NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119120918|ref|NP_997194|]
View 

BICD family-like cargo adapter 1 isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 94-334 1.05e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918    94 SQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESD 173
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   174 VKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM----------QVHALREDFREKNSSTNQ 243
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrledleeQIEELSEDIESLAAEIEE 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   244 HIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQv 323
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942

                          250
                   ....*....|.
gi 119120918   324 kvEELTEERSL 334
Cdd:TIGR02168  943 --ERLSEEYSL 951
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-531 2.37e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   235 REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEV 314
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   315 RLSCRQLQVKVEELTEERSLQSSA-ATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY----------CQVRYLCSHLR 383
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltlLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   384 GNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSED-KE 462
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRE 905

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918   463 PKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 531
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-334 1.05e-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: 68.16  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918    94 SQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESD 173
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   174 VKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM----------QVHALREDFREKNSSTNQ 243
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrledleeQIEELSEDIESLAAEIEE 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   244 HIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQv 323
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942

                          250
                   ....*....|.
gi 119120918   324 kvEELTEERSL 334
Cdd:TIGR02168  943 --ERLSEEYSL 951
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-347 3.26e-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: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELE 182
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 183 RQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQ---HIIRLESLQAEIKMLS 259
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 260 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAA 339
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500


                 ....*...
gi 119120918 340 TSTSLLSE 347
Cdd:COG1196  501 ADYEGFLE 508
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 105-315 6.93e-08

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: 54.26  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849  77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEVERQLSMQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQQMAELSEELARKMEENLRQ 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119120918  238 NSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLELQEVR 315
Cdd:pfam04849 237 QEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEELKELR 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-531 2.37e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   235 REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEV 314
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   315 RLSCRQLQVKVEELTEERSLQSSA-ATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY----------CQVRYLCSHLR 383
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltlLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   384 GNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSED-KE 462
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRE 905

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918   463 PKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 531
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
131-347 3.09e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 131 YEQMHKELTDKLEHLEQEKHELRRRFENRE---GEWEGR---VSELESDVKQLQD---ELERQQIHLREADREKSRAVQE 201
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevlEEHEERreeLETLEAEIEDLREtiaETEREREELAEEVRDLRERLEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 202 LSEQNQRLLDQL-------SRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDR-------KRELEH 267
Cdd:PRK02224 291 LEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERaeelreeAAELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 268 RLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAATSTSLLS 346
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlRTARERVEEAEALLE 450


                 .
gi 119120918 347 E 347
Cdd:PRK02224 451 A 451
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-334 1.05e-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: 68.16  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918    94 SQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELESD 173
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   174 VKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSM----------QVHALREDFREKNSSTNQ 243
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrledleeQIEELSEDIESLAAEIEE 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   244 HIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQv 323
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942

                          250
                   ....*....|.
gi 119120918   324 kvEELTEERSL 334
Cdd:TIGR02168  943 --ERLSEEYSL 951
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 118-333 6.02e-11

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: 65.47  E-value: 6.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   118 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELERQQIHLREADRE 194
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   195 KSRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALREDFREKNSSTNQHIIR-----LESLQAEIKMLSDRKRELEHRL 269
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKL 821

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119120918   270 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 333
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-347 3.26e-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: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELE 182
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 183 RQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQ---HIIRLESLQAEIKMLS 259
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 260 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAA 339
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500


                 ....*...
gi 119120918 340 TSTSLLSE 347
Cdd:COG1196  501 ADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-344 4.47e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.77  E-value: 4.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   103 IRQKEKDLvLAARLG--KALLERNQDMSRQYEQMHKELTD-------KLEHLEQEKHELRRRFENREGEWE---GRVSEL 170
Cdd:TIGR02168  222 LRELELAL-LVLRLEelREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYalaNEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   171 ESDVKQLQ-----------------DELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALRED 233
Cdd:TIGR02168  301 EQQKQILRerlanlerqleeleaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   234 FREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK---DLQLHQSQLE 310
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeleELQEELERLE 460

