlaaQDALER----LREQSGEALADSQEVTAAMQQLLEREREATVErdeLAARKQAL 656
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 27-160 6.00e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 38.12  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    27 RVQLAQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 106
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46276360   107 LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 31-157 6.04e-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: 37.73  E-value: 6.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  31 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 109
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 46276360 110 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 157
Cdd:cd22656 179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
PTZ00121 PTZ00121
MAEBL; Provisional
 16-145 6.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    16 KSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfIRNYEQHRKESED 95
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEE 1658

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46276360    96 AVKALAKEKDLLEREKW---ELRRQAKEATDHATALRSQLD--LKDNRMKELEAE 145
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 25-185 8.02e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.88  E-value: 8.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360   25 ELRVQLAQKEQELARAKEALQAMKADrkrlkgektdlvsqMQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEK 104
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEE--------------LEEKKEKLQEEEDKLL------EEAEKEAQQAIKEAKKEA 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  105 DLLEREKWELRRQAKEAtdhatalrsqldLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGETV----------- 173
Cdd:PRK00409 587 DEIIKELRQLQKGGYAS------------VKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgev 654

                        170
                 ....*....|....
gi 46276360  174 --LNGNQEWVVQAD 185
Cdd:PRK00409 655 lsIPDDKEAIVQAG 668
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-160 8.37e-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: 38.11  E-value: 8.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     29 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY----EQHRKESEDA------VK 98
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAanlrerLE 827

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46276360     99 ALAKEKDLLEREKWELRRQAKEATDHATAL--------------RSQLDLKDNRMKELEAELAMAKQSLATLTKDV 160
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNERASLEEALALLRSELEELSEEL 903
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 16-108 8.38e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 36.80  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    16 KSSEVLSATELRVQLAQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYATLESREEQLRDFIRNYEqhrkese 94
Cdd:pfam10368  55 LSDEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELIDAMEERYEAYDELYDAYK------- 125

                          90
                  ....*....|....
gi 46276360    95 davKALAKEKDLLE 108
Cdd:pfam10368 126 ---KALELDKELYE 136
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-160 8.56e-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: 38.08  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     2 KEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMqqlyATLESREE 77
Cdd:TIGR04523 452 KELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI----SSLKEKIE 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360    78 QLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE-------LAM 148
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeIEE 607

                         170
                  ....*....|..
gi 46276360   149 AKQSLATLTKDV 160
Cdd:TIGR04523 608 KEKKISSLEKEL 619
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-161 8.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 8.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360  44 LQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREkwELRRQAKEATD 123
Cdd:COG4717  70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAELPE 146

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46276360 124 HATALRSQLDL---KDNRMKELEAELAMAKQSLATLTKDVP 161
Cdd:COG4717 147 RLEELEERLEElreLEEELEELEAELAELQEELEELLEQLS 187
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 21-158 9.57e-03

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: 37.85  E-value: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46276360     21 LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESR-------EEQLRDFIRNYEQHRKES 93
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESEraarnkaEKQRRDLGEELEALKTEL 308

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46276360     94 EDAVKALAKEKDL---LEREKWELRRQAKEATDHATALRSQLDLKDNR-MKELEAELAMAKQSLATLTK 158
Cdd:pfam01576  309 EDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQEMRQKHTQaLEELTEQLEQAKRNKANLEK 377
 
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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