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Conserved domains on  [gi|1034556941|ref|XP_016856260|]
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kazrin isoform X12 [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]; ...
 78-261 9.17e-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: 60.72  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         170       180
                  ....*....|....*....|....
gi 1034556941 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-261 9.17e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         170       180
                  ....*....|....*....|....
gi 1034556941 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-252 2.15e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941    2 MEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNmenpqlgaqvLLREE 81
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------QLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   82 VSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 161
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  162 LYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATD-------HATALRSQLDLKDNRMK 234
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNerasleeALALLRSELEELSEELR 904

                          250
                   ....*....|....*...
gi 1034556941  235 ELEAELAMAKQSLATLTK 252
Cdd:TIGR02168  905 ELESKRSELRRELEELRE 922
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-240 6.12e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 155 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 224
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 1034556941 225 QLDLKDNRMKELEAEL 240
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 78-262 5.19e-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: 45.58  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 155
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 156 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 232
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034556941 233 MKELEAELAMAKQSLATLTKDVPKRHSLAM 262
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-261 9.17e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         170       180
                  ....*....|....*....|....
gi 1034556941 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 12-245 6.90e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  12 IDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQL----GAQVLLREEVSRLQE 87
Cdd:COG1196   265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleEELEELEEELEELEE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  88 EVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLE 167
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556941 168 SREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQ 245
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 77-250 7.87e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQL--------------AQKEQELARAKEALQAMK 142
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 143 ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF---IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHA 219
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034556941 220 TALRSQLDLKDNRMKELEAELAMAKQSLATL 250
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-252 2.15e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941    2 MEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNmenpqlgaqvLLREE 81
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------QLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   82 VSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 161
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  162 LYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATD-------HATALRSQLDLKDNRMK 234
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNerasleeALALLRSELEELSEELR 904

                          250
                   ....*....|....*...
gi 1034556941  235 ELEAELAMAKQSLATLTK 252
Cdd:TIGR02168  905 ELESKRSELRRELEELRE 922
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-252 2.49e-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: 53.15  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 150
Cdd:TIGR02169  693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  151 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 222
Cdd:TIGR02169  773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|
gi 1034556941  223 RSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLES 882
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-254 3.55e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQMKEmLAKDLEESQGGKssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvs 157
Cdd:COG4913    240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  158 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG4913    315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170
                   ....*....|....*..
gi 1034556941  238 AELAMAKQSLATLTKDV 254
Cdd:COG4913    387 AEAAALLEALEEELEAL 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-254 9.25e-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: 51.21  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  119 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 195
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556941  196 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
77-243 1.22e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:COG4913    292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  156 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 235
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                   ....*...
gi 1034556941  236 LEAELAMA 243
Cdd:COG4913    445 LRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-254 1.54e-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: 50.44  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSA--------------TELRVQLAQKEQELARAKEALQAMKA 143
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleeriaqlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  144 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 216
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034556941  217 ---DHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 92-256 2.04e-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: 49.38  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  92 LRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREE 171
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 172 QLRDFIRNYEQHRKESEDAV---------------------KALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD 230
Cdd:COG4942   105 ELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                         170       180
                  ....*....|....*....|....*.
gi 1034556941 231 NRMKELEAELAMAKQSLATLTKDVPK 256
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAE 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-253 2.43e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLR-----QMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEK 152
Cdd:COG1196   218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 153 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLK 229
Cdd:COG1196   298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....
gi 1034556941 230 DNRMKELEAELAMAKQSLATLTKD 253
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQ 401
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 119-253 2.68e-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: 48.38  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 198
Cdd:COG1579    28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034556941 199 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 253
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-250 4.16e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 4.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS----EVLSATELRV-----QLAQKEQELARAKEA---LQAMKADR 145
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  146 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 225
Cdd:COG4913    695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770

                          170       180
                   ....*....|....*....|....*
gi 1034556941  226 LdlkDNRMKELEAELAMAKQSLATL 250
Cdd:COG4913    771 L---EERIDALRARLNRAEEELERA 792
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-240 6.12e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:PRK02224  218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 155 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 224
Cdd:PRK02224  298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                         170
                  ....*....|....*.
gi 1034556941 225 QLDLKDNRMKELEAEL 240
Cdd:PRK02224  378 AVEDRREEIEELEEEI 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-197 7.61e-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: 47.84  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   5 NKQLAlRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLLR-EEVS 83
Cdd:COG4942    54 LKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSpEDFL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  84 RLQEEVHLLRQMKEMLAKDLEESQggkssevlsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLY 163
Cdd:COG4942   133 DAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034556941 164 ATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 197
Cdd:COG4942   202 ARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-255 9.42e-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: 48.13  E-value: 9.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKELE 237
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKELQ 439