                          250       260       270
                   ....*....|....*....|....*....|....
gi 119120918   311 LQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 344
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-372 6.61e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  99 LLSVIRQKEKDLVLAarlgKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFE---NREGEWEGRVSELESDV- 174
Cdd:COG1196  230 LLLKLRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDIa 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 175 --KQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQ 252
Cdd:COG1196  306 rlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 253 AEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEER 332
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 119120918 333 -SLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY 372
Cdd:COG1196  466 aELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-478 6.68e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 6.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   120 LLERNQDMSRQYEQMhKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRaV 199
Cdd:TIGR02168  672 ILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-I 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   200 QELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLL 279
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   280 QGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEER--------SLQSSAATSTSLLSEIEQS 351
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasleealaLLRSELEELSEELRELESK 909

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   352 MEAEELEQEREQLRLQLWEAYCQV-RYLCSHLRGNDSADSAVstdsSMDESSETSSAKDVPAGSLRTALNELKRLIQSIv 430
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSL----TLEEAEALENKIEDDEEEARRRLKRLENKIKEL- 984

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 119120918   431 dgmePTVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRDEAI 478
Cdd:TIGR02168  985 ----GPVNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEIDREA 1030
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 105-315 6.93e-08

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: 54.26  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  105 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRR---------------FENREGEWEGRVSE 169
Cdd:pfam04849  77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKddllqiysndaeeseTESSCSTPLRRNES 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  170 LESDVKQLQDELERQQIHLREADREKSRA--------VQELSEQNQRLL----DQLSRASEVERQLSMQVHALREDFREK 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLRGLEEENLKLRSeashlkteTDTYEEKEQQLMsdcvEQLSEANQQMAELSEELARKMEENLRQ 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119120918  238 NSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLELQEVR 315
Cdd:pfam04849 237 QEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEELKELR 307
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-328 1.77e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  129 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  208 RLLDQL----SRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDL----L 279
Cdd:COG4913   338 DRLEQLereiERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdL 417

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 119120918  280 QGTVEELQDRVLILERQGHDKDLQLHQSQLELqevrlsCRQLQVKVEEL 328
Cdd:COG4913   418 RRELRELEAEIASLERRKSNIPARLLALRDAL------AEALGLDEAEL 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-531 2.37e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   235 REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEV 314
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   315 RLSCRQLQVKVEELTEERSLQSSA-ATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY----------CQVRYLCSHLR 383
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltlLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   384 GNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSED-KE 462
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRE 905

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918   463 PKEQLQKAIRDRDEAIAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 531
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-333 5.31e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  139 TDKLEHLEQEKHELRRRFEnregEWEGRVSELESDVKQLQDELER-QQIHLREADREKSRAVQELSEQNQRLLDQLSRAS 217
Cdd:COG4913   609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  218 EVERQLSMQVHALREdfreknsstnqhiiRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQG 297
Cdd:COG4913   685 DDLAALEEQLEELEA--------------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119120918  298 HDKDLQLHQSQLELQEVRlscRQLQVKVEELTEERS 333
Cdd:COG4913   751 LEERFAAALGDAVERELR---ENLEERIDALRARLN 783
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-344 5.91e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   121 LERNQD-MSRQYE--QMHKELTDKLEHLE--------QEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLR 189
Cdd:TIGR02168  198 LERQLKsLERQAEkaERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   190 EADREKSRAVQELSEQNQRLLD---QLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELE 266
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119120918   267 HRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSL 344
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-333 8.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 8.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918    98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   178 QDELERQQIHLREADREKSRAVQELSEQnQRLLDQLSRASEVERqlsMQVHALREDFREKNSSTNQHIIRLESLQAEIKM 257
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEELEREIEEER---KRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918   258 LSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQL---HQSQLELQEVRLScrqLQVKVEELTEERS 333
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKED---KALEIKKQEWKLE 458
COG5022 COG5022
Myosin heavy chain [General function prediction only];
118-348 1.13e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 51.62  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  118 KALLERNQDMSRQYEQMHKELTDKLEHLEQE-KHELRRRFENREgewegRVSELESDV-----KQLQDELERQQIHLREA 191
Cdd:COG5022   816 LACIIKLQKTIKREKKLRETEEVEFSLKAEVlIQKFGRSLKAKK-----RFSLLKKETiylqsAQRVELAERQLQELKID 890

