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Conserved domains on  [gi|2462506714|ref|XP_054191387|]
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kazrin isoform X11 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

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]; ...
 73-359 3.07e-10

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: 62.65  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  73 TEKETLKSSMILMRHLLMDAQ-AKILSMMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAA 151
Cdd:COG1196   220 EELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 152 ASASaagdsaatnmENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELAR 231
Cdd:COG1196   300 LEQD----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 232 AKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAK 311
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462506714 312 EATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLA 359
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 73-359 3.07e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  73 TEKETLKSSMILMRHLLMDAQ-AKILSMMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAA 151
Cdd:COG1196   220 EELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 152 ASASaagdsaatnmENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELAR 231
Cdd:COG1196   300 LEQD----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 232 AKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAK 311
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462506714 312 EATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLA 359
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-350 1.62e-07

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: 53.92  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 248
Cdd:TIGR02169  693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  249 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 320
Cdd:TIGR02169  773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462506714  321 RSQLDLKDNRMKELEAELAMAKQSLATLTK 350
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLES 882
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
176-338 3.01e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 252
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 253 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 322
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 2462506714 323 QLDLKDNRMKELEAEL 338
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 176-360 1.02e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 253
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 254 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 330
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462506714 331 MKELEAELAMAKQSLATLTKDVPKRHSLAM 360
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 73-359 3.07e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  73 TEKETLKSSMILMRHLLMDAQ-AKILSMMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAA 151
Cdd:COG1196   220 EELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 152 ASASaagdsaatnmENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELAR 231
Cdd:COG1196   300 LEQD----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 232 AKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAK 311
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462506714 312 EATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLA 359
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 110-343 4.94e-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: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 110 IDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQL----GAQVLLREEVSRLQE 185
Cdd:COG1196   265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleEELEELEEELEELEE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 186 EVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLE 265
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506714 266 SREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQ 343
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-350 1.62e-07

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: 53.92  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 248
Cdd:TIGR02169  693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  249 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 320
Cdd:TIGR02169  773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462506714  321 RSQLDLKDNRMKELEAELAMAKQSLATLTK 350
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLES 882
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-350 1.75e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  111 DGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQvllREEVSRLQEEVHLL 190
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  191 RQMKEMLAKDLEESQGGKSS-------EVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL---VSQMQQL 260
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEEleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  261 YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATD-------HATALRSQLDLKDNRMKE 333
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleeALALLRSELEELSEELRE 905

                          250
                   ....*....|....*..
gi 2462506714  334 LEAELAMAKQSLATLTK 350
Cdd:TIGR02168  906 LESKRSELRRELEELRE 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
176-352 1.82e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQMKEmLAKDLEESQGGKssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvs 255
Cdd:COG4913    240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  256 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 335
Cdd:COG4913    315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170
                   ....*....|....*..
gi 2462506714  336 AELAMAKQSLATLTKDV 352
Cdd:COG4913    387 AEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-352 6.97e-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: 51.98  E-value: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  217 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 293
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506714  294 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-341 7.44e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 7.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  175 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDL 253
Cdd:COG4913    292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  254 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 333
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                   ....*...
gi 2462506714  334 LEAELAMA 341
Cdd:COG4913    445 LRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-352 1.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSA--------------TELRVQLAQKEQELARAKEALQAMKA 241
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleeriaqlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  242 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 314
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462506714  315 ---DHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 74-295 1.57e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  74 EKETLKSSMILMRHLLMDAQAKILSMMEDNKQLALRIDgavqSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAAS 153
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 154 ASAAGDSAATNMENPQLGAQVLLR-EEVSRLQEEVHLLRQMKEMLAKDLEESQggkssevlsatELRVQLAQKEQELARA 232
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506714 233 KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 295
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 217-351 1.69e-06