                          170
                   ....*....|....*...
gi 1034556941  238 AELAMAKQSLATLTKDVP 255
Cdd:TIGR02168  440 AELEELEEELEELQEELE 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-254 3.88e-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: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  121 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 200
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034556941  201 LErekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4913    687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 78-262 5.19e-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: 45.58  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 155
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 156 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 232
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034556941 233 MKELEAELAMAKQSLATLTKDVPKRHSLAM 262
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
77-252 7.37e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQ----GGK----------SSEVLSATELRVQLAQKEQELARAKEALQAMK 142
Cdd:PRK02224  416 ELREERDELREREAELEATLRTARERVEEAEalleAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 143 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAL 222
Cdd:PRK02224  496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034556941 223 RSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:PRK02224  564 EEEAEEAREEVAELNSKLAELKERIESLER 593
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-225 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 1034556941   17 QSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLlREEVSRLQEEVHLLRqmk 96
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-EREIAELEAELERLD--- 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   97 emlakdleesqggKSSEVLsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 176
Cdd:COG4913    682 -------------ASSDDL--AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034556941  177 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 225
Cdd:COG4913    747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 123-214 1.63e-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: 43.60  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 123 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 202
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90
                  ....*....|..
gi 1034556941 203 REKWELRRQAKE 214
Cdd:COG4942    97 AELEAQKEELAE 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-254 1.86e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 198
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556941 199 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
74-221 2.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   74 AQVLLREEVSRLQEEVHLLRQMKEMLAKDLEE------SQGGKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADR 145
Cdd:COG4913    296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  146 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 218
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                   ...
gi 1034556941  219 ATA 221
Cdd:COG4913    456 DEA 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
80-251 2.40e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  80 EEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQM 159
Cdd:COG4717    88 EEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 160 QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM--KELE 237
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALE 242

                         170
                  ....*....|....
gi 1034556941 238 AELAMAKQSLATLT 251
Cdd:COG4717   243 ERLKEARLLLLIAA 256
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-255 4.32e-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: 42.75  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   78 LREEVSRLQEEVHLLRQMKEMLAKDleesqggkssevlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  158 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 1034556941  238 AELAMAKQSLATLTKDVP 255
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-249 5.77e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALR 223
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                         170       180
                  ....*....|....*....|....*.
gi 1034556941 224 SQLDLKDNRMKELEAELAMAKQSLAT 249
Cdd:PRK02224  356 ERAEELREEAAELESELEEAREAVED 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-249 6.28e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   3 EDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLgaQVLLREEV 82
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  83 SRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL 162
Cdd:COG1196   411 ALLERLERLEEELEELEEALAELEE-----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 163 YATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE 239
Cdd:COG1196   486 LAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565

                         250
                  ....*....|
gi 1034556941 240 LAMAKQSLAT 249
Cdd:COG1196   566 LKAAKAGRAT 575
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
103-254 6.53e-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: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 103 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 176
Cdd:COG3206   162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556941 177 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-250 7.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 117 ATELRVQLAQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 190
Cdd:COG1196   215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556941 191 ----VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 250
Cdd:COG1196   293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-254 7.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 118 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDavkalake 197
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556941 198 kdlLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4372   120 ---LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 83-257 1.05e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  83 SRLQEEVHLLRQMKEMLAkDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKT 153
Cdd:COG1579    17 SELDRLEHRLKELPAELA-ELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 154 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRM 233
Cdd:COG1579    93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEEL 151

                         170       180
                  ....*....|....*....|....
gi 1034556941 234 KELEAELAMAKQSLATLTKDVPKR 257
Cdd:COG1579   152 AELEAELEELEAEREELAAKIPPE 175
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 78-343 1.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKEQELARAKEALQAMKADRKRlKGEKTDLVS 157
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELGERARALYR-SGGSVSYLD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QM--QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 235
Cdd:COG3883   107 VLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 236 LEAELAMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCH 313
Cdd:COG3883   187 LSAEEAAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266

                         250       260       270
                  ....*....|....*....|....*....|
gi 1034556941 314 SRQPSVISDASAAEGDRSSTPSDINSPRHR 343
Cdd:COG3883   267 AAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
PTZ00121 PTZ00121
MAEBL; Provisional
 74-239 1.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   74 AQVLLREEVSRLQEEVHLLRQMKEMLAKDL--EESQGGKSSEVLSATELRVQLAQ----------------KEQELARAK 135
Cdd:PTZ00121  1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQlkkkeaeekkkaeelkKAEEENKIK 1662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  136 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 212
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                          170       180
                   ....*....|....*....|....*..
gi 1034556941  213 KEATDHATALRSQLDLKdNRMKELEAE 239
Cdd:PTZ00121  1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
78-248 1.57e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKEL 236
Cdd:COG4372   137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

