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Conserved domains on  [gi|578824469|ref|XP_006719760|]
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BICD family-like cargo adapter 1 isoform X7 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
98-409 7.51e-13

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 71.24  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469    98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   332 L--TEERSLQSSAATSTSLLSEIEQSMEAEELEQERE-QVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRD 406
Cdd:TIGR02168  948 EysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEID 1027

                   ...
gi 578824469   407 EAI 409
Cdd:TIGR02168 1028 REA 1030
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
98-409 7.51e-13

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: 71.24  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469    98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   332 L--TEERSLQSSAATSTSLLSEIEQSMEAEELEQERE-QVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRD 406
Cdd:TIGR02168  948 EysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEID 1027

                   ...
gi 578824469   407 EAI 409
Cdd:TIGR02168 1028 REA 1030
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-420 2.88e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 135 HKELTDKLEHLEQEKHELRRR-FENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1196  215 YRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVERQLSMQvHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG1196  295 AELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 294 VLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS-LQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS 372
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578824469 373 VEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELA 420
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
95-448 5.93e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.42  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 333
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  334 E--ERSLQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS-----VEMTALKEERdrlrvtsedkepKEQLQKAIRDRD 406
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiAEMVALMEKH------------KHQYDKIIEERD 724
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578824469  407 -----------EAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLE 448
Cdd:pfam05483 725 selglyknkeqEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
118-408 3.88e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTD----------KLEHLEQEKHELRRRFENREGEWEGRVSELESdvkqLQDELERqqIH 187
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEareavedrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERDE--LR 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 188 LREADREKS-RAVQELSEQNQRLLDQ---------------LSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESL 251
Cdd:PRK02224 426 EREAELEATlRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDL 504
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 252 qAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469 332 LTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQvTLLSVEMTALKEERDRLRvTSEDKEPKEQLQKAIRDRDEA 408
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKRERKR-ELEAEFDEARIEEAREDKERA 658
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
98-409 7.51e-13

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: 71.24  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469    98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQL 177
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIEEL 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   178 QDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM------QVHALREDFREKNSSTNQHIIRLESL 251
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrleDLEEQIEELSEDIESLAAEIEELEEL 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   332 L--TEERSLQSSAATSTSLLSEIEQSMEAEELEQERE-QVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRD 406
Cdd:TIGR02168  948 EysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEID 1027