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: 49.15  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 217 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 296
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462506714 297 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 351
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 190-354 1.78e-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: 49.76  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 190 LRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREE 269
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 270 QLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD 328
Cdd:COG4942   105 ELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                         170       180
                  ....*....|....*....|....*.
gi 2462506714 329 NRMKELEAELAMAKQSLATLTKDVPK 354
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAE 210
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
176-348 1.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS----EVLSATELRV-----QLAQKEQELARAKEA---LQAMKADR 243
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  244 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 323
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770

                          170       180
                   ....*....|....*....|....*
gi 2462506714  324 LdlkDNRMKELEAELAMAKQSLATL 348
Cdd:COG4913    771 L---EERIDALRARLNRAEEELERA 792
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
176-338 3.01e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 252
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 253 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 322
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 2462506714 323 QLDLKDNRMKELEAEL 338
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-353 7.72e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 7.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 255
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  256 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKELE 335
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKELQ 439

                          170
                   ....*....|....*...
gi 2462506714  336 AELAMAKQSLATLTKDVP 353
Cdd:TIGR02168  440 AELEELEEELEELQEELE 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
219-352 2.22e-05

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: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  219 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 298
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462506714  299 LErekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:COG4913    687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
175-350 2.99e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 175 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQ----GGK----------SSEVLSATELRVQLAQKEQELARAKEALQAMK 240
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 241 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAL 320
Cdd:PRK02224  496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462506714 321 RSQLDLKDNRMKELEAELAMAKQSLATLTK 350
Cdd:PRK02224  564 EEEAEEAREEVAELNSKLAELKERIESLER 593
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-312 4.14e-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: 4.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  100 MEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATnmenpqlgaqVLLREE 179
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----------EELSED 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  180 VSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 259
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462506714  260 LYATLESREEQLR-DFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKE 312
Cdd:TIGR02168  934 LEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEE----ARRRLKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 74-347 7.22e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  74 EKETLKSSMILMRHLLMDAQAKILSMMEDNKQLALRIDGAVQ---SASQEVTNLRAELTATNRRLAELSGGGGPGPGPGA 150
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 151 AASASAAGDSAATNMENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELA 230
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 231 RAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELR 307
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAA 535

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462506714 308 RQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLAT 347
Cdd:COG1196   536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-323 8.08e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  115 QSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLlREEVSRLQEEVHLLRqmk 194
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-EREIAELEAELERLD--- 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  195 emlakdleesqggKSSEVLsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 274
Cdd:COG4913    682 -------------ASSDDL--AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462506714  275 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 323
Cdd:COG4913    747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 176-360 1.02e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 253
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 254 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 330
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462506714 331 MKELEAELAMAKQSLATLTKDVPKRHSLAM 360
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
172-319 1.31e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  172 AQVLLREEVSRLQEEVHLLRQMKEMLAKDLEE------SQGGKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADR 243
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  244 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 316
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                   ...
gi 2462506714  317 ATA 319
Cdd:COG4913    456 DEA 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-352 1.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 217 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 296
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462506714 297 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 221-312 1.49e-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: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 221 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 300
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90
                  ....*....|..
gi 2462506714 301 REKWELRRQAKE 312
Cdd:COG4942    97 AELEAQKEELAE 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
178-349 2.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 178 EEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 257
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 258 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM--KELE 335
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                         170
                  ....*....|....
gi 2462506714 336 AELAMAKQSLATLT 349
Cdd:COG4717   243 ERLKEARLLLLIAA 256
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
176-347 2.41e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVS 255
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 256 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALR 321
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                         170       180
                  ....*....|....*....|....*.
gi 2462506714 322 SQLDLKDNRMKELEAELAMAKQSLAT 347
Cdd:PRK02224  356 ERAEELREEAAELESELEEAREAVED 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-353 2.69e-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: 43.52  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  176 LREEVSRLQEEVHLLRQMKEMLAKDleesqggkssevlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 255
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  256 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 335
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 2462506714  336 AELAMAKQSLATLTKDVP 353
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
216-352 4.88e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 216 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDavkalake 295
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506714 296 kdlLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:COG4372   120 ---LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 181-355 5.53e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 181 SRLQEEVHLLRQMKEMLAkDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKT 251
Cdd:COG1579    17 SELDRLEHRLKELPAELA-ELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 252 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRM 331
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEEL 151