                         170
                  ....*....|..
gi 1034556941 237 EAELAMAKQSLA 248
Cdd:COG4372   217 AEELLEAKDSLE 228
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 99-250 1.71e-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: 40.73  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   99 LAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlYATLESREEQLRDFIR 178
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQE 366

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556941  179 NYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 250
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 120-255 1.72e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 120 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 199
Cdd:COG0542   402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556941 200 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 255
Cdd:COG0542   460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
78-242 1.83e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSatELRVQLAQKEQELARAKEALQ----AMKADRKRLKGEKT 153
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 154 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKeatdhatALRSQLDLKDNRM 233
Cdd:COG3206   306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-------VARELYESLLQRL 374


                  ....*....
gi 1034556941 234 KELEAELAM 242
Cdd:COG3206   375 EEARLAEAL 383
PTZ00121 PTZ00121
MAEBL; Provisional
 74-239 2.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   74 AQVLLREEVSRLQEEVHLLRQMKEmlAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT 153
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  154 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEATDHATALRSQLD--L 228
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEeaK 1702

                          170
                   ....*....|.
gi 1034556941  229 KDNRMKELEAE 239
Cdd:PTZ00121  1703 KAEELKKKEAE 1713
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 119-277 3.18e-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: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 197
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 198 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 275
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570


                  ..
gi 1034556941 276 VQ 277
Cdd:TIGR04523 571 EE 572
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-186 3.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   4 DNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENpQLGAQVLLREEVS 83
Cdd:COG1196   643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE-LAEAEEERLEEEL 721

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  84 RLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKA-------DRKRLKGEKTDLV 156
Cdd:COG1196   722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaieEYEELEERYDFLS 801

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034556941 157 SQmqqlYATLESREEQLRDFIRNYEQHRKE 186
Cdd:COG1196   802 EQ----REDLEEARETLEEAIEEIDRETRE 827
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 8-255 3.82e-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: 39.36  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   8 LALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGdsaatnmenpqlgaqvlLREEVSRLQE 87
Cdd:COG4942     7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-----------------LERRIAALAR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  88 EVHLLRQMKEMLAKDLEESQggkssevLSATELRVQLAQKEQELARAKEALQAM-KADRKRLKGEKTD------------ 154
Cdd:COG4942    70 RIRALEQELAALEAELAELE-------KEIAELRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDfldavrrlqylk 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 155 -LVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM 233
Cdd:COG4942   143 yLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                         250       260
                  ....*....|....*....|..
gi 1034556941 234 KELEAELAMAKQSLATLTKDVP 255
Cdd:COG4942   223 EELEALIARLEAEAAAAAERTP 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-252 4.57e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 101 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 180
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556941 181 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 93-253 4.67e-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: 4.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   93 RQMKEMLAKDlEESQGGKSSEVLSATELRvQLAQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 172
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  173 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152


                   .
gi 1034556941  253 D 253
Cdd:pfam01576  153 E 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
79-240 5.31e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  79 REEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVlSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ 158
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 159 MQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHATALRSQLDLK 229
Cdd:PRK02224  553 AEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRERLAEK 632

                         170
                  ....*....|.
gi 1034556941 230 DNRMKELEAEL 240
Cdd:PRK02224  633 RERKRELEAEF 643
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-254 5.44e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  80 EEVSRLQEEVHllrqMKEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:TIGR04523 440 SEIKDLTNQDS----VKELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 156 VSQMqqlyATLESREEQLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM 233
Cdd:TIGR04523 516 TKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591

                         170       180
                  ....*....|....*....|....*...
gi 1034556941 234 KELEAE-------LAMAKQSLATLTKDV 254
Cdd:TIGR04523 592 DQKEKEkkdlikeIEEKEKKISSLEKEL 619
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
123-244 7.53e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 123 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 202
Cdd:COG2268   238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034556941 203 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 244
Cdd:COG2268   306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 78-215 7.81e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 38.58  E-value: 7.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHL---LRQMKEMLAKDLEESQGGKSSEVlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEV--AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAAS 563

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556941 155 L---VSQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEA 215
Cdd:pfam07111 564 LrqeLTQQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEA 639
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-255 9.13e-03

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: 38.51  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   16 VQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAatnmenPQLGAQV-LLREEVSRLqeevhllrq 94
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELsKLEEEVSRI--------- 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941   95 mkEMLAKDLEESqggkssevLSATELRVQLAQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQL 173
Cdd:TIGR02169  811 --EARLREIEQK--------LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAAL 877

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  174 RDfirnyeqhrkesedavkaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 253
Cdd:TIGR02169  878 RD------------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939


                   ..
gi 1034556941  254 VP 255
Cdd:TIGR02169  940 KG 941
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-244 9.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:PRK02224  291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556941 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAE 446


                  ....*..
gi 1034556941 238 AELAMAK 244
Cdd:PRK02224  447 ALLEAGK 453
 
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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