                   ...
gi 578824469   407 EAI 409
Cdd:TIGR02168 1028 REA 1030
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
164-462 2.50e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 66.23  E-value: 2.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   164 EGRVSELESDVKQLQDELerqqihlreadreksravQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQ 243
Cdd:TIGR02168  683 EEKIEELEEKIAELEKAL------------------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   244 HIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRL 320
Cdd:TIGR02168  745 LEERIAQLSKELTeleAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   321 SCRQLQVKVEELTEE-RSLQSSAATSTSLLSEIEQSMEAEELEQE--REQVTLLSVEMTALKEERDRLR-----VTSEDK 392
Cdd:TIGR02168  825 RLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEelESELEALLNERASLEEALALLRseleeLSEELR 904
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   393 EPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 462
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-420 2.88e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 135 HKELTDKLEHLEQEKHELRRR-FENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1196  215 YRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVERQLSMQvHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG1196  295 AELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 294 VLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS-LQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS 372
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578824469 373 VEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELA 420
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
103-339 2.23e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRF---ENREGEWEGRVSELESDVKQLQD 179
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 180 ELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEI 259
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQ 339
Cdd:COG1196  396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
118-337 3.71e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.31  E-value: 3.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   118 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   195 KSRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALREDFREKNSSTNQHIIR-LESLQAEQVLEIKMLSDRKRELEHRL 273
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKL 821
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824469   274 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
100-351 4.28e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 100 LSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQD 179
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEE 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 180 ELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVhalredfreknsstnQHIIRLESLQAEQVLEI 259
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA---------------AQLEELEEAEEALLERL 416
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQ 339
Cdd:COG1196  417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
                        250
                 ....*....|..
gi 578824469 340 SSAATSTSLLSE 351
Cdd:COG1196  497 LEAEADYEGFLE 508
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
136-457 5.66e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 5.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   136 KELTDKLEHLEQEKH------ELRRRFENREG-EWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQR 208
Cdd:TIGR02169  194 DEKRQQLERLRREREkaeryqALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   209 LldqlsraseveRQLSMQVHALRED----FREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQ 284
Cdd:TIGR02169  274 L-----------EELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   285 GTVEELQdrvlilerqghdkdLQLHQSQLELQEVRLSCRQLQVKVEEltEERSLQSSAATSTSLLSEIEQsmeaeeleqe 364
Cdd:TIGR02169  343 REIEEER--------------KRRDKLTEEYAELKEELEDLRAELEE--VDKEFAETRDELKDYREKLEK---------- 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   365 reqvtlLSVEMTALKEERDRL-----RVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQ 439
Cdd:TIGR02169  397 ------LKREINELKRELDRLqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
                          330
                   ....*....|....*...
gi 578824469   440 KLNLSQQLEAWQDDMHRV 457
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-416 1.39e-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: 54.29  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESdVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA-LANEISRLEQQKQILRERLANLERQLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   201 ELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREknsstnqhiirLESLQAEQVLEIKMLSDRKRELEHRLsatleen 280
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELES-----------LEAELEELEAELEELESRLEELEEQL------- 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   281 dllqgtvEELQDRVLILERQghdkdLQLHQSQLELQEVRLScrQLQVKVEELTEERSLQSSAATSTSlLSEIEQSMEAEE 360
Cdd:TIGR02168  382 -------ETLRSKVAQLELQ-----IASLNNEIERLEARLE--RLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELE 446
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578824469   361 LEQEREQVTLLSVEmTALKEERDRLRvtsedkEPKEQLQKAIRDRDEAIAKKNAVE 416
Cdd:TIGR02168  447 EELEELQEELERLE-EALEELREELE------EAEQALDAAERELAQLQARLDSLE 495
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-332 2.82e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  129 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  208 RLLDQLSRaseverqlsmQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTV 287
Cdd:COG4913   338 DRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578824469  288 EELQDRVLILERQGHD-----KDLQLHQSQL--ELQEVRLS-CRQLQVKVEEL 332
Cdd:COG4913   408 AEAEAALRDLRRELREleaeiASLERRKSNIpaRLLALRDAlAEALGLDEAEL 460
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
95-448 5.93e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.42  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQA 253
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 333
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  334 E--ERSLQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLS-----VEMTALKEERdrlrvtsedkepKEQLQKAIRDRD 406
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiAEMVALMEKH------------KHQYDKIIEERD 724
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578824469  407 -----------EAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLE 448
Cdd:pfam05483 725 selglyknkeqEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
118-297 2.84e-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: 50.06  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELESDVKQLQDELERQQIHLREADREKSR 197
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----TLRSKVAQLELQIASLNNEIERLEARLER 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   198 AVQELSEQNQRLLDQLSRASEVERQ-LSMQVHALREDFREKNSSTNQHIIRLESLQaEQVLEIKMLSDRKRELEHRLSAT 276
Cdd:TIGR02168  412 LEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQAR 490
                          170       180
                   ....*....|....*....|.
gi 578824469   277 LEENDLLQGTVEELQDRVLIL 297
Cdd:TIGR02168  491 LDSLERLQENLEGFSEGVKAL 511
COG5022 COG5022
Myosin heavy chain [General function prediction only];
168-352 4.46e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 49.69  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  168 SELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLLdqlSRASEVERQLSmqvhalrEDFREKNSSTNQHIIR 247
Cdd:COG5022   867 ETIYLQSAQRVELAERQLQELKIDVKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIAR 932
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  248 LESLQAEqvLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSCRQ 324
Cdd:COG5022   933 LKKLLNN--IDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGA 1010
                         170       180
                  ....*....|....*....|....*...
gi 578824469  325 LQVKVEELTEERSLQSSAATSTSLLSEI 352
Cdd:COG5022  1011 LQESTKQLKELPVEVAELQSASKIISSE 1038
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
105-319 5.96e-06

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 48.10  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849  77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEverqlsmQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQ-------QMAELSEELARK 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  238 NSSTNQHIIRLESLQAEQV---LEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLE 314
Cdd:pfam04849 230 MEENLRQQEEITSLLAQIVdlqHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEE 302