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  192 DREksraVQELSEQNQRLLdqlSRASEVERQLSmqvhalrEDFREKNSSTNQHIIRLESL--QAEIKMLSDRKRELEHRL 269
Cdd:COG5022   891 VKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPEL 956

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  270 SATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATSTSLLS 346
Cdd:COG5022   957 NKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIIS 1036


                  ..
gi 119120918  347 EI 348
Cdd:COG5022  1037 SE 1038
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-477 4.70e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 137 ELTDKLEHLEQEK------HELRRRFENREGEWegRVSELEsdvkQLQDELERQQIHLREADREKSRAVQELSEQNQRLl 210
Cdd:COG1196  197 ELERQLEPLERQAekaeryRELKEELKELEAEL--LLLKLR----ELEAELEELEAELEELEAELEELEAELAELEAEL- 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 211 dqlsraseveRQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENdllqgtvEELQDRV 290
Cdd:COG1196  270 ----------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL-------AELEEEL 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 291 LILERQGHDKDLQLHQSQLELQEVRLScrQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWE 370
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 371 AycqvrylcsHLRGNDSADSAVSTDSsmDESSETSSAKDVPAGSLRTALNELKRLIQSIVDGMEPTVTLLSVEMTALKEE 450
Cdd:COG1196  411 A---------LLERLERLEEELEELE--EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                        330       340
                 ....*....|....*....|....*..
gi 119120918 451 RDRLRvTSEDKEPKEQLQKAIRDRDEA 477
Cdd:COG1196  480 AELLE-ELAEAAARLLLLLEAEADYEG 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-315 8.79e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 8.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  98 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQL 177
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 178 QDE----LERQQ--IHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESL 251
Cdd:COG1196  368 LEAeaelAEAEEelEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119120918 252 QAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVR 315
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
136-296 1.06e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 136 KELTDKLEHLEQEKHELRRRFENREgEWEGRVSELESDVKQLQDELER--QQIHLREADREKSRAVQELSEQNQRL---- 209
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLeele 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 210 --LDQLSRASEVERQLSMQVHALREDF-REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEEL 286
Cdd:COG4717  153 erLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                        170
                 ....*....|
gi 119120918 287 QDRVLILERQ 296
Cdd:COG4717  233 ENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-331 1.46e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  108 KDLVLAARLGKALLERNQDMSRQYEQMHKELTD---KLEHLEQ--EKHELRRRFENREGEWEGRVSELESDVKQLQDELE 182
Cdd:COG4913   214 REYMLEEPDTFEAADALVEHFDDLERAHEALEDareQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  183 RQQIhlREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmqvhalredfrekNSSTNqhiiRLESLQAEIKMLSDRK 262
Cdd:COG4913   294 EAEL--EELRAELARLEAELERLEARLDALREELDELEAQIR-------------GNGGD----RLEQLEREIERLEREL 354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119120918  263 RELEH---RLSATLEENDL-LQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 331
Cdd:COG4913   355 EERERrraRLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 134-327 1.73e-05