                         170       180
                  ....*....|....*....|....
gi 2462506714 332 KELEAELAMAKQSLATLTKDVPKR 355
Cdd:COG1579   152 AELEAELEELEAEREELAAKIPPE 175
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
201-352 7.85e-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: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 201 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 274
Cdd:COG3206   162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506714 275 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 352
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 61-353 8.97e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 8.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714   61 KALEEDKDpFLPTEKETLKSSMILMRHLLMDAQAKILSMMEDNKQLALRIDGAV----------QSASQEVTNLRAELTA 130
Cdd:TIGR02169  684 EGLKRELS-SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  131 TNRRLAELSGGGGPGPGPGAAASASAAGDSAatnmenPQLGAQV-LLREEVSRLqeevhllrqmkEMLAKDLEESqggks 209
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELsKLEEEVSRI-----------EARLREIEQK----- 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  210 sevLSATELRVQLAQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQLRDfirnyeqhrkeseda 288
Cdd:TIGR02169  821 ---LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRD--------------- 879

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506714  289 vkaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 353
Cdd:TIGR02169  880 ---LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
PTZ00121 PTZ00121
MAEBL; Provisional
 172-354 9.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  172 AQVLLREEVSRLQEEVHLLRQMKEMLAKDL--EESQGGKSSEVLSATELRVQLAQ----------------KEQELARAK 233
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQlkkkeaeekkkaeelkKAEEENKIK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  234 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 310
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462506714  311 KEATDHATALRSQLDLKdNRMKELEAELAMAKQSLATLTKDVPK 354
Cdd:PTZ00121  1740 EEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIE 1782
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
176-346 1.09e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 255
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 256 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKEL 334
Cdd:COG4372   137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

                         170
                  ....*....|..
gi 2462506714 335 EAELAMAKQSLA 346
Cdd:COG4372   217 AEELLEAKDSLE 228
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 218-353 1.25e-03

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: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 218 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 297
Cdd:COG0542   402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506714 298 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 353
Cdd:COG0542   460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 197-348 1.48e-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: 41.11  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  197 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlYATLESREEQLRDFIR 276
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQE 366

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462506714  277 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 348
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
PTZ00121 PTZ00121
MAEBL; Provisional
 172-337 1.89e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  172 AQVLLREEVSRLQEEVHLLRQMKEmlAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT 251
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  252 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREKW---ELRRQAKEATDHATALRSQLD--L 326
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaK 1702

                          170
                   ....*....|.
gi 2462506714  327 KDNRMKELEAE 337
Cdd:PTZ00121  1703 KAEELKKKEAE 1713
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
176-340 2.23e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSatELRVQLAQKEQELARAKEALQ----AMKADRKRLKGEKT 251
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 252 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKeatdhatALRSQLDLKDNRM 331
Cdd:COG3206   306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-------VARELYESLLQRL 374


                  ....*....
gi 2462506714 332 KELEAELAM 340
Cdd:COG3206   375 EEARLAEAL 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-284 2.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  92 AQAKILSMMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENpQLG 171
Cdd:COG1196   633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE-LAE 711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 172 AQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQA-----MKADR--K 244
Cdd:COG1196   712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnLLAIEeyE 791

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462506714 245 RLKGEKTDLVSQmqqlYATLESREEQLRDFIRNYEQHRKE 284
Cdd:COG1196   792 ELEERYDFLSEQ----REDLEEARETLEEAIEEIDRETRE 827
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
177-338 2.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 177 REEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVlSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ 256
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 257 MQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHATALRSQLDLK 327
Cdd:PRK02224  553 AEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRERLAEK 632