                  ....*
gi 578824469  315 LQEVR 319
Cdd:pfam04849 303 LKELR 307
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
118-408 3.88e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTD----------KLEHLEQEKHELRRRFENREGEWEGRVSELESdvkqLQDELERqqIH 187
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEareavedrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERDE--LR 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 188 LREADREKS-RAVQELSEQNQRLLDQ---------------LSRASEVERQLSmQVHALREDFREKNSSTNQHIIRLESL 251
Cdd:PRK02224 426 EREAELEATlRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDL 504
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 252 qAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEE 331
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469 332 LTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQvTLLSVEMTALKEERDRLRvTSEDKEPKEQLQKAIRDRDEA 408
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKRERKR-ELEAEFDEARIEEAREDKERA 658
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
98-319 4.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  98 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 178 QDE----LERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhALREDFREKNSSTNQHIIRLESLQA 253
Cdd:COG1196  368 LEAeaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALE 445
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824469 254 EQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVR 319
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-337 5.68e-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: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  139 TDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELER-QQIHLREADREKSRAVQELSEQNQRLLDQLSRAS 217
Cdd:COG4913   609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  218 EVERQLSMQVHALREDFREknsstnqhiirleslqAEQvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 297
Cdd:COG4913   685 DDLAALEEQLEELEAELEE----------------LEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578824469  298 ERQGHDKDLQLHQSQLELQEVRlscRQLQVKVEELTEERS 337
Cdd:COG4913   747 LRALLEERFAAALGDAVERELR---ENLEERIDALRARLN 783
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
125-472 1.71e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   125 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAvqelsE 204
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   205 QNQRLLDQLSRASEVERQLSMQV---HALREDFREKNSSTNQHIIRLESLQAEqvLEIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGSDLD--RTVQQVNQEKQEKQHELDTVVSKIE 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   282 LLQGTVEELQDRVLILERQGHD---KDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEA 358
Cdd:TIGR00606  847 LNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   359 EELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQ--LQKAIRDRDEAIAKKNAvelELAKCRMDMMSLNSQlLDA 436
Cdd:TIGR00606  927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgKDDYLKQKETELNTVNA---QLEECEKHQEKINED-MRL 1002
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 578824469   437 IQQKLNLSQQLEAW-QDDMHRVIDRQLMDTHLKERSQ 472
Cdd:TIGR00606 1003 MRQDIDTQKIQERWlQDNLTLRKRENELKEVEEELKQ 1039
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-452 2.22e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   155 RFENREGEWEGRVSELESDVKQLQD---ELERQQIHLrEADREKSRAVQELSEQnqrlldqlsrasevERQLSMQVHALR 231
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDilnELERQLKSL-ERQAEKAERYKELKAE--------------LRELELALLVLR 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   232 -EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQ 310
Cdd:TIGR02168  234 lEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   311 SQLELQEVRLSCRQLQVKVEELTEErsLQSSAATSTSLLSEIEQ-----SMEAEELEQEREQVTLLSVEMTALKEERDRL 385
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469   386 RVT--------SEDKEPKEQLQKAIRDRDEAIAK--KNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQD 452
Cdd:TIGR02168  392 ELQiaslnneiERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
118-424 2.64e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELE--RQQIHLREADREK 195
Cdd:COG4717  159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEelEEELEQLENELEA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 196 SRAVQELSEQNQRLL-------------DQLSRASEVE--RQLSMQVHALREDFREKNSSTNQHII-RLESLQAEQVLEI 259
Cdd:COG4717  239 AALEERLKEARLLLLiaaallallglggSLLSLILTIAgvLFLVLGLLALLFLLLAREKASLGKEAeELQALPALEELEE 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 260 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDrvLILERQGHDKDLQLHQSQLELQEVRLSC---------------RQ 324
Cdd:COG4717  319 EELEELLAALGLPPDLSPEELLELLDRIEELQE--LLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaleqaEE 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 325 LQVKVEELTE-ERSLQSSAATSTSLLSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIR 403
Cdd:COG4717  397 YQELKEELEElEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
                        330       340
                 ....*....|....*....|.
gi 578824469 404 DRDEAIAKKNAVELELAKCRM 424
Cdd:COG4717  477 ELEELKAELRELAEEWAALKL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