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: 46.46  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 134 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLldql 213
Cdd:COG1579    2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 214 sraSEVERQLsMQVHALREdfreknsstnqhiirLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 293
Cdd:COG1579   76 ---KKYEEQL-GNVRNNKE---------------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119120918 294 ERQGHDK----DLQLHQSQLELQEVRLSCRQLQVKVEE 327
Cdd:COG1579  137 EAELEEKkaelDEELAELEAELEELEAEREELAAKIPP 174
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
131-347 3.09e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 131 YEQMHKELTDKLEHLEQEKHELRRRFENRE---GEWEGR---VSELESDVKQLQD---ELERQQIHLREADREKSRAVQE 201
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevlEEHEERreeLETLEAEIEDLREtiaETEREREELAEEVRDLRERLEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 202 LSEQNQRLLDQL-------SRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDR-------KRELEH 267
Cdd:PRK02224 291 LEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERaeelreeAAELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 268 RLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAATSTSLLS 346
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlRTARERVEEAEALLE 450


                 .
gi 119120918 347 E 347
Cdd:PRK02224 451 A 451
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 95-351 3.09e-05

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: 47.02  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKEL-TDKLEHLEQEKHELRRRFENREgewegrvseLESD 173
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCDKLLLENKE---------LTQE 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  174 VKQLQDELERQQihlreadreksRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLE---- 249
Cdd:pfam05483 508 ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEenar 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  250 SLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELT 329
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEII 656

                         250       260
                  ....*....|....*....|....
gi 119120918  330 E--ERSLQSSAATSTSLLSEIEQS 351
Cdd:pfam05483 657 DnyQKEIEDKKISEEKLLEEVEKA 680
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 127-339 4.00e-05

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: 46.65  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   127 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELEsdvkqlqdeleRQQIHLREADREKSRAVQELSEQN 206
Cdd:pfam15921  588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLE-----------LEKVKLVNAGSERLRAVKDIKQER 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   207 QRLLDQLSRASEVERQLSMQVHALREDFREKN----SSTNQHIIRLESLQAEIKMLSDRKRELE--------------HR 268
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqKQ 735

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119120918   269 LSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEEL-TEERSLQSSAA 339
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLrSQERRLKEKVA 807
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 112-296 4.19e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   112 LAARLGKALLERN--QDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELESDVKQLQDELERQQI 186
Cdd:TIGR02169  817 IEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDfreknSSTNQHIIRLESLQAEIKMLSDRKRELE 266
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-----EEIPEEELSLEDVQAELQRVEEEIRALE 971

                          170       180       190
                   ....*....|....*....|....*....|
gi 119120918   267 HRLSATLEENDLLQGTVEELQDRVLILERQ 296
Cdd:TIGR02169  972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 108-341 4.44e-05

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: 46.04  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  108 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELER---Q 184
Cdd:pfam07888  28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  185 QIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRE 264
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119120918  265 LEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE-RSLQSSAATS 341
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLNAS 249
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 98-296 1.21e-04

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: 45.12  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   98 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 167
Cdd:pfam05557  52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  168 SELESDVKQLQDELERQQIHLREAdrekSRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalrEDFREKNSSTNQHIIR 247
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 119120918  248 LESLQAEIKmlsdRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 296
Cdd:pfam05557 199 IPELEKELE----RLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 125-331 1.28e-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: 45.04  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   125 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAvqelsE 204
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   205 QNQRLLDQLSRASEVERQLSMQV---HALREDFREKNSSTNQHIIRLES--LQAEIKMLSDRKRELEHRLSATLEENDLL 279
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELN 848

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119120918   280 QGTVEELQDRVLILErqghDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 331
Cdd:TIGR00606  849 RKLIQDQQEQIQHLK----SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-288 3.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 136 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELES------DVKQLQDELERQQIHLREADREKSRAVQELSEQ 205
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 206 NQRLLDQLSRASEVERQLSMQVHA-LREDFREKNSstnqhiiRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVE 284
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711


                 ....
gi 119120918 285 ELQD 288
Cdd:PRK03918 712 ELEK 715
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 170-349 3.20e-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: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   170 LESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmqvhALREDFREKNSSTNQHIIRLE 249
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   250 SLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqgHDKDLQLHQSQLELQEVRLSCRQLQVKVEELt 329
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREI- 817