                         170
                  ....*....|.
gi 2462506714 328 DNRMKELEAEL 338
Cdd:PRK02224  633 RERKRELEAEF 643
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 215-441 3.28e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 215 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIR-NYEQHR----------- 282
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaLYRSGGsvsyldvllgs 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 283 ------------------------KESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAEL 338
Cdd:COG3883   112 esfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 339 AMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPS 416
Cdd:COG3883   192 AAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271

                         250       260
                  ....*....|....*....|....*
gi 2462506714 417 VISDASAAEGDRSSTPSDINSPRHR 441
Cdd:COG3883   272 AGAGAAAASAAGGGAGGAGGGGGGG 296
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 106-353 3.29e-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: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 106 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAqvlLREEVSRLQE 185
Cdd:COG4942     7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 186 EVHLLRQMKEMLAKDLEEsQGGKSSEVLSATElRVQLAQKEQELARAKEALQAMKAdRKRLKgektDLVSQMQQLYATLE 265
Cdd:COG4942    84 ELAELEKEIAELRAELEA-QKEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRR-LQYLK----YLAPARREQAEELR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 266 SREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 345
Cdd:COG4942   157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236


                  ....*...
gi 2462506714 346 ATLTKDVP 353
Cdd:COG4942   237 AAAAERTP 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 217-375 4.93e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 217 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 295
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 296 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 373
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570


                  ..
gi 2462506714 374 VQ 375
Cdd:TIGR04523 571 EE 572
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 191-351 5.54e-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: 39.39  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  191 RQMKEMLAKDlEESQGGKSSEVLSATELRvQLAQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 270
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714  271 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 350
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152


                   .
gi 2462506714  351 D 351
Cdd:pfam01576  153 E 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
176-342 5.78e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 255
Cdd:PRK02224  291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 256 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATDHATALRSQLDLKDNRMKELE 335
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAE 446


                  ....*..
gi 2462506714 336 AELAMAK 342
Cdd:PRK02224  447 ALLEAGK 453
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
221-342 6.61e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 221 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 300
Cdd:COG2268   238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462506714 301 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 342
Cdd:COG2268   306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 199-350 6.79e-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: 38.85  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 199 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 278
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462506714 279 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 350
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
176-342 7.24e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEEsQGGKSSEVLSATELRVQLAQKEQ-ELARAKEALQAMKADRKRLKGEKTDLV 254
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKELEPFYNEYlELKDAEKELEREEKELKKLEEELDKAF 632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 255 SQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 332
Cdd:PRK03918  633 EELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711

                         170
                  ....*....|.
gi 2462506714 333 ELEA-ELAMAK 342
Cdd:PRK03918  712 ELEKlEKALER 722
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 176-313 8.82e-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: 37.60  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 176 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEAL---------QAMKADRKRL 246
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyEALQKEIESL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462506714 247 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEA 313
Cdd:COG1579   102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 178-273 9.01e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.52  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 178 EEVSRLQEEVHLLRQMKEMLAKDLEESqggkSSEvlSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ- 256
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEA----SFE--RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRy 484

                          90
                  ....*....|....*....
gi 2462506714 257 --MQQLYATLESREEQLRD 273
Cdd:COG0542   485 gkIPELEKELAELEEELAE 503
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 178-352 9.42e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 178 EEVSRLQEEVHllrqMKEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 253
Cdd:TIGR04523 440 SEIKDLTNQDS----VKELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 254 VSQMqqlyATLESREEQLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM 331
Cdd:TIGR04523 516 TKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591

                         170       180
                  ....*....|....*....|....*...
gi 2462506714 332 KELEAE-------LAMAKQSLATLTKDV 352
Cdd:TIGR04523 592 DQKEKEkkdlikeIEEKEKKISSLEKEL 619
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 217-349 9.87e-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: 38.17  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 217 ELRVQLAQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 283
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506714 284 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN----RMKELEAELAMAKQSLATLT 349
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
 
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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