170-452 2.68e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   170 LESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmqvhALREDFREKNSSTNQHIIRLE 249
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   250 SLQAeqvlEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqgHDKDLQLHQSQLELQEVRLSCRQLQVKV 329
Cdd:TIGR02169  741 ELEE----DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   330 EELteERSLQSSAATSTSLLSEIEQSMEAEEL-----EQEREQVTLLSVEMTALKEERDRLRVTSEDKEpkEQLQKAIRD 404
Cdd:TIGR02169  815 REI--EQKLNRLTLEKEYLEKEIQELQEQRIDlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLE--SRLGDLKKE 890
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 578824469   405 RDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQD 452
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
153-456 3.50e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   153 RRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASE----VERQLSMQVH 228
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsqedLRNQLQNTVH 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   229 ------ALREDFREkNSSTNQHIIRLESLQAEQVL-EIKML-------SDRK------------RELEHRLSATLEEND- 281
Cdd:pfam15921  153 eleaakCLKEDMLE-DSNTQIEQLRKMMLSHEGVLqEIRSIlvdfeeaSGKKiyehdsmstmhfRSLGSAISKILRELDt 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   282 ---LLQGTVEELQDRVLILERQGHDK-DLQLHQSQLELQEVrlsCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSME 357
Cdd:pfam15921  232 eisYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   358 AEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKepkeqlqkaIRDRDEAIAKKNAvELELAKCRMDMMSlnsqlldai 437
Cdd:pfam15921  309 RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---------IEELEKQLVLANS-ELTEARTERDQFS--------- 369
                          330
                   ....*....|....*....
gi 578824469   438 QQKLNLSQQLEAWQDDMHR 456
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHK 388
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
121-300 5.73e-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: 42.06  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---FENREGEWEGRVSELESDVKQLQDELERQQIHLRE------- 190
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 191 ---ADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKR 267
Cdd:COG4942  116 lgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
                        170       180       190
                 ....*....|....*....|....*....|...
gi 578824469 268 ELEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:COG4942  196 ERQKLLARLEKELAELAAELAELQQEAEELEAL 228
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-453 8.75e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 201 ELSE-QNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEE 279
Cdd:COG4717  228 ELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 280 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRlSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAE 359
Cdd:COG4717  308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 360 ELEQEREQVtllsvEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEaiakknaVELELAKCRMDMMSLNSQLLDAIQQ 439
Cdd:COG4717  387 LRAALEQAE-----EYQELKEELEELEEQLEELLGELEELLEALDEEE-------LEEELEELEEELEELEEELEELREE 454
                        330
                 ....*....|....
gi 578824469 440 KLNLSQQLEAWQDD 453
Cdd:COG4717  455 LAELEAELEQLEED 468
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
127-254 9.14e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 9.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   127 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELEsdvkqlqdeleRQQIHLREADREKSRAVQELSEQN 206
Cdd:pfam15921  588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLE-----------LEKVKLVNAGSERLRAVKDIKQER 655
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578824469   207 QRLLDQLSRASEVERQLSMQVHALREDFREKN----SSTNQHIIRLESLQAE 254
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSE 707
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
118-300 9.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 9.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGE---WEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   195 KSRAVQELSEQNQRLLDQLSRASEVERQLS------MQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRE 268
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
                          170       180       190
                   ....*....|....*....|....*....|..
gi 578824469   269 LEHRLSATLEENDLLQGTVEELQDRVLILERQ 300
Cdd:TIGR02169  460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-449 1.08e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   258 EIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEER- 336
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELt 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   337 -------SLQSSAATSTSLLSEIEQSMEAEELE--QEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQ--------LQ 399
Cdd:TIGR02168  758 eleaeieELEERLEEAEEELAEAEAEIEELEAQieQLKEELKALREALDELRAELTLLNEEAANLRERLEslerriaaTE 837
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 578824469   400 KAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEA 449
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
247-462 1.12e-03