                          170       180
                   ....*....|....*....|
gi 119120918   330 eERSLQSSAATSTSLLSEIE 349
Cdd:TIGR02169  818 -EQKLNRLTLEKEYLEKEIQ 836
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-275 4.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  111 VLAARLGKALLERNQDmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEG----RVSELESDVKQLQDELERQQI 186
Cdd:COG4913   283 LWFAQRRLELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERER 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  187 HLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELE 266
Cdd:COG4913   360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439


                  ....*....
gi 119120918  267 HRLSATLEE 275
Cdd:COG4913   440 ARLLALRDA 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-493 4.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 121 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 201 EL-SEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLL 279
Cdd:COG4717  235 ELeAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 280 QGTVEELQDrvlILERQGHDKDLQLHQSQLELQEVRlSCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQ 359
Cdd:COG4717  315 ELEEEELEE---LLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 360 EREQLRLQLWEAycQVRYLCSHLRGNDSADSAVSTDSSMDEssetssakdvpagsLRTALNELKRLIQSIVDgmeptvtl 439
Cdd:COG4717  391 LEQAEEYQELKE--ELEELEEQLEELLGELEELLEALDEEE--------------LEEELEELEEELEELEE-------- 446

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119120918 440 lsvEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCRM 493
Cdd:COG4717  447 ---ELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 168-354 6.10e-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: 42.44  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 168 SELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSmqvhALREDFREKNSSTNQHIIR 247
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 248 LESLQAEIK--MLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCR--QLQV 323
Cdd:COG4942   99 LEAQKEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraELEA 178

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119120918 324 KVEELTEER-SLQSSAATSTSLLSEIEQSMEA 354
Cdd:COG4942  179 LLAELEEERaALEALKAERQKLLARLEKELAE 210
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-300 8.79e-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: 42.35  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   104 RQKEKDLVLAARLGKALLERNQDMSRQYEQmHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQDELER 183
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEE 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   184 QQIHLREADREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIR-----LESLQaEIKML 258
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnLAAIE-EYEEL 998

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 119120918   259 SDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK 300
Cdd:TIGR02168  999 KERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQ 1040
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 131-350 9.67e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  131 YEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELESDVKQLQDELERQQIHLREADREksraVQELSEQNQRLL 210
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQN------------------NQLKDNIEKKQQEINEKTTEISNTQTQ----LNQLKDEQNKIK 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  211 DQLSR-ASEVER------QLSMQVHALREDFREKNSSTNQHIIRleSLQAEIKMLSDRKRELEHRLSATLEENDLLQGTV 283
Cdd:TIGR04523 267 KQLSEkQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119120918  284 EELQDRVLILERQGHDKDLQLHQSQLELQEVRlscRQLQVKVEELTeerSLQSSaatSTSLLSEIEQ 350
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLK---KENQSYKQEIK---NLESQ---INDLESKIQN 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-296 9.99e-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: 42.35  E-value: 9.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918    95 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELrrrfenregewEGRVSELESDV 174
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-----------SEDIESLAAEI 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   175 KQLQDELERQQIHLREADREKSravqELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAE 254
Cdd:TIGR02168  862 EELEELIEELESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 119120918   255 IKMLSDRKRELEHRLSATLEEN-DLLQGTVEELQDRVLILERQ 296
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENK 980
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-333 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 103 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEwegrVSELESDVKQLQDELE 182
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 183 RQQIHLREAdREKSRAVQELSEQNQRLLdQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRK 262
Cdd:PRK03918 270 ELKKEIEEL-EEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119120918 263 RELEHRLsatleendllqgtvEELQDRVLILER----QGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERS 333
Cdd:PRK03918 348 KELEKRL--------------EELEERHELYEEakakKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 142-518 1.01e-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: 42.03  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   142 LEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIH---LREADREKSRAVQELSEQNQRLLDQLSRASE 218
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   219 VERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRK------------RELEHRLSATLEEND----LLQGT 282
Cdd:pfam15921  160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSLGSAISKILRELDteisYLKGR 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   283 VEELQDRVLILERQGHDK-DLQLHQSQLELQEVrlsCRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSmeaeeleqer 361
Cdd:pfam15921  240 IFPVEDQLEALKSESQNKiELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---------- 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   362 eqlrlqlweaycQVRYLCS-HLRGNDSADSAVStdssmdessetssakdvpagSLRTALNELKRLIQSIVDGMEPTVTLL 440
Cdd:pfam15921  307 ------------QARNQNSmYMRQLSDLESTVS--------------------QLRSELREAKRMYEDKIEELEKQLVLA 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   441 SVEMTALKEERDRLrvTSEDKEPKEQLQKAIRDRDEAiAKKNAVELELAKCRMDMMSLNSQLLDAIQQKLNLS----QQL 516
Cdd:pfam15921  355 NSELTEARTERDQF--SQESGNLDDQLQKLLADLHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevQRL 431


                   ..
gi 119120918   517 EA 518
Cdd:pfam15921  432 EA 433
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
130-349 1.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 130 QYEQMHKELTDKLEHLEQEKHELRRRFENREG--EWEGRVSELESDVKQLQDELERQqihlREADREKSRAVQELSEQNQ 207
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 208 RLLDQLSRASEVERQLSMQVHALREDF------REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQG 281
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVaelnskLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRE 627

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918 282 TVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLScrQLQVKVEELTEER-SLQSSAATSTSLLSEIE 349
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--QVEEKLDELREERdDLQAEIGAVENELEELE 694
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 118-331 1.80e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEW---EGRVSELESDVKQLQDELERQQihlreadre 194
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIralEQELAALEAELAELEKEIAELR--------- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 195 ksravQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLE 274
Cdd:COG4942   97 -----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119120918 275 ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEE 331
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 118-353 2.43e-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: 40.80  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   118 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRrfenregewegRVSELESDVKQLQDELERQQIHLREADREKsr 197
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ-----------EKTELLVEQGRLQLQADRHQEHIRARDSLI-- 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   198 avqeLSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLE-EN 276
Cdd:TIGR00606  371 ----QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIElKK 446

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119120918   277 DLLQGTVEELQDRVLILER-QGHDKDLQLHQSQLELQEVRLSCRQLQVKVE-ELTEERSLQSSAATSTSLLSEIEQSME 353
Cdd:TIGR00606  447 EILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQEME 525
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 121-485 2.63e-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: 40.86  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  121 LERNQDMSRQYEQMHKElTDKLEHLEQEKHELRRRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQ 200
Cdd:pfam05483  70 FENSEGLSRLYSKLYKE-AEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  201 ELSEQNQ---RLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKmlsDRKRELEHRLSatlEEND 277
Cdd:pfam05483 149 ENNATRHlcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAE---NARLEMHFKLK---EDHE 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  278 LLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEERSLQSSAATS--------TSLLSEIE 349
Cdd:pfam05483 223 KIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEliekkdhlTKELEDIK 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  350 QSME-AEELEQEREQLRLQLWEAYCQVrylcshlrgndsadsAVSTDSSMDESSETSSAKDVPAGSLRT---ALNELKRL 425
Cdd:pfam05483 303 MSLQrSMSTQKALEEDLQIATKTICQL---------------TEEKEAQMEELNKAKAAHSFVVTEFEAttcSLEELLRT 367

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119120918  426 IQSIVDGMEPTVTLLSVEMTALKEERDRLRVTSEDKEPK-EQLQKAIRDRDEAIAKKNAVE 485
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEKKQFE 428
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 120-354 3.47e-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: 40.49  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   120 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELESDVKQLQDELerqqihl 188
Cdd:pfam15921  261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALREDFREKNSSTNQHIIRLESLQAEIKMLSDR------- 261
Cdd:pfam15921  334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsit 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918   262 ----KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSCRQLQVKVEELTEER-S 333
Cdd:pfam15921  414 idhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKmT 490