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: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 247 RLESL--QAEQVLEIKMLSDRKRELEHRLsaTLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQ 324
Cdd:COG1196  201 QLEPLerQAEKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 325 LQVKVEELTEERSLQSSAatstslLSEIEQsmeaeeleqereqvtllsvEMTALKEERDRLRVTSEDKEpkEQLQKAIRD 404
Cdd:COG1196  279 LELELEEAQAEEYELLAE------LARLEQ-------------------DIARLEERRRELEERLEELE--EELAELEEE 331
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469 405 RDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 462
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-282 1.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELES------DVKQLQDELERQQIHLREADREKSRAVQELSEQ 205
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469 206 NQRLLDQLSRASEVERQLSMQVHA-LREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDL 282
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
136-315 1.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELER--QQIHLREADREKSRAVQELSEQNQRLlDQL 213
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERL-EEL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVERQLSMQVHALREDFREKNSSTNQHiirLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDR 293
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                        170       180
                 ....*....|....*....|..
gi 578824469 294 VLILERQGHDKDLQLHQSQLEL 315
Cdd:COG4717  229 LEQLENELEAAALEERLKEARL 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
112-224 2.43e-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: 40.82  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   112 LAARLGKALLERN--QDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELESDVKQLQDELERQQI 186
Cdd:TIGR02169  817 IEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 578824469   187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLS 224
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
136-413 3.09e-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: 40.39  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELERQQIHLREADREKsravQELSEQNQRLLDQLSR 215
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK----ELLEKEIERLKETIIK 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  216 ASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAE-----------------QVLEIKMLSDRKRELEHRLSATLE 278
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnleqkqkelksKEKELKKLNEEKKELEEKVKDLTK 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  279 ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRL--SCRQLQVKVEELTEE-RSLQSSAATSTSLLSEIEQS 355
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekEIDEKNKEIEELKQTqKSLKKKQEEKQELIDQKEKE 597
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469  356 MEAEELEQEREQVTLLSV--EMTALKEERDRL----RVTSEDKEPKEQLQKAIRDR-DEAIAKKN 413
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLekELEKAKKENEKLssiiKNIKSKKNKLKQEVKQIKETiKEIRNKWP 662
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
168-386 3.18e-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: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 168 SELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQ----------LSMQVHALREDFREK 237
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaleaelaeLEKEIAELRAELEAQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 238 NSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLsatleenDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQE 317
Cdd:COG4942  103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRAD--LAELAALRAELEAER 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824469 318 VRLScrqlQVKVEELTEERSLQSSAATSTSLLSEIEQsmeaeeleqereQVTLLSVEMTALKEERDRLR 386
Cdd:COG4942  174 AELE----ALLAELEEERAALEALKAERQKLLARLEK------------ELAELAAELAELQQEAEELE 226
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
129-289 3.20e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  129 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  208 RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLE-SLQAEQVLEIKMLSDRKRELEHRLSatlEENDLLQGT 286
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQLA---EEQKRLMEM 471

                  ...
gi 578824469  287 VEE 289
Cdd:pfam15709 472 AEE 474
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
98-300 3.73e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.11  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 167
Cdd:pfam05557  52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  168 SELESDVKQLQDELERQQIHLREAdrekSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalrEDFREKNSSTNQHIIR 247
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578824469  248 LESLQAEQvleikmlsDRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 300
Cdd:pfam05557 199 IPELEKEL--------ERLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
108-345 4.47e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  108 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELER---Q 184
Cdd:pfam07888  28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  185 QIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNqhiiRLESLQAEQVLEIKMLSD 264
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE----RMKERAKKAGAQRKEEEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  265 RKRELEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAA 343
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLN 247

                  ..
gi 578824469  344 TS 345
Cdd:pfam07888 248 AS 249
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
134-293 4.65e-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: 38.75  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 134 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL 213
Cdd:COG1579    2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 214 SRASEVE-----RQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVE 288
Cdd:COG1579   80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159

                 ....*
gi 578824469 289 ELQDR 293
Cdd:COG1579  160 ELEAE 164
PTZ00121 PTZ00121
MAEBL; Provisional
121-418 4.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  121 LERNQDMSRQYEQMHK--ELTDKLEHLEQEKHELRRRFENREGEWEGRVSElesDVKQLQDELERQQIHLREADREKSRA 198
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADEAKKAAEAKKKA 1512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  199 VQELSEQNQRLLDQLSRASEVERQlsmqvhalrEDFREKNSSTNQHIIRlESLQAEQVLEIKMLSDRKRELEHRLSATLE 278
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKA---------DEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  279 ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLElqevrlscrqlQVKVEELTEERSLQSSAatsTSLLSEIEQSMEA 358
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-----------KIKAEELKKAEEEKKKV---EQLKKKEAEEKKK 1648
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  359 EELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELE 418
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
118-337 5.07e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 118 KALLERNQDMSRQYEQMHKELTDKLEH---LEQEKHELRRRFENREGEWEgRVSELESDVKQLQDELERQQIHLR---EA 191
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRkleEK 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469 192 DREKSRAVQELSEQNQRLLDQLSRASEVER--QLSMQVHALREDFREKNSSTNQHIIRLESLQA---EQVLEIKMLSDRK 266
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEkaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieERIKELEEKEERL 340
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469 267 RELEHRLSATLEENDLLQGTVEELQD-RVLILERQGHDK---DLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 337
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKrltGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
174-354 5.28e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  174 VKQLQDELERQQIHlrEADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQ--VHALREDFREKNSSTNQHIIRLESL 251
Cdd:COG3096   481 VCKIAGEVERSQAW--QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQqnAERLLEEFCQRIGQQLDAAEELEEL 558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  252 QAEQVLEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLI-------LERQGHdkdlQLHQSQLELQEVrLSCRQ 324
Cdd:COG3096   559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaaqdaLERLRE----QSGEALADSQEV-TAAMQ 633
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578824469  325 LQVKVE-ELTEERSLqsSAATSTSLLSEIEQ 354
Cdd:COG3096   634 QLLERErEATVERDE--LAARKQALESQIER 662
PRK11281 PRK11281
mechanosensitive channel MscK;
122-349 5.47e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  122 ERNQDMSRQYEQMHKELTDKLEHLE----QEKHELRRRFENREgewegrVSELESDVKQLQDELERQQIHLREADrekSR 197
Cdd:PRK11281   80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTLS------LRQLESRLAQTLDQLQNAQNDLAEYN---SQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  198 AV--QELSEQNQRLLDQ-LSRASEVERQLsmqvhalredfreKNSSTNQHIIRLES---LQAEQVLEIKMLSDRKRELEH 271
Cdd:PRK11281  151 LVslQTQPERAQAALYAnSQRLQQIRNLL-------------KGGKVGGKALRPSQrvlLQAEQALLNAQNDLQRKSLEG 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824469  272 rlSATLEenDLLQGTVEELQDRVLILERQghdkdLQLhqsqleLQEVrLSCRQLQVKVEELTEERSLQSSAATSTSLL 349
Cdd:PRK11281  218 --NTQLQ--DLLQKQRDYLTARIQRLEHQ-----LQL------LQEA-INSKRLTLSEKTVQEAQSQDEAARIQANPL 279
PTZ00121 PTZ00121
MAEBL; Provisional
118-418 5.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEK---HELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADR- 193
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEl 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  194 ---EKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLES--LQAEQVLEIKMLSDRKRE 268
Cdd:PTZ00121 1558 kkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQ 1637
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  269 LEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 348
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824469  349 LSEIEQSmeaeeleqerEQVTLLSVEMTALKEERDR-----LRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELE 418
Cdd:PTZ00121 1718 AEELKKA----------EEENKIKAEEAKKEAEEDKkkaeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
118-467 6.40e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.26  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRfenregewegrVSELESDVKQLQDELERQQIHLREADREKsr 197
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE-----------KTELLVEQGRLQLQADRHQEHIRARDSLI-- 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   198 avqeLSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSatl 277
Cdd:TIGR00606  371 ----QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE--- 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   278 EENDLLQGTVEELQDRVLILER-QGHDKDLQLHQSQLELQEVRLSCRQLQVKVE-ELTEERSLQSSAATSTSLLSEIEQS 355
Cdd:TIGR00606  444 LKKEILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQE 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   356 MEAEELEQEREQVTLLSVEMTALKEER---------DRLRVTSEDKEPKEQLQKAIRDRDEaiaKKNAVELELAKCRMDM 426
Cdd:TIGR00606  524 MEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrhsDELTSLLGYFPNKKQLEDWLHSKSK---EINQTRDRLAKLNKEL 600
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 578824469   427 MSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHL 467
Cdd:TIGR00606  601 ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL 641
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
131-493 7.63e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   131 YEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRV------SELESDVKQLQDELERQQIHLREADREKSRAVQE--- 201
Cdd:pfam12128  417 LQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVERLQSElrq 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   202 -----------LSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLES------------LQAEQVLE 258
Cdd:pfam12128  497 arkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISpellhrtdldpeVWDGSVGG 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   259 IKMLSDRKRELEHrlsatLEENDLLQGTvEELQDRVLILErqghdKDLQLHQSQLELQEVRLScrQLQVKVEELTEERSL 338
Cdd:pfam12128  577 ELNLYGVKLDLKR-----IDVPEWAASE-EELRERLDKAE-----EALQSAREKQAAAEEQLV--QANGELEKASREETF 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   339 QSSAATSTSL----LSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLrvtseDKEPKEQLQKAIRDRDEAIAKKNA 414
Cdd:pfam12128  644 ARTALKNARLdlrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL-----DKKHQAWLEEQKEQKREARTEKQA 718
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   415 VELELAKCRMDMMSLNSQLLDAIQQklNLSQQLEAWQDDMHRVIDRQLMD-THLKERSQPAAALCRGHSAGRGDEPSIAE 493
Cdd:pfam12128  719 YWQVVEGALDAQLALLKAAIAARRS--GAKAELKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
120-405 7.65e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   120 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELESDVKQLQDELerqqihl 188
Cdd:pfam15921  261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLeSLQAEQVleiKMLSDR--- 265
Cdd:pfam15921  334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQN---KRLWDRdtg 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469   266 --------KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTE 334
Cdd:pfam15921  410 nsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA 486
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824469   335 ER-SLQSSAATSTSL---LSEIEQSMEAEELE--QEREQVTLLSVEMTALKEERDRLRVTSEDKEPKeQLQKAIRDR 405
Cdd:pfam15921  487 KKmTLESSERTVSDLtasLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-KLQMAEKDK 562
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
129-421 7.76e-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: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  129 RQYEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELESDVKQLQDELERQQIHLREADREKSRAVQE---LSEQ 205
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKEL------------------TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknLESQ 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  206 NQRLLDQLSRASEVERQLSMQVHALR----------EDFREKNSSTNQHIIRLESLQAEQVLEIKMLSDRKRELEHRLSA 275
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQqekellekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  276 TLEENDLLQGTVEELQDRVLILERQghDKDLQLHQSQLELQEVRLSCRQ--LQVKVEELTEERSLQSSAAtsTSLLSEIE 353
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKE--LKKLNEEKKELEEKVKDLTKKIssLKEKIEKLESEKKEKESKI--SDLEDELN 548
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824469  354 QSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPK-EQLQKAIRDRDEAIAKKNAVELELAK 421
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELiDQKEKEKKDLIKEIEEKEKKISSLEK 617
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
131-447 8.38e-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: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  131 YEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLL 210
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQN------------------NQLKDNIEKKQQEINEKTTEISNTQTQ----LNQLKDEQNKIK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  211 DQLSR-ASEVERQlsmqvhalREDFREKNSSTNQHIIRLESL--QAEQVL------EIKMLSDRKRELEHRLSATLEEND 281
Cdd:TIGR04523 267 KQLSEkQKELEQN--------NKKIKELEKQLNQLKSEISDLnnQKEQDWnkelksELKNQEKKLEEIQNQISQNNKIIS 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  282 LLQGTVEELQDRVLILERQGHDKDLQLHQSQLEL-------QEVRLSCRQLQVKVEELteERSLQSSAATSTSLLSEIEQ 354
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkkenQSYKQEIKNLESQINDL--ESKIQNQEKLNQQKDEQIKK 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  355 smEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKE--------PKEQLQKAIRDRDEAIakkNAVELELAKCRMDM 426
Cdd:TIGR04523 417 --LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiknldnTRESLETQLKVLSRSI---NKIKQNLEQKQKEL 491
                         330       340
                  ....*....|....*....|.
gi 578824469  427 MSLNSQLLDAIQQKLNLSQQL 447
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKV 512
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
120-483 8.41e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  120 LLERNQDMSRQYEQMHK-------ELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVK---QLQDELERQQIHLR 189
Cdd:pfam05483 262 LLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKticQLTEEKEAQMEELN 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  190 EADREKSRAVQELSEQ----NQRLLDQLSRASEVERQL---SMQVHALREDFREKNSSTNQHIIRLESLQAEQVLEIKML 262
Cdd:pfam05483 342 KAKAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLkiiTMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  263 SDRKrelehRLSATLEEndlLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVeeltEERSLQSSA 342
Cdd:pfam05483 422 DEKK-----QFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL----EKEKLKNIE 489
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824469  343 ATSTSLLSEIEQSMEAEELEQEREQVTLLSVEMTALKEERDRLRVTSEDKEPKEQlqkAIRDRDEAIAKKNAVELELAKC 422
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM---NLRDELESVREEFIQKGDEVKC 566
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578824469  423 RMDMMSLNSQLLD-AIQQKLNLSQQLEAWQDDMHRVIDRQlmDTHLKERSQPAAALCRGHSA 483
Cdd:pfam05483 567 KLDKSEENARSIEyEVLKKEKQMKILENKCNNLKKQIENK--NKNIEELHQENKALKKKGSA 626
 
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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