                          250       260
                   ....*....|....*....|....
gi 119120918   334 LQSSAATSTSL---LSEIEQSMEA 354
Cdd:pfam15921  491 LESSERTVSDLtasLQEKERAIEA 514
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 129-285 3.59e-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: 40.32  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  129 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQ 207
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  208 RLLDQLSRASEVERQLSMQVHALRE-------DFREKNSSTNQHIIRLESLQAEIKmlSDRKRELEHRLSatlEENDLLQ 280
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQErarqqqeEFRRKLQELQRKKQQEEAERAEAE--KQRQKELEMQLA---EEQKRLM 469


                  ....*
gi 119120918  281 GTVEE 285
Cdd:pfam15709 470 EMAEE 474
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
114-294 4.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 114 ARLGKALLERNQDMsRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEG--RVSELESDVKQLQDELERQQIHL 188
Cdd:PRK03918 241 EELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRL 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 189 READREKSRAVQELSEQNQRLLDQLSRASEVERQLSM--QVHALREDFREKNSSTNQHIIRL-----ESLQAEIKMLSDR 261
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119120918 262 KRELEHRLSATLEENDLLQGTVEELQDRVLILE 294
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELK 432
PRK11281 PRK11281
mechanosensitive channel MscK;
122-345 4.22e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  122 ERNQDMSRQYEQMHKELTDKLEHLE----QEKHELRRRFENREgewegrVSELESDVKQLQDELERQQIHLREADrekSR 197
Cdd:PRK11281   80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTLS------LRQLESRLAQTLDQLQNAQNDLAEYN---SQ 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  198 AV--QELSEQNQRLLDQ-LSRASEVERQLsmqvhalredfreKNSSTNQHIIRLES---LQAEIKMLsDRKRELEHRLsa 271
Cdd:PRK11281  151 LVslQTQPERAQAALYAnSQRLQQIRNLL-------------KGGKVGGKALRPSQrvlLQAEQALL-NAQNDLQRKS-- 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119120918  272 tLEENDLLQGTVEELQDrvLILERQGhdkdlQLHQSQLELQEVrLSCRQLQVKVEELTEERSLQSSAATSTSLL 345
Cdd:PRK11281  215 -LEGNTQLQDLLQKQRD--YLTARIQ-----RLEHQLQLLQEA-INSKRLTLSEKTVQEAQSQDEAARIQANPL 279
mreC TIGR00219
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape ...
 167-295 4.84e-03

rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped. Cells defective in MreC are round. Species with MreC include many of the Proteobacteria, Gram-positives, and spirochetes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 129323 [Multi-domain]  Cd Length: 283  Bit Score: 39.07  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918  167 VSELESDVKQLQDELERQQIHLREADREKSRAVQELSEQNQRLLDQL-SRASEVERQLSMQVHALREDFREKNSSTNQ-- 243
Cdd:TIGR00219  61 ISENLKDVNNLEYENYKLRQELLKKNQQLEILTQNLKQENVRLRELLnSPLSSDEYKISAEVIYLNYDNYSTQVVINKgf 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119120918  244 -------------------HIIRLESLQAEIKMLSDRkrelEHRLSATLEEND---LLQGTVEELQDRVLILER 295
Cdd:TIGR00219 141 ndgvykdmpviadgkglvgKVVSVGSNTSRVLLLTDY----TNFVPAQILRSDfrgLIEGNGYGKTLEMNLVNR 210
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 129-290 7.11e-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: 38.37  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 129 RQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEG---RVSELESDVKQLQDELERQQIHLREAdrEKSRAVQELSEQ 205
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQKE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120918 206 NQRLLDQLSRASEVERQLSMQVHALREDFREKNSstnqhiiRLESLQAEikmLSDRKRELEHRLSATLEENDLLQGTVEE 285
Cdd:COG1579   98 IESLKRRISDLEDEILELMERIEELEEELAELEA-------ELAELEAE---LEEKKAELDEELAELEAELEELEAEREE 167


                 ....*
gi 119120918 286 LQDRV 290
Cdd:COG1579  168 LAAKI 172
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH